Fonts, Syllabi, and Poop | TAPP 123

Host Kevin Patton revisits the concept of using the syllabus and other course documents to build a positive and productive course culture. Poop—it's everywhere! Does the font or typeface we use affect students—especially regarding learning and memory? We look for answers in this episode!

00:00 | Introduction

00:52 | Revisiting the Syllabus

16:28 | Poop. Poop. Poop.

19:00 | Sponsored by AAA

19:59 | Fonts Are Important in Teaching & Learning

30:54 | Sponsored by HAPI

31:57 | Desirably Difficult Reading?

42:00 | Sponsored by HAPS

43:00 | Fluent & Dysfluent Fonts

56:12 | Staying Connected

 

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Typography must often draw attention to itself before it will be read. Yet in order to be read, it must relinquish the attention it has drawn. (Robert Bringhurst)

 

Revisiting the Syllabus

15.5 minutes

Creating and nurturing a course culture can be influenced by our syllabus and other course materials. We revisit this idea with a few more tips and tweaks.

★ Anatomy &; Physiology Syllabus: It's an Art | TAPP 120

★ Are We Answering Student Questions? | Science Updates | TAPP 92

★ Wendy Riggs has a huge collection of anatomy, physiology, and general bio, instructional videos she uses in her flipped classes youtube.com/user/wendogg1

★ Natalie Wade has engaging short videos about A&P content and study tips at The Anatomy Gal youtube.com/c/TheAnatomyGal

★ Jamie Chapman has a collection (Chapman Histology) of short (under 3 minutes) videos guiding students through lessons in histology youtube.com/c/ChapmanHistology

Poop. Poop. Poop.

2.5 minutes

After releasing The Poop Episode | Using Fecal Changes to Monitor Health | TAPP 121, I learned of a whole movement of poop listening on smart speakers. And that there are actually poop songs that are viral hits. Really.

★ When kids yell 'Alexa, play poop,' you'll hear these songs (story from All Things Considered on National Public Radioo) AandP.info/wv2

★ The Foot Book (Bright & Early children's book by Dr. Seuss; can be read as The Poop Book) geni.us/afvGc

★ CHOC Stool Diary AandP.info/4yq

★ Bowel Symptom Journal (from Alberta Health Services) AandP.info/6fw

★ Poop Apps: 5 Tools for Tracking Your Stools AandP.info/5ow

 

Sponsored by AAA

56 seconds

A searchable transcript for this episode, as well as the captioned audiogram of this episode, are sponsored by the American Association for Anatomy (AAA) at anatomy.org.

Searchable transcript

Captioned audiogram 

Don't forget—HAPS members get a deep discount on AAA membership!

AMERICAN ASSOCIATION FOR ANATOMY STATEMENT OF RESPONSIBILITY FOR ITS HISTORY OF RACISM (Press release from AAA, giving the full text of the statement) AandP.info/eei

Fonts Are Important in Teaching & Learning

11 minutes

At the suggestion of listener Dr. David Curole, we examine the roles that different fonts can play in teaching, learning, and memory. This segment reviews some past discussions of fonts, then introduces some new concepts of using fonts in teaching. Featured is a Word Dissection of the terms fluent font and dysfluent (disfluent) font.

★ Communication, Clarity, & Medical Errors | Episode 55

★ Anatomy & Physiology Syllabus: It's an Art | TAPP 120

★ Why Anatomy & Physiology Students Need Sectional Anatomy | TAPP 116

 

Sponsored by HAPI Online Graduate Program

59 seconds

The Master of Science in Human Anatomy & Physiology Instruction—the MS-HAPI—is a graduate program for A&P teachers, especially for those who already have a graduate/professional degree. A combination of science courses (enough to qualify you to teach at the college level) and courses in contemporary instructional practice, this program helps you be your best in both on-campus and remote teaching. Kevin Patton is a faculty member in this program at Northeast College of Health Sciences. Check it out!

northeastcollege.edu/hapi

Desirably Difficult Reading?

