As Seen on TV! Restoring Hair with LASERS!!!!!!

The author’s rapidly-expanding forehead.

Anyone who watches TV, reads magazines, or flips through catalogs has seen some interesting products. Maybe they seem plausible to you, maybe they don’t. However, a little investigation shows they are based less on science and well…actually working, and more on wishful thinking. At worst they’re actual con-jobs, designed to separate you from your money as efficiently as possible (which I guess is a certain standard of success). As a result, we at Double X Science bring you “As Seen on TV!” In these features, we’ll look at some of the products shilled on talk shows and infomercials, items lurking between the articles you read in magazines, or things you might find on the shelves of the stores where you shop.

I admit it, I’m a balding dude. My forehead is gradually taking over my entire scalp, replacing my formerly thick and curly hair with a vast expanse of pink skin. Yes, dear readers: My hair was once so thick and curly that, when I wore it long and in a ponytail, ladies would ask me for my secret. (The answer: Wash it every other day with some brand of cheap shampoo and let it air dry. Don’t tell.) I don’t like the fact of my impending baldness, so I’m sympathetic toward defoliation-sufferers who want to bring their hair back at any cost.

On the other hand, I don’t think I’ll invest in any of the hair restoration products advertised in the SkyMall catalog I picked up on my flight to my brother’s wedding in San Francisco. I counted seven products in this single catalog promising to restore hair in one way or another, either reversing baldness or filling in thin patches on the scalp –- and that doesn’t include hair-coloring, extensions, or other options. I won’t cover all of them, but no fewer than three products pledge to bring hair back through the magic of lasers.

Ah, lasers. They may not have the mystique of magnets or the nous of “natural”, but they are a frequent ingredient in modern snake oil. (Come to think of it, one of the hair-restoration products may have contained snake oil. I don’t want to ask.) But while lasers can help correct nearsightedness in some cases, perform minimally invasive surgeries, and remove hair, color my scalp skeptical about their ability to restore hair.

First, a disclaimer: I’m not a biologist, a doctor, medical researcher, or in any field related to those. I’m a physicist, so the closest I ever get professionally to this topic is the “no-hair” theorem in black hole physics. The “no-hair” theorem says that black holes have very few distinguishing characteristics: only mass and rotational rate (and technically electric charge as well, though it’s hard to build up enough charge to make a difference). The analogy is that, if all humans were completely hairless, we would have a lot fewer ways to tell each other apart. In other words, this ain’t my area, so bear (bare) with me!

Night on Baldhead Mountain

Hair loss can occur for a wide variety of reasons: chemotherapy, a number of unrelated diseases, even stress. However, as humans (both men and women!) age, we all tend to lose our hair to some degree. The effect is most pronounced in male pattern baldness (a bare patch on the top of the head merging over time with the growing forehead to leave a fringe around the edges of the scalp) or female pattern baldness (a general loss of hair at the top of the scalp). However, past the age of 80, nearly everyone starts losing hair, regardless of genetics, diet, or health.

The reasons, as with so many other things, are hormonal. Hair production is governed by sex hormones: most famously testosterone, but also a less well-known cousin known as dihydrotestosterone (DHT). In some people, DHT commands the follicles — the small organs in the skin that produce and feed hair — to shrink, producing ever-finer hair until they cease operating entirely. Thus, gradual hair loss of the usual (as opposed to disease- or circumstance-derived) variety is generally preceded by the hair itself becoming thinner and fuzzier.

My naive understanding of the biology of hair loss leads me to suspect that since hormones are the culprit behind hair loss, then any hair restoration should address those hormones in some way. That alone makes me suspicious of the laser-based products SkyMall peddles. To see why, let’s look at lasers themselves.

Lasers (without sharks)

The word “laser” began as an acronym: Light Amplification by the Stimulated Emission of Radiation. The details could be an Everyday Science or Double Xplainer post in their own right, but here’s the short version. The lasers used in the SkyMall products are LED lasers, meaning they are based on the underlying physics as LED lights. An electric current kicks electrons or other electric charge carriers from one type of material to another across a junction. The excess energy the electric charge sheds during this process is given off in the form of a photon, a particle of light. Since the same amount of energy is involved every time, light from LEDs is nearly monochromatic, meaning it is almost purely one color.

The “amplification” part of the name comes by putting the LED into a special kind of cavity with reflective walls. These walls set up standing waves for the light, which interfere constructively like vibrations in a guitar string, making them brighter. However, unlike guitar strings, the production of the light in lasers is a self-feeding process, resulting in the different parts of the system synchronizing until they emit photons in concert with each other. It’s really interesting stuff, and while it’s somewhat complicated, there’s nothing really mysterious or magical about it, any more than magnets are magical.

In fact, LED lasers are so unmagical that you can buy them as cat toys. LED lasers are the inner workings of laser pointers, which you can buy very inexpensively at any number of shops.

The smell of frying follicles

One of three laser-based hair-restoration products from SkyMall.
This one features built-in headphones, so you can at least listen
to music while you sit around looking like a fool. However,
I recommend a cheaper set of headphones, since the $700
price tag is a bit steep, and you’d get the same result with
regards to hair restoration.
Laser hair removal uses intense lasers to selectively heat the follicles in the skin, hopefully avoiding damage to the rest of the skin. This process can slow down hair growth and cause the hair to fall out of the treated follicles, but it doesn’t always actually stop it: the treatment must be continued for a long term. Basically, the laser is damaging the follicle.

As you can imagine, that also makes me skeptical that lasers can stimulate new hair growth. Lasers produce light…and that’s it! In addition to the usual red lasers like in laser pointers, manufacturers also make infrared lasers, which are useful for surgery. While we perceive infrared as heat (which is why sunshine feels warm), I don’t think merely warming the scalp is going to make hair grow faster, or else you wouldn’t need lasers at all — an electric blanket would do just as well. Too much heating and we’re back at laser hair removal.

Similarly, visible-light lasers like the kind that seem to be in these SkyMall products simply produce red light. Because ordinary light bulbs produce a broad range of colors (white light is a mixture of all the visible-light wavelengths), sitting under a desk lamp would expose your scalp to red light. Yes, it wouldn’t be as intense as lasers, but you could do the same trick with a laser pointer from Schtaples (the Scmoffice Schmupply Schtore), provided you have the patience to hold it against your scalp for long periods of time.

The author engages in home laser hair restoration, while his cats
meow around his feet.
So, to summarize:
  • Hair loss in its most common forms is hormonal, so it’s unclear to me that light (whether laser or otherwise) has anything to do with it. Hair removal can be achieved with lasers, but that involves causing damage to hair follicles, not using anything intrinsic to light.
  • Lasers are simply very monochromatic light sources, that use synchronization of atoms on the microscopic level to do their business. There’s nothing in a laser that isn’t in ordinary light bulbs, though you can make things far more intense with a laser. However, high intensity brings us back to laser hair removal, not restoration.
  • As always, if a product sounds miraculous, it’s probably bunkum. If all it took to regrow hair was a glorified laser pointer, nobody would be bald! LED lasers are cheap and ubiquitous; we could all restore our hair without paying a company $700 (and listen to the music on inexpensive headphones, to boot).
Now if you’ll pardon me, I’ll get back to shining this laser pointer at my scalp.

Historical Physicists

Featured today are 10 more women who broke boundaries by their presence in physics. They lived from 1711 to 2000. While I again limited information to one paragraph, I tried to highlight how they got their start, what universities, family members, and scientists were supportive of them. For these women, without the support of fathers, mothers, husbands, and mentors (all male with one exception) their life in science would not have happened. While barriers are not as difficult today as they were at the times these women made their way, it is a testament to what can be done when families and scientists support each other. These women are an inspiration and I hope you look up more information for them. In addition, I’d love to hear who your favorite women in science are in the comments.

Laura Bassi by Carlo Vandi 
Laura Bassi (1711-78) lectured on science until a few hoursbefore her death. An Italian scientist of international fame and one of the first women physicists in western history, Dr. Bassi earned her doctorate in philosophy and science through public debate from the University of Bologna. The University of Bologna offered Dr. Bassi a position in an effort to be known as a leader in women’s education. Unfortunately, this forward step was not acceptable to much of the rest of the world’s academic community and required stipulations to Dr. Bassi teaching. However, she countered these limitations with determination and passion. Her appointment to full membership in the Bendettini Academics also deterred some naysayers of Dr. Bassi’s involvement in research and teaching. In order to further her career, she married. A married woman could achieve more than a single woman at that time. Her death in 1778 was unexpected, especially as she had participated in an Academy of Sciences lecture on a few hours before.



If you can access the full article, I highly recommend The Desire to Contribute: AnEighteenth-Century Italian Woman of Science by Gabriella Berti Logan for more information on Laura Bassi.
Margaret Eliza Maltby (1860-1944) was a recognized scientistand advocate for women in science. She overcame the education offered to women by taking extra courses in order to attend Oberlin College and receive a B.A. She studied with the Art Students’ League in New York City to explore her interest in art and then taught high school before enrolling as a “special student” at the Massachusetts Institute of Technology (MIT), receiving her B.S. Oberlin recognized this extra effort by awarding Dr. Maltby an M.S. She became a physics instructor at Wellesley College. She was encouraged in her graduate students by an AAUW fellowship to attend Göttingen University, which culminated in Dr. Maltby being the first American woman to receive a Ph.D. in physics from any German university. Dr. Maltby worked as an instructor, a researcher, and administrator in many universities and colleges in the U.S. and abroad. Her stature as a scientist was acknowledged with her entry in the first edition of AmericanMen of Science. She also was active in the AAUW, advocating for women to gain education and enter scientific fields. After her retirement from university life, she maintained her interest in the arts.

Frederic and Irene Joliot-Cure by By James Lebenthal
Irène Joliot-Curie (1897-1956) was a Nobel Prize Laureate for “artificial radioactivity.”  Born to  the woman every person thinks of as the epitome of a woman in science, Marie Curie, Irène had an extremely close relationship with her paternal grandfather. Her schooling was outside of the standard schooling type, her first years at home and her latter years in a science and math heavy co-operative school of Madame Curie’s colleagues. She received her Bachelor’s degree from the Collège Sévigné and went on to study at the Sorbonne. She received her doctorate in 1925 based on work with her mother at the Radium Institute of the Sorbonne. She married Frédéric Joliot, another research assistant of Madame Curie’s. Dr. Joliot-Curie continued her research, interrupted by a stint as Undersecretary of State for Scientific Research, one of the first high government posts to be offered to a woman. She worked as a professor for the Sorbonne and director of the Radium Institute, but was not admitted to the Academy of Sciences due to discrimination despite her work. She died, like her mother, of acute leukemia. Her scientific work was complemented by her love of physical activity and motherhood.
Katharine Burr Blodgett By Smithsonian Institution, U.S.
Katharine Burr Blodgett (1898-1979) was a woman with an amazing number of firsts.  Born to a widow, she was a world citizen in her formative years, attended high school at a private school in New York City, won a scholarship to attend Bryn Mawr, and graduated second in her class there. She received her Master’s degree from the University of Chicago, then headed off to work with Nobel Laureate Irving Langmuir at General Electric (GE) and becoming the first woman research scientist there. She was able to work with Nobel Laureate Sir Ernest Rutherford and earn her Ph.D. from Cambridge University as the first woman to earn a doctorate from Cambridge. She returned to GE. During her career, she invented many applications and is credited with six patents. She achieved much when many women did not, but her work was de-valued in the media. She did earn recognition from her peers, including the ACS Garvan Medal, the Photographic Society of America Progress Medal, and a day named after her in her hometown of Schenectady, NY. In addition to her scientific life, she enjoyed gardening, civic engagement, acting, and “dart[ing] about Lake George in a fast motor boat.”
Astrophysicist Charlotte Emma Moore Sitterly (1898-1990) was an authority on sun composition. She started her career as an excellent student with extracurricular interests, attending Swarthmore College to earn her B.A. Upon graduation, she accepted a position as a mathematics computer at Princeton University Observatory, one of the few employment opportunities available to science inclined women at the time. A stint at the Mount Wilson Observatory led to results published a 1928 monograph which was considered the authoritative work on the solar spectrum for four decades. She received her Ph.D. from the University of California, Berkeley in 1931. Her work earned her the Annie J. Cannon Prize, Silver and Gold Medals from the Department of Commerce, and several honorary doctorates in the U.S. and abroad. She was the first woman elected foreign associate by the Royal Astronomical Society of London. Her enthusiasm for her work continued until her death.

Maria Goeppert-Mayer By Nobel Foundation
Nuclear Physicist Maria Goeppert-Mayer (1906-1972)  was the second woman to win the  physics NobelHer early education was public education for girls followed by a private school founded by suffragettes. Circumstances led Dr. Goeppert-Mayer to take her exiting exams a year early, passing them she attended the University of Göttingen for her college education in mathematics. She continued to study physics at the University of Göttingen, earning her Ph.D. in 1930. She also married that year. The couple moved to America in hopes of better career trajectory for Dr. Goeppert-Mayer. Finding a position was difficult. When she had her first child, she stayed home with her for one year, then returned to research. While her positions were always part-time and not well recognized, she grew a well-respected network of collaborators. This network led to work with Hans Jensen which won her the Nobel Prize, shared with Jensen. Her network also eventually led to a full professorship position after 20 years of volunteer work. During this time, her health began to fail. She persevered with her work, publishing her last paper in 1965. The American Physical Society established an award in her honor in1985
Gertrude Scharff Goldhaber (1911-1998) was a respected researcher. She grew up in a time in Germany where girls were expected to become schoolteachers. She had a fascination with numbers, and eventually studied physics at the University of Munich, receiving her PhD in 1935. She fled Germany during the rise of the Nazis due to being Jewish, arriving in the United States and becoming a citizen in 1944. She had a wide involvement in the various National Laboratories studying nuclear physics. She also maintained several committee positions in the science community. She was also a strong advocate for women in the science community, forming a Women in Science group at Brookhaven National Lab and supporting other similar groups elsewhere. After her retirement from research, she continued interests in the history of science, outdoor activities, and art.
The Chicago Pile One Team 
Physicist, Molecular Spectroscopist Leona Woods MarshallLibby (1919-1986) Leona Woods grew up on a farm and was known for her inexhaustible energy. She attained her B.S. in chemistry from the University of Chicago when she was only 19 years old, and earned her PhD 5 years later. She worked as the only woman and youngest member of the Chicago Metallurgical Laboratory, a secret war group led by Enrico Fermi who built the world’s first nuclear fission reactor during her graduate work. Dr. Woods’ expertise was essential to the undertaking. She married another member of her team. She hid her first pregnancy until 2 days before her son’s birth. She took one week off before returning to work. Childcare was provided by her mother and sometimes Fermi’s bodyguard, John Baudino. Dr. Marshall was encouraged by Fermi as a female physicist. In the late 1950s, Dr. Marshall was divorced from her husband, pursuing her own career. In the early 1960s, Dr. Marshall moved to Colorado to work and married Willard Libby. Her mind was always considering any number of problems from many angles. She worked up until her death and was honored posthumously for her work, along with Lise Meitner, Marie Curie, and Irene Joliot-Curie.
Chien-Shiung Wu 
Chien-Shiung Wu (1912-1997) was a foremost experimental physicist of modern eraShe was encouraged as a girl to pursue her schooling as far as possible. This led her to teaching training, which lacked science so she taught herself physics, chemistry, and mathematics. She graduated high school with the highest grades in her class, earning her a place at the National Central University in Nanjing. She taught and did research upon graduation, then moved to the United States to pursue graduate studies. She earned her Ph.D. from the University of California – Berkeley in 1940, four years after leaving China. She was known for her expertise in nuclear fission and was consulted by top scientists. Despite this, her gender and nationality hindered her finding appropriate employment due to discrimination on both accounts. She married and started a teaching career, although she missed research. Upon the recommendation of Ernest Lawrence, she received offers from several Ivy League schools who were not accepting female students at the time. She became Princeton’s first woman instructor at that time. She was offered several positions, including back in China, but chose to remain in the U.S. to raise her son. She was unable to return to China until 1973. She worked at Columbia for many decades and earned accolades for her work.

Xide Xie (1921-2000) is a woman in China who needs no introductionHer early life involved much moving due to war and ill health, during which she taught herself English, calculus, and physics. She graduated in 1942 with a degree from Xiamen University. She moved to the United States to receive her master’s degree from Smith College in 1949 and her Ph.D. in physics from M.I.T. in 1951. She married in England and returned to China, despite the political climate. She taught and did research at the prestigious Fudan University. During the Cultural Revolution of 1966-76, she was detained, publicly humiliated, and endured breast cancer. After this upheaval, she returned to Fudan University, growing the physics department and achieving more esteemed positions in the University and government. She had also remained connected to her family, caring for her husband through lengthy illness. Her achievements were internationally recognized.

Awards Mentioned

Benedettini Academics were a select group of scholars from the Academy of Sciences created and named for Pope Benedict XIV to conduct research and present it annually at Academy meetings. This appointment escalated the prestige of the scientist above that given by being a member of the Academy of Sciences.

American Association for University Women (AAUW): Margaret Maltby received the European Fellowship from the Association of Collegiate Alumnae, which became the AAUW. This fellowship was specifically intended to help American women pursue graduate studies to circumvent rules that did not allow women to enroll in coeducational universities or earn graduate degrees.

The Nobel Prize is an international award given in several fields. It is one of the most prestigious awards for scientists in the eyes of the public.

The Garvan Medal is an award from the American Chemical Society to recognize distinguished service to chemistry by women chemists.
The Photographic Society of AmericaProgress Medal recognized a person who has made an outstanding contribution to the progress of photography or an allied subject. 
Annie Jump Cannon Prize is given to a North American female astronomer in the early stages of her career for her distinguished contribution to the field.
Department of Commerce Silver Medal, Gold Medal are the highest honors granted by the department for distinguished and exceptional performance.


Much of the information for this post came from the book Notable Women in the Physical Sciences: A Biographical Dictionary edited by Benjamin F. Shearer and Barbara S. Shearer.
Images for this post came from Wikimedia Commons

Adrienne M Roehrich, Double X Science Chemistry Editor


Biology Explainer: The big 4 building blocks of life–carbohydrates, fats, proteins, and nucleic acids

The short version
  • The four basic categories of molecules for building life are carbohydrates, lipids, proteins, and nucleic acids.
  • Carbohydrates serve many purposes, from energy to structure to chemical communication, as monomers or polymers.
  • Lipids, which are hydrophobic, also have different purposes, including energy storage, structure, and signaling.
  • Proteins, made of amino acids in up to four structural levels, are involved in just about every process of life.                                                                                                      
  • The nucleic acids DNA and RNA consist of four nucleotide building blocks, and each has different purposes.
The longer version
Life is so diverse and unwieldy, it may surprise you to learn that we can break it down into four basic categories of molecules. Possibly even more implausible is the fact that two of these categories of large molecules themselves break down into a surprisingly small number of building blocks. The proteins that make up all of the living things on this planet and ensure their appropriate structure and smooth function consist of only 20 different kinds of building blocks. Nucleic acids, specifically DNA, are even more basic: only four different kinds of molecules provide the materials to build the countless different genetic codes that translate into all the different walking, swimming, crawling, oozing, and/or photosynthesizing organisms that populate the third rock from the Sun.

                                                  

Big Molecules with Small Building Blocks

The functional groups, assembled into building blocks on backbones of carbon atoms, can be bonded together to yield large molecules that we classify into four basic categories. These molecules, in many different permutations, are the basis for the diversity that we see among living things. They can consist of thousands of atoms, but only a handful of different kinds of atoms form them. It’s like building apartment buildings using a small selection of different materials: bricks, mortar, iron, glass, and wood. Arranged in different ways, these few materials can yield a huge variety of structures.