10 minutes

The article How Fonts Affect Learning and Memory by Carla Delgado takes our conversation a step further by looking the potential role of dysfluent fonts in learning.

★ How Fonts Affect Learning and Memory (article in Discover Magazine by Carla Delgado mentioned in this segment) AandP.info/wof

★ A Review of the Cognitive Effects of Disfluent Typography on Functional Reading (review article from The Design Journal) AandP.info/mwt

★ Fortune Favors the Bold (and the Italicized): Effects of Disfluency on Educational Outcomes (article from Proceedings of the Annual Meeting of the Cognitive Science Society) AandP.info/jjt

★ Changing Fonts in Education: How the Benefits Vary with Ability and Dyslexia (article from The Journal of Educational Research) AandP.info/yt4

★ Fluency and the Detection of Misleading Questions: Low Processing Fluency Attenuates the Moses Illusion (article from the journal Social Cognition) AandP.info/jul

 

Sponsored by HAPS

56 seconds

The Human Anatomy & Physiology Society (HAPS) is a sponsor of this podcast.  You can help appreciate their support by clicking the link below and checking out the many resources and benefits found there. Watch for virtual town hall meetings and upcoming regional meetings!

Anatomy & Physiology Society

theAPprofessor.org/haps

Fluent & Dysfluent Fonts

13 minutes

We identify some potentially fluent fonts, as well as a few dysfluent fonts (see image below or at AandP.info/ihy). Sans Forgetica font was developed specifically to be dysfluent in a way that promotes remembering what is read. Does it work? Should we incorporate dysfluent fonts in our teaching materials?

★ Fonts and Fluency: The Effects of Typeface Familiarity, Appropriateness, and Personality on Reader Judgments (thesis by Tim Wang) AandP.info/0hf

★ Previously claimed memory boosting font 'Sans Forgetica' does not actually boost memory (story from ScienceDaily) AandP.info/zp4

★ The science of Sans Forgetica - The font to remember (video from the creators of Sans Forgetica) AandP.info/ox5

★ An unforgettable year – Sans Forgetica turns one (article from the RMIT University website) AandP.info/fo3

★ Sans Forgetica: Study Mode by RMIT University (plugin for Chrome browser lets you read any web page in Sans Forgetica) AandP.info/fc3

★ Sans Forgetica (free download for personal use) AandP.info/o4g

★ Can very small font size enhance memory? (article from journal Memory & Cognition) AandP.info/rlk

★ Sans Forgetica is not desirable for learning (article from the journal Memory) AandP.info/hmu

★ The role of font size and font style in younger and older adults' predicted and actual recall performance (article from
Neuropsychology, development, and cognition. Section B, Aging, Neuropsychology and Cognition) AandP.info/r6s

 

People

Contributors: David Curole, Terry Thompson

Mentions: Wendy Riggs, Natalie Wade, Jaime Chapman, Robert Bringhurst, Carla Delgado

Production: Aileen Park (announcer), Andrés Rodriguez (theme composer,  recording artist), Rev.com team (transcription), Kevin Patton (writer, editor, producer, host)

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★ Transcript and captions for this episode are supported by the American Association for Anatomy | anatomy.org

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Biomolecule Imaging Pioneers Share Nobel Prize

Today, the Royal Swedish Academy of Sciences has decided to award the Nobel Prize in Chemistry 2017 to Jacques Dubochet (University of Lausanne, Switzerland) and Joachim Frank (Columbia University, New York, USA), and Richard Henderson (MRC Laboratory of Molecular Biology, Cambridge, UK). The award is given "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution"

Cool microscope technology revolutionises biochemistry

We may soon have detailed images of life’s complex machineries in atomic resolution. The Nobel Prize in Chemistry 2017 is awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for the development of cryo-electron microscopy, which both simplifies and improves the imaging of biomolecules. This method has moved biochemistry into a new era.