We encountered functional groups and the SPHONC in Chapter 3. These components form the four categories of molecules of life. These Big Four biological molecules are carbohydrates, lipids, proteins, and nucleic acids. They can have many roles, from giving an organism structure to being involved in one of the millions of processes of living. Let’s meet each category individually and discover the basic roles of each in the structure and function of life.
Carbohydrates

You have met carbohydrates before, whether you know it or not. We refer to them casually as “sugars,” molecules made of carbon, hydrogen, and oxygen. A sugar molecule has a carbon backbone, usually five or six carbons in the ones we’ll discuss here, but it can be as few as three. Sugar molecules can link together in pairs or in chains or branching “trees,” either for structure or energy storage.

When you look on a nutrition label, you’ll see reference to “sugars.” That term includes carbohydrates that provide energy, which we get from breaking the chemical bonds in a sugar called glucose. The “sugars” on a nutrition label also include those that give structure to a plant, which we call fiber. Both are important nutrients for people.

Sugars serve many purposes. They give crunch to the cell walls of a plant or the exoskeleton of a beetle and chemical energy to the marathon runner. When attached to other molecules, like proteins or fats, they aid in communication between cells. But before we get any further into their uses, let’s talk structure.

The sugars we encounter most in basic biology have their five or six carbons linked together in a ring. There’s no need to dive deep into organic chemistry, but there are a couple of essential things to know to interpret the standard representations of these molecules.

Check out the sugars depicted in the figure. The top-left molecule, glucose, has six carbons, which have been numbered. The sugar to its right is the same glucose, with all but one “C” removed. The other five carbons are still there but are inferred using the conventions of organic chemistry: Anywhere there is a corner, there’s a carbon unless otherwise indicated. It might be a good exercise for you to add in a “C” over each corner so that you gain a good understanding of this convention. You should end up adding in five carbon symbols; the sixth is already given because that is conventionally included when it occurs outside of the ring.

On the left is a glucose with all of its carbons indicated. They’re also numbered, which is important to understand now for information that comes later. On the right is the same molecule, glucose, without the carbons indicated (except for the sixth one). Wherever there is a corner, there is a carbon, unless otherwise indicated (as with the oxygen). On the bottom left is ribose, the sugar found in RNA. The sugar on the bottom right is deoxyribose. Note that at carbon 2 (*), the ribose and deoxyribose differ by a single oxygen.

The lower left sugar in the figure is a ribose. In this depiction, the carbons, except the one outside of the ring, have not been drawn in, and they are not numbered. This is the standard way sugars are presented in texts. Can you tell how many carbons there are in this sugar? Count the corners and don’t forget the one that’s already indicated!

If you said “five,” you are right. Ribose is a pentose (pent = five) and happens to be the sugar present in ribonucleic acid, or RNA. Think to yourself what the sugar might be in deoxyribonucleic acid, or DNA. If you thought, deoxyribose, you’d be right.

The fourth sugar given in the figure is a deoxyribose. In organic chemistry, it’s not enough to know that corners indicate carbons. Each carbon also has a specific number, which becomes important in discussions of nucleic acids. Luckily, we get to keep our carbon counting pretty simple in basic biology. To count carbons, you start with the carbon to the right of the non-carbon corner of the molecule. The deoxyribose or ribose always looks to me like a little cupcake with a cherry on top. The “cherry” is an oxygen. To the right of that oxygen, we start counting carbons, so that corner to the right of the “cherry” is the first carbon. Now, keep counting. Here’s a little test: What is hanging down from carbon 2 of the deoxyribose?

If you said a hydrogen (H), you are right! Now, compare the deoxyribose to the ribose. Do you see the difference in what hangs off of the carbon 2 of each sugar? You’ll see that the carbon 2 of ribose has an –OH, rather than an H. The reason the deoxyribose is called that is because the O on the second carbon of the ribose has been removed, leaving a “deoxyed” ribose. This tiny distinction between the sugars used in DNA and RNA is significant enough in biology that we use it to distinguish the two nucleic acids.

In fact, these subtle differences in sugars mean big differences for many biological molecules. Below, you’ll find a couple of ways that apparently small changes in a sugar molecule can mean big changes in what it does. These little changes make the difference between a delicious sugar cookie and the crunchy exoskeleton of a dung beetle.

Sugar and Fuel

A marathon runner keeps fuel on hand in the form of “carbs,” or sugars. These fuels provide the marathoner’s straining body with the energy it needs to keep the muscles pumping. When we take in sugar like this, it often comes in the form of glucose molecules attached together in a polymer called starch. We are especially equipped to start breaking off individual glucose molecules the minute we start chewing on a starch.

Double X Extra: A monomer is a building block (mono = one) and a polymer is a chain of monomers. With a few dozen monomers or building blocks, we get millions of different polymers. That may sound nutty until you think of the infinity of values that can be built using only the numbers 0 through 9 as building blocks or the intricate programming that is done using only a binary code of zeros and ones in different combinations.

Our bodies then can rapidly take the single molecules, or monomers, into cells and crack open the chemical bonds to transform the energy for use. The bonds of a sugar are packed with chemical energy that we capture to build a different kind of energy-containing molecule that our muscles access easily. Most species rely on this process of capturing energy from sugars and transforming it for specific purposes.

Polysaccharides: Fuel and Form

Plants use the Sun’s energy to make their own glucose, and starch is actually a plant’s way of storing up that sugar. Potatoes, for example, are quite good at packing away tons of glucose molecules and are known to dieticians as a “starchy” vegetable. The glucose molecules in starch are packed fairly closely together. A string of sugar molecules bonded together through dehydration synthesis, as they are in starch, is a polymer called a polysaccharide (poly = many; saccharide = sugar). When the monomers of the polysaccharide are released, as when our bodies break them up, the reaction that releases them is called hydrolysis.

Double X Extra: The specific reaction that hooks one monomer to another in a covalent bond is called dehydration synthesis because in making the bond–synthesizing the larger molecule–a molecule of water is removed (dehydration). The reverse is hydrolysis (hydro = water; lysis = breaking), which breaks the covalent bond by the addition of a molecule of water.

Although plants make their own glucose and animals acquire it by eating the plants, animals can also package away the glucose they eat for later use. Animals, including humans, store glucose in a polysaccharide called glycogen, which is more branched than starch. In us, we build this energy reserve primarily in the liver and access it when our glucose levels drop.

Whether starch or glycogen, the glucose molecules that are stored are bonded together so that all of the molecules are oriented the same way. If you view the sixth carbon of the glucose to be a “carbon flag,” you’ll see in the figure that all of the glucose molecules in starch are oriented with their carbon flags on the upper left.

The orientation of monomers of glucose in polysaccharides can make a big difference in the use of the polymer. The glucoses in the molecule on the top are all oriented “up” and form starch. The glucoses in the molecule on the bottom alternate orientation to form cellulose, which is quite different in its function from starch.

Storing up sugars for fuel and using them as fuel isn’t the end of the uses of sugar. In fact, sugars serve as structural molecules in a huge variety of organisms, including fungi, bacteria, plants, and insects.

The primary structural role of a sugar is as a component of the cell wall, giving the organism support against gravity. In plants, the familiar old glucose molecule serves as one building block of the plant cell wall, but with a catch: The molecules are oriented in an alternating up-down fashion. The resulting structural sugar is called cellulose.

That simple difference in orientation means the difference between a polysaccharide as fuel for us and a polysaccharide as structure. Insects take it step further with the polysaccharide that makes up their exoskeleton, or outer shell. Once again, the building block is glucose, arranged as it is in cellulose, in an alternating conformation. But in insects, each glucose has a little extra added on, a chemical group called an N-acetyl group. This addition of a single functional group alters the use of cellulose and turns it into a structural molecule that gives bugs that special crunchy sound when you accidentally…ahem…step on them.

These variations on the simple theme of a basic carbon-ring-as-building-block occur again and again in biological systems. In addition to serving roles in structure and as fuel, sugars also play a role in function. The attachment of subtly different sugar molecules to a protein or a lipid is one way cells communicate chemically with one another in refined, regulated interactions. It’s as though the cells talk with each other using a specialized, sugar-based vocabulary. Typically, cells display these sugary messages to the outside world, making them available to other cells that can recognize the molecular language.

Lipids: The Fatty Trifecta

Starch makes for good, accessible fuel, something that we immediately attack chemically and break up for quick energy. But fats are energy that we are supposed to bank away for a good long time and break out in times of deprivation. Like sugars, fats serve several purposes, including as a dense source of energy and as a universal structural component of cell membranes everywhere.

Fats: the Good, the Bad, the Neutral

Turn again to a nutrition label, and you’ll see a few references to fats, also known as lipids. (Fats are slightly less confusing that sugars in that they have only two names.) The label may break down fats into categories, including trans fats, saturated fats, unsaturated fats, and cholesterol. You may have learned that trans fats are “bad” and that there is good cholesterol and bad cholesterol, but what does it all mean?

Let’s start with what we mean when we say saturated fat. The question is, saturated with what? There is a specific kind of dietary fat call the triglyceride. As its name implies, it has a structural motif in which something is repeated three times. That something is a chain of carbons and hydrogens, hanging off in triplicate from a head made of glycerol, as the figure shows.  Those three carbon-hydrogen chains, or fatty acids, are the “tri” in a triglyceride. Chains like this can be many carbons long.

Double X Extra: We call a fatty acid a fatty acid because it’s got a carboxylic acid attached to a fatty tail. A triglyceride consists of three of these fatty acids attached to a molecule called glycerol. Our dietary fat primarily consists of these triglycerides.