A picture is a key to understanding. Scientific breakthroughs often build upon the successful visualization of objects invisible to the human eye. However, biochemical maps have long been filled with blank spaces because the available technology has had difficulty generating images of much of life’s molecular machinery. Cryo-electron microscopy changes all of this. Researchers can now freeze biomolecules mid-movement and visualize processes they have never previously seen, which is decisive for both the basic understanding of life’s chemistry and for the development of pharmaceuticals.

Electron microscopes were long believed to only be suitable for imaging dead matter, because the powerful electron beam destroys biological material. But in 1990, Richard Henderson succeeded in using an electron microscope to generate a three-dimensional image of a protein at atomic resolution. This breakthrough proved the technology’s potential.

Joachim Frank made the technology generally applicable. Between 1975 and 1986 he developed an image processing method in which the electron microscope’s fuzzy two-dimensional images are analysed and merged to reveal a sharp three-dimensional structure.

Jacques Dubochet added water to electron microscopy. Liquid water evaporates in the electron microscope’s vacuum, which makes the biomolecules collapse. In the early 1980s, Dubochet succeeded in vitrifying water – he cooled water so rapidly that it solidified in its liquid form around a biological sample, allowing the biomolecules to retain their natural shape even in a vacuum.

Following these discoveries, the electron microscope’s every nut and bolt have been optimised. The desired atomic resolution was reached in 2013, and researchers can now routinely produce three-dimensional structures of biomolecules. In the past few years, scientific literature has been filled with images of everything from proteins that cause antibiotic resistance, to the surface of the Zika virus. Biochemistry is now facing an explosive development and is all set for an exciting future.

About the Nobel Laureates

Jacques Dubochet, born 1942 in Aigle, Switzerland. Ph.D. 1973, University of Geneva and University of Basel, Switzerland. Honorary Professor of Biophysics, University of Lausanne, Switzerland.
www.unil.ch/dee/en/home/menuinst/people/honorary-professors/prof-jacques-dubochet.html

Joachim Frank, born 1940 in Siegen, Germany. Ph.D. 1970, Technical University of Munich, Germany. Professor of Biochemistry and Molecular Biophysics and of Biological Sciences, Columbia University, New York, USA.
http://franklab.cpmc.columbia.edu/franklab/

Richard Henderson, born 1945 in Edinburgh, Scotland. Ph.D. 1969, Cambridge University, UK. Programme Leader, MRC Laboratory of Molecular Biology, Cambridge, UK.
www2.mrc-lmb.cam.ac.uk/groups/rh15/

What can we use from this in teaching undergraduate A&P?

• If you talk about imaging molecules in your course, this could be a way to garner student interest—considering that this is a current and ongoing effort in science. I always have a brief "shape is important in biological chemistry and here's what we can see with current tools" because they're going to see all those little odd-shaped rutabaga blobs in illustrations in their textbooks.


• If you bring up microscopy in your course, perhaps describing the types of microscopy, adding a bit of info on this could help show students that microscopy is still evolving—in exciting ways.


• Consider using the annual Nobel Prize announcements as a springboard to discuss the process of scientific discovery. 


• Consider mentioning the other major awards for scientific achievement and discuss what the judges seem to value most about scientific discoveries. The Nobel Prize is the one everyone has heard of, so it's a great place to start.


• Use the Nobel Prizes (and other awards) over time as a way to keep students aware of the history of, and progress, of human biology. One could also address the global diversity of laureates.  Or the lack of other kinds of diversity among laureates.

Want to know more?

Popular Information 

• my-ap.us/2hNGb1D 

Scientific Background

• my-ap.us/2hPtKm0

Images

Image - 3D structures (pdf 1.4 MB)

• © Johan Jarnestad/The Royal Swedish Academy of Sciences
• my-ap.us/2hNUq6o

Image - Blobology (pdf 8.5 MB)

• © Martin Högbom/The Royal Swedish Academy of Sciences
• my-ap.us/2hLMaDV

Image - Dubochet's preparation method (948 kB)

• © Johan Jarnestad/The Royal Swedish Academy of Sciences 
• hmy-ap.us/2hPtYJS

Image - Frank's image analysis (pdf 1 MB)

• © Johan Jarnestad/The Royal Swedish Academy of Sciences
• my-ap.us/2hMkU8i 

Cool Animations (literally)

Structure and gating of the nuclear pore complex

• Eibauer M, Pellanda M, Turgay Y, Dubrovsky A, Wild A, Medalia 
• my-ap.us/2hMolMe
• my-ap.us/2hKWxbd

Ion gating in the sarcoplasmic reticulum membrane

• Samsó M, Feng W, Pessah I, Allen P
• my-ap.us/2hLJCWg

Antibody structure

• Zhang L, Ren G
• my-ap.us/2hLQp2j

Native LDL particles

• Kumar V, Butcher S, Öörni K, Engelhardt P, Heikkonen J, Kaski K, Ala-Korpela M, Kovanen P
• my-ap.us/2hO4Qms

Changes in the water and ion contents of organelles during apoptosis

• Nolin F, Michel J, Wortham L, Tchelidze P, Banchet V, Lalun N, Terryn C, Ploton D
• my-ap.us/2hMTYW4

Adapted from press release at nobelprize.org
Click each image for its source/attribution

Nobel Prize for Biological Clock Mechanisms

The Nobel Assembly at Karolinska Institutet has today decided to award the 2017 Nobel Prize in Physiology or Medicine jointly to Jeffrey C. Hall, Michael Rosbash, and Michael W. Young for their discoveries of molecular mechanisms controlling the circadian rhythm.

Summary

Life on Earth is adapted to the rotation of our planet. For many years we have known that living organisms, including humans, have an internal, biological clock that helps them anticipate and adapt to the regular rhythm of the day. But how does this clock actually work? Jeffrey C. Hall, Michael Rosbash and Michael W. Young were able to peek inside our biological clock and elucidate its inner workings. Their discoveries explain how plants, animals and humans adapt their biological rhythm so that it is synchronized with the Earth's revolutions.

Using fruit flies as a model organism, this year's Nobel laureates isolated a gene that controls the normal daily biological rhythm. They showed that this gene encodes a protein that accumulates in the cell during the night, and is then degraded during the day. Subsequently, they identified additional protein components of this machinery, exposing the mechanism governing the self-sustaining clockwork inside the cell. We now recognize that biological clocks function by the same principles in cells of other multicellular organisms, including humans.

With exquisite precision, our inner clock adapts our physiology to the dramatically different phases of the day. The clock regulates critical functions such as behavior, hormone levels, sleep, body temperature and metabolism. Our wellbeing is affected when there is a temporary mismatch between our external environment and this internal biological clock, for example when we travel across several time zones and experience "jet lag". There are also indications that chronic misalignment between our lifestyle and the rhythm dictated by our inner timekeeper is associated with increased risk for various diseases.

Our inner clock

Most living organisms anticipate and adapt to daily changes in the environment. During the 18th century, the astronomer Jean Jacques d'Ortous de Mairan studied mimosa plants, and found that the leaves opened towards the sun during daytime and closed at dusk. He wondered what would happen if the plant was placed in constant darkness. He found that independent of daily sunlight the leaves continued to follow their normal daily oscillation (Figure 1). Plants seemed to have their own biological clock.

Other researchers found that not only plants, but also animals and humans, have a biological clock that helps to prepare our physiology for the fluctuations of the day. This regular adaptation is referred to as the circadian rhythm, originating from the Latin words circa meaning "around" and dies meaning "day". But just how our internal circadian biological clock worked remained a mystery.