Triglycerides come in several forms. You may recall that carbon can form several different kinds of bonds, including single bonds, as with hydrogen, and double bonds, as with itself. A chain of carbon and hydrogens can have every single available carbon bond taken by a hydrogen in single covalent bond. This scenario of hydrogen saturation yields a saturated fat. The fat is saturated to its fullest with every covalent bond taken by hydrogens single bonded to the carbons.

Saturated fats have predictable characteristics. They lie flat easily and stick to each other, meaning that at room temperature, they form a dense solid. You will realize this if you find a little bit of fat on you to pinch. Does it feel pretty solid? That’s because animal fat is saturated fat. The fat on a steak is also solid at room temperature, and in fact, it takes a pretty high heat to loosen it up enough to become liquid. Animals are not the only organisms that produce saturated fat–avocados and coconuts also are known for their saturated fat content.

The top graphic above depicts a triglyceride with the glycerol, acid, and three hydrocarbon tails. The tails of this saturated fat, with every possible hydrogen space occupied, lie comparatively flat on one another, and this kind of fat is solid at room temperature. The fat on the bottom, however, is unsaturated, with bends or kinks wherever two carbons have double bonded, booting a couple of hydrogens and making this fat unsaturated, or lacking some hydrogens. Because of the space between the bumps, this fat is probably not solid at room temperature, but liquid.

You can probably now guess what an unsaturated fat is–one that has one or more hydrogens missing. Instead of single bonding with hydrogens at every available space, two or more carbons in an unsaturated fat chain will form a double bond with carbon, leaving no space for a hydrogen. Because some carbons in the chain share two pairs of electrons, they physically draw closer to one another than they do in a single bond. This tighter bonding result in a “kink” in the fatty acid chain.

In a fat with these kinks, the three fatty acids don’t lie as densely packed with each other as they do in a saturated fat. The kinks leave spaces between them. Thus, unsaturated fats are less dense than saturated fats and often will be liquid at room temperature. A good example of a liquid unsaturated fat at room temperature is canola oil.

A few decades ago, food scientists discovered that unsaturated fats could be resaturated or hydrogenated to behave more like saturated fats and have a longer shelf life. The process of hydrogenation–adding in hydrogens–yields trans fat. This kind of processed fat is now frowned upon and is being removed from many foods because of its associations with adverse health effects. If you check a food label and it lists among the ingredients “partially hydrogenated” oils, that can mean that the food contains trans fat.

Double X Extra: A triglyceride can have up to three different fatty acids attached to it. Canola oil, for example, consists primarily of oleic acid, linoleic acid, and linolenic acid, all of which are unsaturated fatty acids with 18 carbons in their chains.

Why do we take in fat anyway? Fat is a necessary nutrient for everything from our nervous systems to our circulatory health. It also, under appropriate conditions, is an excellent way to store up densely packaged energy for the times when stores are running low. We really can’t live very well without it.

Phospholipids: An Abundant Fat

You may have heard that oil and water don’t mix, and indeed, it is something you can observe for yourself. Drop a pat of butter–pure saturated fat–into a bowl of water and watch it just sit there. Even if you try mixing it with a spoon, it will just sit there. Now, drop a spoon of salt into the water and stir it a bit. The salt seems to vanish. You’ve just illustrated the difference between a water-fearing (hydrophobic) and a water-loving (hydrophilic) substance.

Generally speaking, compounds that have an unequal sharing of electrons (like ions or anything with a covalent bond between oxygen and hydrogen or nitrogen and hydrogen) will be hydrophilic. The reason is that a charge or an unequal electron sharing gives the molecule polarity that allows it to interact with water through hydrogen bonds. A fat, however, consists largely of hydrogen and carbon in those long chains. Carbon and hydrogen have roughly equivalent electronegativities, and their electron-sharing relationship is relatively nonpolar. Fat, lacking in polarity, doesn’t interact with water. As the butter demonstrated, it just sits there.

There is one exception to that little maxim about fat and water, and that exception is the phospholipid. This lipid has a special structure that makes it just right for the job it does: forming the membranes of cells. A phospholipid consists of a polar phosphate head–P and O don’t share equally–and a couple of nonpolar hydrocarbon tails, as the figure shows. If you look at the figure, you’ll see that one of the two tails has a little kick in it, thanks to a double bond between the two carbons there.

Phospholipids form a double layer and are the major structural components of cell membranes. Their bend, or kick, in one of the hydrocarbon tails helps ensure fluidity of the cell membrane. The molecules are bipolar, with hydrophilic heads for interacting with the internal and external watery environments of the cell and hydrophobic tails that help cell membranes behave as general security guards.

The kick and the bipolar (hydrophobic and hydrophilic) nature of the phospholipid make it the perfect molecule for building a cell membrane. A cell needs a watery outside to survive. It also needs a watery inside to survive. Thus, it must face the inside and outside worlds with something that interacts well with water. But it also must protect itself against unwanted intruders, providing a barrier that keeps unwanted things out and keeps necessary molecules in.

Phospholipids achieve it all. They assemble into a double layer around a cell but orient to allow interaction with the watery external and internal environments. On the layer facing the inside of the cell, the phospholipids orient their polar, hydrophilic heads to the watery inner environment and their tails away from it. On the layer to the outside of the cell, they do the same.
As the figure shows, the result is a double layer of phospholipids with each layer facing a polar, hydrophilic head to the watery environments. The tails of each layer face one another. They form a hydrophobic, fatty moat around a cell that serves as a general gatekeeper, much in the way that your skin does for you. Charged particles cannot simply slip across this fatty moat because they can’t interact with it. And to keep the fat fluid, one tail of each phospholipid has that little kick, giving the cell membrane a fluid, liquidy flow and keeping it from being solid and unforgiving at temperatures in which cells thrive.

Steroids: Here to Pump You Up?

Our final molecule in the lipid fatty trifecta is cholesterol. As you may have heard, there are a few different kinds of cholesterol, some of which we consider to be “good” and some of which is “bad.” The good cholesterol, high-density lipoprotein, or HDL, in part helps us out because it removes the bad cholesterol, low-density lipoprotein or LDL, from our blood. The presence of LDL is associated with inflammation of the lining of the blood vessels, which can lead to a variety of health problems.

But cholesterol has some other reasons for existing. One of its roles is in the maintenance of cell membrane fluidity. Cholesterol is inserted throughout the lipid bilayer and serves as a block to the fatty tails that might otherwise stick together and become a bit too solid.

Cholesterol’s other starring role as a lipid is as the starting molecule for a class of hormones we called steroids or steroid hormones. With a few snips here and additions there, cholesterol can be changed into the steroid hormones progesterone, testosterone, or estrogen. These molecules look quite similar, but they play very different roles in organisms. Testosterone, for example, generally masculinizes vertebrates (animals with backbones), while progesterone and estrogen play a role in regulating the ovulatory cycle.

Double X Extra: A hormone is a blood-borne signaling molecule. It can be lipid based, like testosterone, or short protein, like insulin.

Proteins

As you progress through learning biology, one thing will become more and more clear: Most cells function primarily as protein factories. It may surprise you to learn that proteins, which we often talk about in terms of food intake, are the fundamental molecule of many of life’s processes. Enzymes, for example, form a single broad category of proteins, but there are millions of them, each one governing a small step in the molecular pathways that are required for living.

Levels of Structure

Amino acids are the building blocks of proteins. A few amino acids strung together is called a peptide, while many many peptides linked together form a polypeptide. When many amino acids strung together interact with each other to form a properly folded molecule, we call that molecule a protein.

For a string of amino acids to ultimately fold up into an active protein, they must first be assembled in the correct order. The code for their assembly lies in the DNA, but once that code has been read and the amino acid chain built, we call that simple, unfolded chain the primary structure of the protein.

This chain can consist of hundreds of amino acids that interact all along the sequence. Some amino acids are hydrophobic and some are hydrophilic. In this context, like interacts best with like, so the hydrophobic amino acids will interact with one another, and the hydrophilic amino acids will interact together. As these contacts occur along the string of molecules, different conformations will arise in different parts of the chain. We call these different conformations along the amino acid chain the protein’s secondary structure.

Once those interactions have occurred, the protein can fold into its final, or tertiary structure and be ready to serve as an active participant in cellular processes. To achieve the tertiary structure, the amino acid chain’s secondary interactions must usually be ongoing, and the pH, temperature, and salt balance must be just right to facilitate the folding. This tertiary folding takes place through interactions of the secondary structures along the different parts of the amino acid chain.

The final product is a properly folded protein. If we could see it with the naked eye, it might look a lot like a wadded up string of pearls, but that “wadded up” look is misleading. Protein folding is a carefully regulated process that is determined at its core by the amino acids in the chain: their hydrophobicity and hydrophilicity and how they interact together.

In many instances, however, a complete protein consists of more than one amino acid chain, and the complete protein has two or more interacting strings of amino acids. A good example is hemoglobin in red blood cells. Its job is to grab oxygen and deliver it to the body’s tissues. A complete hemoglobin protein consists of four separate amino acid chains all properly folded into their tertiary structures and interacting as a single unit. In cases like this involving two or more interacting amino acid chains, we say that the final protein has a quaternary structure. Some proteins can consist of as many as a dozen interacting chains, behaving as a single protein unit.

A Plethora of Purposes

What does a protein do? Let us count the ways. Really, that’s almost impossible because proteins do just about everything. Some of them tag things. Some of them destroy things. Some of them protect. Some mark cells as “self.” Some serve as structural materials, while others are highways or motors. They aid in communication, they operate as signaling molecules, they transfer molecules and cut them up, they interact with each other in complex, interrelated pathways to build things up and break things down. They regulate genes and package DNA, and they regulate and package each other.

As described above, proteins are the final folded arrangement of a string of amino acids. One way we obtain these building blocks for the millions of proteins our bodies make is through our diet. You may hear about foods that are high in protein or people eating high-protein diets to build muscle. When we take in those proteins, we can break them apart and use the amino acids that make them up to build proteins of our own.