Figure 1. An internal biological clock. The leaves of the mimosa plant open towards the sun during day but close at dusk (upper part). Jean Jacques d'Ortous de Mairan placed the plant in constant darkness (lower part) and found that the leaves continue to follow their normal daily rhythm, even without any fluctuations in daily light.

Identification of a clock gene

During the 1970's, Seymour Benzer and his student Ronald Konopka asked whether it would be possible to identify genes that control the circadian rhythm in fruit flies. They demonstrated that mutations in an unknown gene disrupted the circadian clock of flies. They named this gene period. But how could this gene influence the circadian rhythm?

This year's Nobel Laureates, who were also studying fruit flies, aimed to discover how the clock actually works. In 1984, Jeffrey Hall and Michael Rosbash, working in close collaboration at Brandeis University in Boston, and Michael Young at the Rockefeller University in New York, succeeded in isolating the period gene. Jeffrey Hall and Michael Rosbash then went on to discover that PER, the protein encoded by period, accumulated during the night and was degraded during the day. Thus, PER protein levels oscillate over a 24-hour cycle, in synchrony with the circadian rhythm.

A self-regulating clockwork mechanism

The next key goal was to understand how such circadian oscillations could be generated and sustained. Jeffrey Hall and Michael Rosbash hypothesized that the PER protein blocked the activity of the period gene. They reasoned that by an inhibitory feedback loop, PER protein could prevent its own synthesis and thereby regulate its own level in a continuous, cyclic rhythm (Figure 2A).

Figure 2B. A simplified illustration of the molecular components of the circadian clock.

Such a regulatory feedback mechanism explained how this oscillation of cellular protein levels emerged, but questions lingered. What controlled the frequency of the oscillations? Michael Young identified yet another gene, doubletime, encoding the DBT protein that delayed the accumulation of the PER protein. This provided insight into how an oscillation is adjusted to more closely match a 24-hour cycle.

The paradigm-shifting discoveries by the laureates established key mechanistic principles for the biological clock. During the following years other molecular components of the clockwork mechanism were elucidated, explaining its stability and function. For example, this year's laureates identified additional proteins required for the activation of the period gene, as well as for the mechanism by which light can synchronize the clock.

Keeping time on our human physiology

The biological clock is involved in many aspects of our complex physiology. We now know that all multicellular organisms, including humans, utilize a similar mechanism to control circadian rhythms. A large proportion of our genes are regulated by the biological clock and, consequently, a carefully calibrated circadian rhythm adapts our physiology to the different phases of the day (Figure 3). Since the seminal discoveries by the three laureates, circadian biology has developed into a vast and highly dynamic research field, with implications for our health and wellbeing.

Figure 3. The circadian clock anticipates and adapts our physiology to the different phases of the day. Our biological clock helps to regulate sleep patterns, feeding behavior, hormone release, blood pressure, and body temperature.

About the Nobel Laureates

Jeffrey C. Hall was born 1945 in New York, USA. He received his doctoral degree in 1971 at the University of Washington in Seattle and was a postdoctoral fellow at the California Institute of Technology in Pasadena from 1971 to 1973. He joined the faculty at Brandeis University in Waltham in 1974. In 2002, he became associated with University of Maine.

Michael Rosbash was born in 1944 in Kansas City, USA. He received his doctoral degree in 1970 at the Massachusetts Institute of Technology in Cambridge. During the following three years, he was a postdoctoral fellow at the University of Edinburgh in Scotland. Since 1974, he has been on faculty at Brandeis University in Waltham, USA.

Michael W. Young was born in 1949 in Miami, USA. He received his doctoral degree at the University of Texas in Austin in 1975. Between 1975 and 1977, he was a postdoctoral fellow at Stanford University in Palo Alto. From 1978, he has been on faculty at the Rockefeller University in New York.

What can we use from this in teaching undergraduate A&P?

• When you discuss biological clocks and rhythms in your course, this could be a way to garner student interest—considering that this is a current and ongoing effort in science. I begin discussing this at the beginning of the course—when covering  homeostasis.


• Consider using the annual Nobel Prize announcements as a springboard to discuss the process of scientific discovery. 


• Consider mentioning the other major awards for scientific achievement and discuss what the judges seem to value most about scientific discoveries. The Nobel Prize is the one everyone has heard of, so it's a great place to start.


• Use the Nobel Prizes (and other awards) over time as a way to keep students aware of the history of, and progress, of human biology. One could also address the global diversity of laureates.  Or the lack of other kinds of diversity among laureates.

The sources below are great places to find media for teaching and for great, pithy explanations of complex topics for a "beginner" audience like our A&P students.

Want to know more?

Advanced information

• my-ap.us/2hJ7lGZ

P-element transformation with period locus DNA restores rhythmicity to mutant, arrhythmic Drosophila melanogaster.

• Zehring, W.A., Wheeler, D.A., Reddy, P., Konopka, R.J., Kyriacou, C.P., Rosbash, M., and Hall, J.C. (1984).  Cell 39, 369–376.
• my-ap.us/2kkb5ze

Restoration of circadian behavioural rhythms by gene transfer in Drosophila. 

• Bargiello, T.A., Jackson, F.R., and Young, M.W. (1984). Nature 312, 752–754.
• my-ap.us/2kmvMux

Antibodies to the period gene product of Drosophila reveal diverse tissue distribution and rhythmic changes in the visual system.

• Siwicki, K.K., Eastman, C., Petersen, G., Rosbash, M., and Hall, J.C. (1988).  Neuron 1, 141–150.
• my-ap.us/2klDMvI

Feedback of the Drosophila period gene product on circadian cycling of its messenger RNA levels.

• Hardin, P.E., Hall, J.C., and Rosbash, M. (1990).  Nature 343, 536–540.
• my-ap.us/2knh2LS

The period gene encodes a predominantly nuclear protein in adult Drosophila.

• Liu, X., Zwiebel, L.J., Hinton, D., Benzer, S., Hall, J.C., and Rosbash, M. (1992).  J Neurosci 12, 2735–2744.
• my-ap.us/2kngfuu

Block in nuclear localization of period protein by a second clock mutation, timeless.

• Vosshall, L.B., Price, J.L., Sehgal, A., Saez, L., and Young, M.W. (1994).  Science 263, 1606–1609.
• my-ap.us/2kneqh8

double-time is a novel Drosophila clock gene that regulates PERIOD protein accumulation. 

• Price, J.L., Blau, J., Rothenfluh, A., Abodeely, M., Kloss, B., and Young, M.W. (1998). Cell 94, 83–95.
• my-ap.us/2kocqVJ

Content: Adapted from press release at nobelprize.org 

Illustrations: © The Nobel Committee for Physiology or Medicine. Illustrator: Mattias Karlén

Autophagy Discovery Garners Nobel Prize

The Nobel Assembly at Karolinska Institutet has today decided to award the 2016 Nobel Prize in Physiology or Medicine to Yoshinori Ohsumi for his discoveries of mechanisms for autophagy.

Overview

This year's Nobel Laureate discovered and elucidated mechanisms underlying autophagy, a fundamental process for degrading and recycling cellular components.

The word autophagy (aw-toh-FAY-jee) originates from the Greek words auto-, meaning "self", and phagein, meaning "to eat". Thus, autophagy denotes "self eating".

This concept emerged during the 1960's, when researchers first observed that the cell could destroy its own contents by enclosing it in membranes, forming sack-like vesicles that were transported to a recycling compartment, called the lysosome, for degradation.

Difficulties in studying the phenomenon meant that little was known until, in a series of brilliant experiments in the early 1990's, Yoshinori Ohsumi used baker's yeast to identify genes essential for autophagy. He then went on to elucidate the underlying mechanisms for autophagy in yeast and showed that similar sophisticated machinery is used in our cells.