Nucleic Acids

How does a cell know which proteins to make? It has a code for building them, one that is especially guarded in a cellular vault in our cells called the nucleus. This code is deoxyribonucleic acid, or DNA. The cell makes a copy of this code and send it out to specialized structures that read it and build proteins based on what they read. As with any code, a typo–a mutation–can result in a message that doesn’t make as much sense. When the code gets changed, sometimes, the protein that the cell builds using that code will be changed, too.

Biohazard!The names associated with nucleic acids can be confusing because they all start with nucle-. It may seem obvious or easy now, but a brain freeze on a test could mix you up. You need to fix in your mind that the shorter term (10 letters, four syllables), nucleotide, refers to the smaller molecule, the three-part building block. The longer term (12 characters, including the space, and five syllables), nucleic acid, which is inherent in the names DNA and RNA, designates the big, long molecule.

DNA vs. RNA: A Matter of Structure

DNA and its nucleic acid cousin, ribonucleic acid, or RNA, are both made of the same kinds of building blocks. These building blocks are called nucleotides. Each nucleotide consists of three parts: a sugar (ribose for RNA and deoxyribose for DNA), a phosphate, and a nitrogenous base. In DNA, every nucleotide has identical sugars and phosphates, and in RNA, the sugar and phosphate are also the same for every nucleotide.

So what’s different? The nitrogenous bases. DNA has a set of four to use as its coding alphabet. These are the purines, adenine and guanine, and the pyrimidines, thymine and cytosine. The nucleotides are abbreviated by their initial letters as A, G, T, and C. From variations in the arrangement and number of these four molecules, all of the diversity of life arises. Just four different types of the nucleotide building blocks, and we have you, bacteria, wombats, and blue whales.

RNA is also basic at its core, consisting of only four different nucleotides. In fact, it uses three of the same nitrogenous bases as DNA–A, G, and C–but it substitutes a base called uracil (U) where DNA uses thymine. Uracil is a pyrimidine.

DNA vs. RNA: Function Wars

An interesting thing about the nitrogenous bases of the nucleotides is that they pair with each other, using hydrogen bonds, in a predictable way. An adenine will almost always bond with a thymine in DNA or a uracil in RNA, and cytosine and guanine will almost always bond with each other. This pairing capacity allows the cell to use a sequence of DNA and build either a new DNA sequence, using the old one as a template, or build an RNA sequence to make a copy of the DNA.

These two different uses of A-T/U and C-G base pairing serve two different purposes. DNA is copied into DNA usually when a cell is preparing to divide and needs two complete sets of DNA for the new cells. DNA is copied into RNA when the cell needs to send the code out of the vault so proteins can be built. The DNA stays safely where it belongs.

RNA is really a nucleic acid jack-of-all-trades. It not only serves as the copy of the DNA but also is the main component of the two types of cellular workers that read that copy and build proteins from it. At one point in this process, the three types of RNA come together in protein assembly to make sure the job is done right.


 By Emily Willingham, DXS managing editor 
This material originally appeared in similar form in Emily Willingham’s Complete Idiot’s Guide to College Biology

Making Light in Electronics

By DXS Physics Editor Matthew Francis 

A while back, I wrote about one of the most common ways of making electric light: fluorescent bulbs. Understanding fluorescent lights requires quantum mechanics! While a lot of quantum physics seems pretty removed from our daily lives, it’s essential to most of our modern technology. In fact, reading what I’m writing requires quantum mechanics, since you are using a computer (maybe a handheld computer like an iPad or smart phone, but it’s still a computer) or a printout from a computer.

Modern electronics, including computers and phones, depend on semiconductors. Conductors (like the copper wire in power cords) let electricity flow easily, but semiconductors conduct electricity more reluctantly—but that very reluctance lets us control the flow. While they can’t sustain large currents like conductors can, we can tinker with the chemistry of semiconductors to make them conduct electricity in very precise ways. One of those ways lets semiconductor devices make light: those are known as light-emitting diodes, or LEDs.

You likely have many LEDs in your home: they’re common as indicator lights on appliances, and you might even have LED light bulbs. While they’re pretty expensive right now, the price of LED lights is getting lower all the time, and they have major advantages over both incandescent (old-style) light bulbs and fluorescents. They won’t burn out even as quickly as fluorescent lights (themselves longer-lived than incandescents), and consume less energy. Since they are based on solids rather than gases, they’re not going to break easily, either! But how do they work?

The Electrons in the Band

When I described fluorescent lights in my earlier post, I described how atoms have distinct energy levels inside them, and light is produced when electrons move between those energy levels. Fluorescent lights use gases (generally mercury vapor), so the atoms are relatively widely separated. In solids, including semiconductors, atoms are tightly packed together, forming bonds that don’t break without high pressures or temperatures. In fact, they may also share electrons with each other; a particularly dramatic example of this is in metals, where the electrons in the highest energy levels of the atoms all form a gas that surrounds the atoms. That’s why metals are such good conductors—a little push from a battery or other power source makes those electrons flow in one direction (on average at least), much as a fan creates currents in the air.

Semiconductors are a bit more complicated: their electrons are loosely bound, but still stuck to their host atoms. The way physicists understand this is something known as the band model: just like atoms have energy levels, solids have energy bands. Low energies correspond to electrons stuck to their atoms, which can’t leave; we call these closed shell electrons (for reasons that aren’t important for this particular post). Moderate energies are known as valence electrons, which stay put ordinarily, but can be persuaded to move if given the right incentive. Finally, high energies are conduction electrons, which aren’t tied to a particular atom at all; as their name suggests, they are the ones that carry electric current.

Whether a solid conducts electricity depends on its band structure, and the size of the energy barrier in between the bands, which is called a gap. Large gaps require large energies for electrons to jump them, while smaller gaps are more easily jumped. Conductors have negligible gaps between their valence and conduction bands, while insulators have huge gaps. Semiconductors lie in between; adding extra atoms to a semiconductor can make the gap smaller (a process known as “doping”, which sometimes makes describing it unintentionally funny).

Cars and Roads and Electrons

At low temperatures, semiconductors may not conduct electricity at all, since no electrons can jump the gap into the conduction band. Either warming them up a bit or applying an external electric current gives the electrons the energy they need to move into the conduction band.

I was pondering analogies about band structures to help us understand them, and thought of this one based on cars and roads. Think of closed shells as like parking spaces along a road: cars (which stand in for electrons) are stationary. Valence bands are the slow lane, which is clogged with traffic, so the cars technically can move, but don’t. The conduction bands are fast lanes: cars can really zip, but there’s a traffic barrier between the slow lane and fast lane. (That barrier is the weakest part of my analogy, so remember that we should be thinking of a barrier as something that can be traversed under some conditions but not others.)

One more complication: there are two types of semiconductors, known as n-type and p-type. In n-type, just a few electrons (cars) have access to the conduction band (fast lane) at a time, but in p-type, enough electrons get in to leave holes in the valence band. Applying a current to the semiconductor shifts another valence electron into the hole, but that leaves another hole, and so forth…so it looks like the hole is moving! In fact, physicists refer to this as “hole conduction”, which also sounds odd if you’re not used to it.

Now we’re finally ready to understand LEDs. If you join an n-type semiconductor to a p-type semiconductor, you make something known as a diode. (The prefix di- refers to the number two. If you join three semiconductors, you get a transistor of either the pnp or npn types, depending on the order you use.) The bands (lanes) don’t line up perfectly at the junction: the conduction band in the n-type is generally only slightly higher than the valence band of the p-type, so just a little nudge is needed to move electrons across. This means when they reach the junction between the materials, electrons from the n-type semiconductor can fill the holes on the p-type, which is a decrease in energy. Just as in individual atoms, moving from a higher energy level to a lower energy level makes a photon—and that’s where the LE in the D comes from!

LEDs tend to produce very pure colors, rather than the mixture of colors our eyes perceive as white light. To create LED light bulbs, generally blue LEDs are coated with a phosphorescent material, much like the kind used in fluorescent bulbs. Unlike fluorescents, though, there’s no gas involved, and less heat is lost (though there is still a little bit). Together these factors make LED light bulbs longer-lasting and more efficient even than fluorescents, though currently they are far more expensive.

Despite how common LEDs and other semiconductors are, they’re considered fairly advanced physics. But guess what: if I did my job right, you should understand LED physics now! What is often thought of as “advanced” is really everyday science, and it’s a part of how quantum mechanics (with all its electrons and fascinating interactions on the microscopic level) has helped create our modern world.

Is the bar high enough for screening breast ultrasounds for breast cancer?

The stormy landscape of the breast, as seen
on ultrasound. At top center (dark circle) is
a small cyst. Source: Wikimedia Commons.
Credit: Nevit Dilmen.
By Laura Newman, contributor

In a unanimous decision, FDA has approved the first breast ultrasound imaging system for dense breast tissue “for use in combination with a standard mammography in women with dense breast tissue who have a negative mammogram and no symptoms of breast cancer.” Patients should not interpret FDA’s approval of the somo-v Automated Breast Ultrasound System as an endorsement of the device as necessarily beneficial for this indication and this will be a thorny concept for many patients to appreciate.

If the approval did not take place in the setting of intense pressure to both inform women that they have dense breasts and lobbying to roll out all sorts of imaging studies quickly, no matter how well they have been studied, it would not be worth posting.

Dense breasts are worrisome to women, especially young women (in their 40s particularly) because they have proved a risk factor for developing breast cancer. Doing ultrasound on every woman with dense breasts, though, who has no symptoms, and a normal mammogram potentially encompasses as many as 40% of women undergoing screening mammography who also have dense breasts, according to the FDA’s press release. Dense breast tissue is most common in young women, specifically women in their forties, and breast density declines with age.

The limitations of mammography in seeing through dense breast tissue have been well known for decades and the search has been on for better imaging studies. Government appointed panels have reviewed the issue and mammography for women in their forties has been controversial. What’s new is the “Are You Dense?” patient movement and legislation to inform women that they have dense breasts.

Merits and pitfalls of device approval
The approval of breast ultrasound hinges on a study of 200 women with dense breast evaluated retrospectively at 13 sites across the United States with mammography and ultrasound. The study showed a statistically significant increase in breast cancer detection when ultrasound was used with mammography.

Approval of a device of this nature (noninvasive, already approved in general, but not for this indication) does not require the company to demonstrate that use of the device reduces morbidity or mortality, or that health benefits outweigh risks.

Eitan Amir, MD, PhD, medical oncologist at Princess Margaret Hospital, Toronto, Canada, said: “It’s really not a policy decision. All this is, is notice that if you want to buy the technology, you can.”

That’s clearly an important point, but not one that patients in the US understand. Patients hear “FDA approval” and assume that means a technology most certainly is for them and a necessary add-on. This disconnect in the FDA medical device approval process and in what patients think it means warrants an overhaul or at the minimum, a clarification for the public.

Materials for FDA submission are available on the FDA website, including the study filed with FDA and a PowerPoint presentation, but lots of luck, finding them quickly. “In the submission by Sunnyvale CA uSystems to FDA, the company stated that screening reduces lymph node positive breast cancer,” noted Amir. “There are few data to support this comment.”

Is cancer detection a sufficient goal?
In the FDA study, more cancers were identified with ultrasound. However, one has to question whether breast cancer detection alone is meaningful in driving use of a technology. In the past year, prostate cancer detection through PSA screening has been attacked because several studies and epidemiologists have found that screening is a poor predictor of who will die from prostate cancer or be bothered by it during their lifetime. We seem to be picking up findings that don’t lead to much to worry about, according to some researchers. Could new imaging studies for breast cancer suffer the same limitation? It is possible.

Another question is whether or not the detected cancers on ultrasound in the FDA study would have been identified shortly thereafter on a routine mammogram. It’s a question that is unclear from the FDA submission, according to Amir.

One of the problems that arises from excess screening is overdiagnosis, overtreatment, and high-cost, unaffordable care. An outcomes analysis of 9,232 women in the US Breast Cancer Surveillance Consortium led by Gretchen L. Gierach, PhD, MPH, at the National Institutes of Health MD, and published online in the August 21 Journal of the National Cancer Institute, revealed: “High mammographic breast density was not associated with risk of death from breast cancer or death from any cause after accounting for other patient and tumor characteristics.” –Gierach et al., 2012

Proposed breast cancer screening tests
Meanwhile, numerous imaging modalities have been proposed as an adjunct to mammography and as potential replacements for mammography. In 2002, proponents of positron emission tomography (PET) asked Medicare to approve pet scans for imaging dense breast tissue, especially in Asian women. The Medicare Coverage Advisory Commission heard testimony, but in the end, Medicare did not approve it for the dense-breast indication.

PET scans are far less popular today, while magnetic resonance imaging (AKA MR, MRI) and imaging have emerged as as adjuncts to mammography for women with certain risk factors. Like ultrasound, the outcomes data is not in the bag for screening with it.

In an interview with Monica Morrow, MD, Chief of Breast Surgery at Memorial Sloan-Kettering Cancer Center, New York, several months ago concerning the rise in legislation to inform women about dense breasts, which frequently leads to additional imaging studies, she said: “There is no good data that women with dense breasts benefit from additional MR screening.” She is not the only investigator to question potentially deleterious use of MR ahead of data collection and analysis. Many breast researchers have expressed fear that women will opt for double mastectomies, based on MR, that in the end, may have been absolutely unnecessary.

“There is one clear indication for MR screening,” stressed Morrow, explaining that women with BRCA mutations should be screened with MRI. “Outside of that group, there was no evidence that screening women with MR was beneficial.”

At just about every breast cancer meeting in the past two years, the benefits and harms of MR and other proposed screening modalities come up, and there is no consensus in the field.  It  should be noted, though, that plenty of breast physicians are skeptical about broad use of MR– not just generalists outside of the field. In other words, it is not breast and radiology specialists versus the US Preventive Services Task Force – a very important message for patients to understand.

One thing is clear: as these new technologies gain FDA approval, it will be a windfall for industry. If industry is successful and doctors are biased to promoting these tests, many may offer them on the estimated 40% of women with dense breasts who undergo routine mammograms, as well as other women evaluated as having a high lifetime risk.  The tests will be offered in a setting of unclear value and uncertain harms. Even though FDA has not approved breast MRI for screening dense breasts, breast MR is being used off label and it is far more costly than mammography.

When patients raise concerns about the unaffordability of medical care, they should be counseled about the uncertain benefit and potential harms of such a test. That may be a tall bill for most Americans to consider: it’s clear that the more is better philosophy is alive and well. Early detection of something, anything, even something dormant, going nowhere, is preferable to skipping a test, and risking who-knows-what, and that is something, most of us cannot imagine at the outset.

[Today's post is from Patient POVthe blog of Laura Newman, a science writer who has worked in health care for most of her adult life, first as a health policy analyst, and as a medical journalist for the last two decades. She was a proud member of the women’s health movement. She has a longstanding interest in what matters to patients and thinks that patients should play a major role in planning and operational discussions about healthcare. Laura’s news stories have appeared in Scientific American blogs, WebMD Medical News, Medscape, Drug Topics, Applied Neurology, Neurology Today, the Journal of the National Cancer Institute, The Lancet, and BMJ, and numerous other outlets. You can find her on Twitter @lauranewmanny.]

Ed note: The original version of this post contains a posted correction that is incorporated into the version you’ve read here.

The opinions in this article do not necessarily conflict with or reflect those of the DXS editorial team. 

Anorexia nervosa, neurobiology, and family-based treatment

Via Wikimedia Commons
Photo credit: Sandra Mann
By Harriet Brown, DXS contributor

Back in 1978, psychoanalyst Hilde Bruch published the first popular book on anorexia nervosa. In The Golden Cage, she described anorexia as a psychological illness caused by environmental factors: sexual abuse, over-controlling parents, fears about growing up, and/or other psychodynamic factors. Bruch believed young patients needed to be separated from their families (a concept that became known as a “parentectomy”) so therapists could help them work through the root issues underlying the illness. Then, and only then, patients would choose to resume eating. If they were still alive.

Bruch’s observations dictated eating-disorders treatments for decades, treatments that led to spectacularly ineffective results. Only about 35% of people with anorexia recovered; another 20% died, of starvation or suicide; and the rest lived with some level of chronic illness for the rest of their lives.

Not a great track record, overall, and especially devastating for women, who suffer from anorexia at a rate of 10 times that of men. Luckily, we know a lot more about anorexia and other eating disorders now than we did in 1978.

“It’s Not About the Food”

In Bruch’s day, anorexia wasn’t the only illness attributed to faulty parenting and/or trauma. Therapists saw depression, anxiety, schizophrenia, eating disorders, and homosexuality (long considered a psychiatric “illness”) as ailments of the mind alone. Thanks to the rising field of behavioral neuroscience, we’ve begun to untangle the ways brain circuitry, neural architecture, and other biological processes contribute to these disorders. Most experts now agree that depression and anxiety can be caused by, say, neurotransmitter imbalances as much as unresolved emotional conflicts, and treat them accordingly. But the field of eating-disorders treatment has been slow to jump on the neurobiology bandwagon. When my daughter was diagnosed with anorexia in 2005, for instance, we were told to find her a therapist and try to get our daughter to eat “without being the food police,” because, as one therapist informed us, “It’s not about the food.”

Actually, it is about the food. Especially when you’re starving.

Ancel Keys’ 1950 Semi-Starvation Study tracked the effects of starvation and subsequent re-feeding on 36 healthy young men, all conscientious objectors who volunteered for the experiment. Keys was drawn to the subject during World War II, when millions in war-torn Europe – especially those in concentration camps – starved for years. One of Keys’ most interesting findings was that starvation itself, followed by re-feeding after a period of prolonged starvation, produced both physical and psychological symptoms, including depression, preoccupation with weight and body image, anxiety, and obsessions with food, eating, and cooking—all symptoms we now associate with anorexia. Re-feeding the volunteers eventuallyreversed most of the symptoms. However, this approach proved to be difficult on a psychological level, and in some ways more difficult than the starvation period. These results were a clear illustration of just how profound the effects of months of starvation were on the body and mind.

Alas, Keys’ findings were pretty much ignored by the field of eating-disorders treatment for 40-some years, until new technologies like functional magnetic resonance imaging (fMRI) and research gave new context to his work. We now know there is no single root cause for eating disorders. They’re what researchers call multi-factorial, triggered by a perfect storm of factors that probably differs for each person who develops an eating disorder. “Personality characteristics, the environment you live in, your genetic makeup—it’s like a cake recipe,” says Daniel le Grange, Ph.D., director of the Eating Disorders Program at the University of Chicago. “All the ingredients have to be there for that person to develop anorexia.”

One of those ingredients is genetics. Twenty years ago, the Price Foundation sponsored a project that collected DNA samples from thousands of people with eating disorders, their families, and control participants. That data, along with information from the 2006 Swedish Twin Study, suggests that anorexia is highly heritable. “Genes play a substantial role in liability to this illness,” says Cindy Bulik, Ph.D., a professor of psychiatry and director of the University of North Carolina’s Eating Disorders Program. And while no one has yet found a specific anorexia gene, researchers are focusing on an area of chromosome 1 that shows important gene linkages.

Certain personality traits associated with anorexia are probably heritable as well. “Anxiety, inhibition, obsessionality, and perfectionism seem to be present in families of people with an eating disorder,” explains Walter Kaye, M.D., who directs the Eating Disorders Treatment and Research Program at the University of California-San Diego. Another ingredient is neurobiology—literally, the way your brain is structured and how it works. Dr. Kaye’s team at UCSD uses fMRI technology to map blood flow in people’s brains as they think of or perform a task. In one study, Kaye and his colleagues looked at the brains of people with anorexia, people recovered from anorexia, and people who’d never had an eating disorder as they played a gambling game. Participants were asked to guess a number and were rewarded for correct guesses with money or “punished” for incorrect or no guesses by losing money.