Ohsumi's discoveries led to a new paradigm in our understanding of how the cell recycles its content. His discoveries opened the path to understanding the fundamental importance of autophagy in many physiological processes, such as in the adaptation to starvation or response to infection. Mutations in autophagy genes can cause disease, and the autophagic process is involved in several conditions including cancer and neurological disease.

Degradation – a central function in all living cells

In the mid 1950's scientists observed a new specialized cellular compartment, called an organelle, containing enzymes that digest proteins, carbohydrates and lipids. This specialized compartment is referred to as a "lysosome" and functions as a workstation for degradation of cellular constituents. The Belgian scientist Christian de Duve was awarded the Nobel Prize in Physiology or Medicine in 1974 for the discovery of the lysosome.

New observations during the 1960's showed that large amounts of cellular content, and even whole organelles, could sometimes be found inside lysosomes. The cell therefore appeared to have a strategy for delivering large cargo to the lysosome. Further biochemical and microscopic analysis revealed a new type of vesicle transporting cellular cargo to the lysosome for degradation (Figure 1).

Christian de Duve, the scientist behind the discovery of the lysosome, coined the term autophagy, "self-eating", to describe this process. The new vesicles were named autophagosomes.

Figure 1: Autophagosome. Our cells have different specialized compartments. Lysosomes constitute one such compartment and contain enzymes for digestion of cellular contents. A new type of vesicle called autophagosome was observed within the cell. As the autophagosome forms, it engulfs cellular contents, such as damaged proteins and organelles. Finally, it fuses with the lysosome, where the contents are degraded into smaller constituents. This process provides the cell with nutrients and building blocks for renewal.

During the 1970's and 1980's researchers focused on elucidating another system used to degrade proteins, namely the "proteasome". Within this research field Aaron Ciechanover, Avram Hershko and Irwin Rose were awarded the 2004 Nobel Prize in Chemistry for "the discovery of ubiquitin-mediated protein degradation". The proteasome efficiently degrades proteins one-by-one, but this mechanism did not explain how the cell got rid of larger protein complexes and worn-out organelles. Could the process of autophagy be the answer and, if so, what were the mechanisms?

A groundbreaking experiment

Yoshinori Ohsumi had been active in various research areas, but upon starting his own lab in 1988, he focused his efforts on protein degradation in the vacuole, an organelle that corresponds to the lysosome in human cells.

Yeast cells are relatively easy to study and consequently they are often used as a model for human cells. They are particularly useful for the identification of genes that are important in complex cellular pathways. But Ohsumi faced a major challenge; yeast cells are small and their inner structures are not easily distinguished under the microscope and thus he was uncertain whether autophagy even existed in this organism.

Ohsumi reasoned that if he could disrupt the degradation process in the vacuole while the process of autophagy was active, then autophagosomes should accumulate within the vacuole and become visible under the microscope. He therefore cultured mutated yeast lacking vacuolar degradation enzymes and simultaneously stimulated autophagy by starving the cells.

The results were striking! Within hours, the vacuoles were filled with small vesicles that had not been degraded (Figure 2). The vesicles were autophagosomes and Ohsumi's experiment proved that authophagy exists in yeast cells. But even more importantly, he now had a method to identify and characterize key genes involved this process. This was a major break-through and Ohsumi published the results in 1992.

Figure 2: Yeast. In yeast (left panel) a large compartment called the vacuole corresponds to the lysosome in mammalian cells. Ohsumi generated yeast lacking vacuolar degradation enzymes. When these yeast cells were starved, autophagosomes rapidly accumulated in the vacuole (middle panel). His experiment demonstrated that autophagy exists in yeast. As a next step, Ohsumi studied thousands of yeast mutants (right panel) and identified 15 genes that are essential for autophagy.