Participants in the control group responded to wins and losses by “living in the moment,” wrote researchers: “That is, they made a guess and then moved on to the next task.” But people with anorexia, as well as people who’d recovered from anorexia, showed greater blood flow to the dorsal caudate, an area of the brain that helps link actions and their outcomes, as well as differences in their brains’ dopamine pathways. “People with anorexia nervosa do not live in the moment,” concluded Kaye. “They tend to have exaggerated and obsessive worry about the consequences of their behaviors, looking for rules when there are none, and they are overly concerned about making mistakes.” This study was the first to show altered pathways in the brain even in those recovered from anorexia, suggesting that inherent differences in the brain’s architecture and signaling systems help trigger the illness in the first place.

Food Is Medicine

Some of the best news to come out of research on anorexia is a new therapy aimed at kids and teens. Family-based treatment (FBT), also known as the Maudsley approach, was developed at the Maudsley Hospital in London by Ivan Eisler and Christopher Dare, family therapists who watched nurses on the inpatient eating-disorders unit get patients to eat by sitting with them, talking to them, rubbing their backs, and supporting them. Eisler and Dare wondered how that kind of effective encouragement could be used outside the hospital.

Their observations led them to develop family-based treatment, or FBT, a three-phase treatment for teens and young adults that sidesteps the debate on etiology and focuses instead on recovery. “FBT is agnostic on cause,” says Dr. Le Grange. During phase one, families (usually parents) take charge of a child’s eating, with a goal of fully restoring weight (rather than get to the “90 percent of ideal body weight” many programs use as a benchmark). In phase two, families gradually transfer responsibility for eating back to the teen. Phase three addresses other problems or issues related to normal adolescent development, if there are any.

FBT is a pragmatic approach that recognizes that while people with anorexia are in the throes of acute malnourishment, they can’t choose to eat. And that represents one of the biggest shifts in thinking about eating disorders. The DSM-IV, the most recent “bible” of psychiatric treatment, lists as the first symptom of anorexia “a refusal to maintain body weight at or above a minimally normal weight for age and height.” That notion of refusal is key to how anorexia has been seen, and treated, in the past: as a refusal to eat or gain weight. An acting out. A choice. Which makes sense within the psychodynamic model of cause.

But it doesn’t jibe with the research, which suggests that anorexia is more of an inability to eat than a refusal. Forty-five years ago, Aryeh Routtenberg, then (and still) a professor of psychology at Northwestern University, discovered that when he gave rats only brief daily access to food but let them run as much as they wanted on wheels, they would gradually eat less and less, and run more and more. In fact, they would run without eating until they died, a paradigm Routtenberg called activity-based anorexia (ABA). Rats with ABA seemed to be in the grip of a profound physiological imbalance, one that overrode the normal biological imperatives of hunger and self-preservation. ABA in rats suggests that however it starts, once the cycle of restricting and/or compulsive exercising passes a certain threshold, it takes on a life of its own. Self-starvation is no longer (if it ever was) a choice, but a compulsion to the death.

That’s part of the thinking in FBT. Food is the best medicine for people with anorexia, but they can’t choose to eat. They need someone else to make that choice for them. Therapists don’t sit at the table with patients, but parents do. And parents love and know their children. Like the nurses at the Maudsley Hospital, they find ways to get kids to eat. In a sense, what parents do is outshout the anorexia “voice” many sufferers report hearing, a voice in their heads that tells them not to eat and berates them when they do. Parents take the responsibility for making the choice to eat away from the sufferer, who may insist she’s choosing not to eat but who, underneath the illness, is terrified and hungry.

The best aspect of FBT is that it works. Not for everyone, but for the majority of kids and teens. Several randomized controlled studies of FBT and “treatment as usual” (talk therapy without pressure to eat) show recovery rates of 80 to 90 percent with FBT—a huge improvement over previous recovery rates. A study at the University of Chicago is looking at adapting the treatment for young adults; early results are promising.

The most challenging aspect of FBT is that it’s hard to find. Relatively few therapists in the U.S. are trained in the approach. When our daughter got sick, my husband and I couldn’t find a local FBT therapist. So we cobbled together a team that included our pediatrician, a therapist, and lots of friends who supported our family through the grueling work of re-feeding our daughter. Today she’s a healthy college student with friends, a boyfriend, career goals, and a good relationship with us.

A few years ago, Dr. Le Grange and his research partner, Dr. James Lock of Stanford, created a training institute that certifies a handful of FBT therapists each year. (For a list of FBT providers, visit the Maudsley Parents website.) It’s a start. But therapists are notoriously slow to adopt new treatments, and FBT is no exception. Some therapists find FBT controversial because it upends the conventional view of eating disorders and treatments. Some cling to the psychodynamic view of eating disorders despite the lack of evidence. Still, many in the field have at least heard of FBT and Kaye’s neurobiological findings, even if they don’t believe in them yet.

Change comes slowly. But it comes.

* * *

Harriet Brown teaches magazine journalism at the S.I. Newhouse School of Public Communications in Syracuse, New York. Her latest book is Brave Girl Eating: A Family’s Struggle with Anorexia (William Morrow, 2010).

be there for that person to develop anorexia.”

One of those ingredients is genetics. Twenty years ago, the Price Foundation sponsored a project that collected DNA samples from thousands of people with eating disorders, their families, and control participants. That data, along with information from the 2006 Swedish Twin Study, suggests that anorexia is highly heritable. “Genes play a substantial role in liability to this illness,” says Cindy Bulik, Ph.D., a professor of psychiatry and director of the University of North Carolina’s Eating Disorders Program. And while no one has yet found a specific anorexia gene, researchers are focusing on an area of chromosome 1 that shows important gene linkages.
Certain personality traits associated with anorexia are probably heritable as well. “Anxiety, inhibition, obsessionality, and perfectionism seem to be present in families of people with an eating disorder,” explains Walter Kaye, M.D., who directs the Eating Disorders Treatment and Research Program at the University of California-San Diego. Another ingredient is neurobiology—literally, the way your brain is structured and how it works. Dr. Kaye’s team at UCSD uses fMRI technology to map blood flow in people’s brains as they think of or perform a task. In one study, Kaye and his colleagues looked at the brains of people with anorexia, people recovered from anorexia, and people who’d never had an eating disorder as they played a gambling game. Participants were asked to guess a number and were rewarded for correct guesses with money or “punished” for incorrect or no guesses by losing money.
Participants in the control group responded to wins and losses by “living in the moment,” wrote researchers: “That is, they made a guess and then moved on to the next task.” But people with anorexia, as well as people who’d recovered from anorexia, showed greater blood flow to the dorsal caudate, an area of the brain that helps link actions and their outcomes, as well as differences in their brains’ dopamine pathways. “People with anorexia nervosa do not live in the moment,” concluded Kaye. “They tend to have exaggerated and obsessive worry about the consequences of their behaviors, looking for rules when there are none, and they are overly concerned about making mistakes.” This study was the first to show altered pathways in the brain even in those recovered from anorexia, suggesting that inherent differences in the brain’s architecture and signaling systems help trigger the illness in the first place.
Food Is Medicine
Some of the best news to come out of research on anorexia is a new therapy aimed at kids and teens. Family-based treatment (FBT), also known as the Maudsley approach, was developed at the Maudsley Hospital in London by Ivan Eisler and Christopher Dare, family therapists who watched nurses on the inpatient eating-disorders unit get patients to eat by sitting with them, talking to them, rubbing their backs, and supporting them. Eisler and Dare wondered how that kind of effective encouragement could be used outside the hospital.
Their observations led them to develop family-based treatment, or FBT, a three-phase treatment for teens and young adults that sidesteps the debate on etiology and focuses instead on recovery. “FBT is agnostic on cause,” says Dr. Le Grange. During phase one, families (usually parents) take charge of a child’s eating, with a goal of fully restoring weight (rather than get to the “90 percent of ideal body weight” many programs use as a benchmark). In phase two, families gradually transfer responsibility for eating back to the teen. Phase three addresses other problems or issues related to normal adolescent development, if there are any.
FBT is a pragmatic approach that recognizes that while people with anorexia are in the throes of acute malnourishment, they can’t choose to eat. And that represents one of the biggest shifts in thinking about eating disorders. The DSM-IV, the most recent “bible” of psychiatric treatment, lists as the first symptom of anorexia “a refusal to maintain body weight at or above a minimally normal weight for age and height.” That notion of refusal is key to how anorexia has been seen, and treated, in the past: as a refusal to eat or gain weight. An acting out. A choice. Which makes sense within the psychodynamic model of cause.
But it doesn’t jibe with the research, which suggests that anorexia is more of an inability to eat than a refusal. Forty-five years ago, Aryeh Routtenberg, then (and still) a professor of psychology at Northwestern University, discovered that when he gave rats only brief daily access to food but let them run as much as they wanted on wheels, they would gradually eat less and less, and run more and more. In fact, they would run without eating until they died, a paradigm Routtenberg called activity-based anorexia (ABA). Rats with ABA seemed to be in the grip of a profound physiological imbalance, one that overrode the normal biological imperatives of hunger and self-preservation. ABA in rats suggests that however it starts, once the cycle of restricting and/or compulsive exercising passes a certain threshold, it takes on a life of its own. Self-starvation is no longer (if it ever was) a choice, but a compulsion to the death.
That’s part of the thinking in FBT. Food is the best medicine for people with anorexia, but they can’t choose to eat. They need someone else to make that choice for them. Therapists don’t sit at the table with patients, but parents do. And parents love and know their children. Like the nurses at the Maudsley Hospital, they find ways to get kids to eat. In a sense, what parents do is outshout the anorexia “voice” many sufferers report hearing, a voice in their heads that tells them not to eat and berates them when they do. Parents take the responsibility for making the choice to eat away from the sufferer, who may insist she’s choosing not to eat but who, underneath the illness, is terrified and hungry.
The best aspect of FBT is that it works. Not for everyone, but for the majority of kids and teens. Several randomized controlled studies of FBT and “treatment as usual” (talk therapy without pressure to eat) show recovery rates of 80 to 90 percent with FBT—a huge improvement over previous recovery rates. A study at the University of Chicago is looking at adapting the treatment for young adults; early results are promising.
The most challenging aspect of FBT is that it’s hard to find. Relatively few therapists in the U.S. are trained in the approach. When our daughter got sick, my husband and I couldn’t find a local FBT therapist. So we cobbled together a team that included our pediatrician, a therapist, and lots of friends who supported our family through the grueling work of re-feeding our daughter. Today she’s a healthy college student with friends, a boyfriend, career goals, and a good relationship with us.
A few years ago, Dr. Le Grange and his research partner, Dr. James Lock of Stanford, created a training institute that certifies a handful of FBT therapists each year. (For a list of FBT providers, visit the Maudsley Parents website.) It’s a start. But therapists are notoriously slow to adopt new treatments, and FBT is no exception. Some therapists find FBT controversial because it upends the conventional view of eating disorders and treatments. Some cling to the psychodynamic view of eating disorders despite the lack of evidence. Still, many in the field have at least heard of FBT and Kaye’s neurobiological findings, even if they don’t believe in them yet.
Change comes slowly. But it comes.
* * *
Harriet Brown teaches magazine journalism at the S.I. Newhouse School of Public Communications in Syracuse, New York. Her latest book is Brave Girl Eating: A Family’s Struggle with Anorexia (William Morrow, 2010).

Mariette DiChristina

Mariette DiChristina is editor in chief of Scientific American.

[Ed. note: This interview is the second installment in our new series, Double Xpression: Profiles of Women into Science. The focus of these profiles is how women in science express themselves in ways that aren’t necessarily scientific, how their ways of expression inform their scientific activities and vice-versa, and the reactions they encounter.]

Today’s profile is an interview with Mariette DiChristina, editor in chief, Scientific American, who answered our questions via email with DXS Biology Editor Jeanne Garbarino. Read on to find out what a Marx Brothers movie has to do with communicating science.

                         

DXS: First, can you give me a quick overview of what your scientific background is and your current connection to science?

MD: Like most kids, I was born a scientist. What I mean is, I wanted to know how everything worked, and I wanted to learn about it firsthand. At a tag sale, for instance, I remember buying a second-hand biology book called The Body along with my second-hand Barbie for 50 cents. “Are you sure your mom is going to be OK with you buying that?” asked the concerned neighbor, eyeing the biology book.

I memorized the names and orbital periods of the planets and of dinosaurs like some kids spout baseball stats (which I could also do as a kid, by the way). We didn’t have a lot of money, so I caught my own pet fish from a nearby pond by using my little finger as a pretend worm. I scooped up my fish with an old plastic container and put it on my nightstand. If it died, I buried it and dug it up later so I could look at the bones. My proudest birthday gifts were when I got a chemistry set and a microscope with 750x. A girlfriend and I got the idea to pick up a gerbil that had a bad habit of biting fingers, just so we could get blood to squeeze on a glass slide. (She was braver than I was about being the one to get bitten.)

In middle school, I was a proud member of the Alchemists—an after-school science club—so I could do extra labs and clean the beakers and put away Bunsen burners for fun. I knew I would be a scientist when I grew up.

But somewhere during my high school courses, I came to believe that being a scientist meant I’d have to pick one narrow discipline and stick to it. I felt that I liked everything too much to do that, however. As an undergraduate, I eventually figured out that what I really wanted was to be a student of many different things for life, and then share those things I learned with others. That led me to a journalism degree. It also means that, as far as knowledge about science goes, I fit the cliché of being “an inch deep and a mile wide.”

DXS: What ways do you express yourself creatively that may not have a single thing to do with science?

MD: This one is a tough one for me to answer because I am always trying to convince people that pretty much everything they care about in the headlines actually has to do with science! In my case, I’ve also always been interested in drawing and in visuals in general. I was a pretty serious art student in high school as well, although I later decided that I didn’t have enough passion for it to make that my career choice. My interest in art partly led me to work at magazines like Scientific American and Popular Science, where the ability to storyboard an informational graphic and otherwise think visually is very helpful.

When I’m home, I really enjoy making things with my two daughters, such as helping them with crafts or scrapbooks, although I definitely spend a lot more time on planning dinners and cooking for (and with) the family than anything else. I like the puzzle solving of setting up the meals for the week during the weekend, so it’s easier for my husband to get things ready weeknights. We’re big on eating dinner together as a family every night. I like gardening and mapping out planting beds. I’m better at planting than at keeping up with tending, however, because of my intense work schedule and travel. In short, if I have free time at all, I’m enjoying it with my family. And if we’re doing some creative expression while we’re at it, great!

DXS: Do you find that your connection to science informs your creativity, even though what you do may not specifically be scientific?

MD: My connection to science informs most things that I do in one way or another. When I’m making dinner, I sometimes find myself talking about the chemistry of cooking with the girls. Especially when our daughters were smaller, if one of them had a question, I’d try to come up with ways to make finding the answer together into a kind of science adventure or project.

I suppose that since I spend most of my waking hours thinking about how best to present science to the public, it’s just a mental routine, or a lens through which I tend to view the world.

DXS: Have you encountered situations in which your expression of yourself outside the bounds of science has led to people viewing you differently–either more positively or more negatively?

MD: It’s more the other way around. I get amusing reactions from people once they find out what I do. How could I seem so normal and yet work in a field that relates to…shudder…science? An attorney friend has sometimes kidded me, saying there’s no way he can understand what’s in Scientific American, so I must be incredibly smart. I don’t feel that way at all! Anybody who has a high school degree and an interest in the topic can understand a feature article in Scientific American. Science is for everyone. And science isn’t only for people who work in labs. It’s just a rational way of looking at life. I also believe science is the engine of human prosperity. And if I sound a little evangelistic about that, well, I am.
DXS: Have you found that your non-science expression of creativity/activity/etc. has in any way informed your understanding of science or how you may talk about it or present it to others?

MD: I think it’s helpful to look to non-science areas for ideas about ways to help make science appealing, especially for people who might be intimidated by the subject. My main job is to try to make a connection for people to the science we cover in Scientific American. I once had a boss at Popular Sciencewho made all us editors take an intensive, three-day screenwriting course that culminated in the showing and exposition, scene by scene, of the structure and writing techniques of Casablanca. When I came back, he gave me a big grin and said, “So, what did you think?” I got his point about bringing narrative techniques into feature articles. Like most people, I enjoy movies and plays; now I also look at them for storytelling tips. And there are lots of creative ways to tell science stories beyond words: pictures, slide shows, videos, songs. Digital media are so flexible.

DXS: How comfortable are you expressing your femininity and in what ways? How does this expression influence people’s perception of you in, say, a scientifically oriented context?

MD: I was the oldest of three daughters raised by a single dad (my mom died when I was 12) and I was always a tomboy, playing softball through college and so on. So I can’t say I’ve ever been terribly feminine, at least in the stereotypical ways. At the same time, I’m obviously a wife and a mother who, like most parents, tries not to talk about my kids so often that it’s irritating to friends and coworkers. I once was scolded in a letter from an irritated reader after I had mentioned my kids in a “From the Editor” column about education. He wrote that if I was so interested in science education and kids, I should go back home and “bake cookies.” I laughed pretty hard at that.

DXS: Do you think that the combination of your non-science creativity and scientific-related activity shifts people’s perspectives or ideas about what a scientist or science communicator is? If you’re aware of such an influence, in what way, if any, do you use it to (for example) reach a different corner of your audience or present science in a different sort of way?

MD: I’m sure that’s true. I think personality and approach also might shift perspectives. A girlfriend of mine once called me “the friendly face of science.” I guess I smile a lot, and I like to meet people and try to get to know them. That ability—being able to make a personal connection to different people—is important for every good editor. My job, essentially, is to understand your interests well enough to make sure Scientific American is something that you’ll enjoy each day, week, month.

Increasingly, also, the audiences are different in different media, so we need to understand how to flex the approach a bit to appeal to those different audiences. In print, for instance, according to the most recent data we have from MRI, the median age of Scientific American readers is 47, with 70 percent men and 30 percent women. The picture is quite different online, where, according to Nielsen, our median age is 40 and the male/female ratio is closer to half and half, with 56.5 percent men to 43.5 percent women. You need to bring a lot of creative thinking to the task of how to make one brand serve rather different sets of people.

Fortunately, I have terrific, creative staff! And another part of the way you do that, I think, is to invite your readers in to collaborate; we’ve done a bit of that in the past year on http://www.scientificamerican.com/, and I’m looking forward to experimenting further in the coming months. Ultimately, I’d like to turn Scientific American from a magazine with an amazing 166-year tradition of being a conduit of authoritative information about science and technology into a platform where curious minds can gather and share.

DXS: If you had something you could say to the younger you about the role of expression and creativity in your chosen career path, what would you say? 

MD: I was pretty determined to do something—whatever it was—that would let me satisfy my curiosity and passion about science. I would tell younger me, who, by the way, never intended to go into magazine management: It’s just as fun, rewarding and creative to be a science writer as you suspect it might be. I’d also tell the younger me something that didn’t occur to me early enough to pull it off—that a double major in journalism and science might be a good idea. And, I would add, it’s also a good idea to take some business classes, so you’ll be better armed for dealing with the working world.


Also on Double X Science

More about Mariette DiChristina

Mariette DiChristina oversees Scientific American Continue reading