Autophagy genes are discovered

Ohsumi now took advantage of his engineered yeast strains in which autophagosomes accumulated during starvation. This accumulation should not occur if genes important for autophagy were inactivated. Ohsumi exposed the yeast cells to a chemical that randomly introduced mutations in many genes, and then he induced autophagy.

His strategy worked! Within a year of his discovery of autophagy in yeast, Ohsumi had identified the first genes essential for autophagy. In his subsequent series of elegant studies, the proteins encoded by these genes were functionally characterized. The results showed that autophagy is controlled by a cascade of proteins and protein complexes, each regulating a distinct stage of autophagosome initiation and formation (Figure 3).

Figure 3: Stages of autophagosome formation. Ohsumi studied the function of the proteins encoded by key autophagy genes. He delineated how stress signals initiate autophagy and the mechanism by which proteins and protein complexes promote distinct stages of autophagosome formation.

Autophagy – an essential mechanism in our cells

After the identification of the machinery for autophagy in yeast, a key question remained. Was there a corresponding mechanism to control this process in other organisms? Soon it became clear that virtually identical mechanisms operate in our own cells. The research tools required to investigate the importance of autophagy in humans were now available.

Thanks to Ohsumi and others following in his footsteps, we now know that autophagy controls important physiological functions where cellular components need to be degraded and recycled.

Autophagy can rapidly provide fuel for energy and building blocks for renewal of cellular components, and is therefore essential for the cellular response to starvation and other types of stress.

After infection, autophagy can eliminate invading intracellular bacteria and viruses. Autophagy contributes to embryo development and cell differentiation. Cells also use autophagy to eliminate damaged proteins and organelles, a quality control mechanism that is critical for counteracting the negative consequences of aging.

Disrupted autophagy has been linked to Parkinson's disease, type 2 diabetes and other disorders that appear in the elderly. Mutations in autophagy genes can cause genetic disease. Disturbances in the autophagic machinery have also been linked to cancer. Intense research is now ongoing to develop drugs that can target autophagy in various diseases.

Autophagy has been known for over 50 years but its fundamental importance in physiology and medicine was only recognized after Yoshinori Ohsumi's paradigm-shifting research in the 1990's. For
Yoshinori Ohsumi was born 1945 in Fukuoka, Japan. He received a Ph.D. from University of Tokyo in 1974. After spending three years at Rockefeller University, New York, USA, he returned to the University of Tokyo where he established his research group in 1988. He is since 2009 a professor at the Tokyo Institute of Technology.

More background on the winner and the prize

Yoshinori Ohsumi was born in Fukuoka, Japan, in 1945.  He is affiliated with the Tokyo Institute of Technology in Tokyo, Japan. His monetary award will be nearly one million dollars.

The Nobel Assembly, consisting of 50 professors at Karolinska Institutet, awards the Nobel Prize in Physiology or Medicine. Its Nobel Committee evaluates the nominations. Since 1901 the Nobel Prize has been awarded to scientists who have made the most important discoveries for the benefit of mankind.his discoveries, he is awarded this year's Nobel Prize in physiology or medicine.

Nobel Prize® is the registered trademark of the Nobel Foundation

What can we use from this in teaching undergraduate A&P?

• Consider using the Nobel Prizes as a discussion-starter in your class about 
• How science influences society
• How society influences science
• How science progresses
• Rewarding of science discoveries
• What makes a discovery "important"


• Relate this discovery to prior (or upcoming) discussions of 
• Cell function
• Organelle specialization
• How cells handle protein
• How autophagosomes work with lysosomes
• Compare/contrast with phagocytosis
• Compare/contrast with proteasome function and protein "quality control


• Relate this discovery to the general idea of cellular mechanisms of disease
• Consider taking this opportunity to emphasize "why we need to know all this" detail about cellular structure and function.

Want to know more?

Scientific Background Discoveries of Mechanisms for Autophagy

• Larsson, N-G, Msucci, M. G. Nobelprize.org accessed 8 October 2016
• A more advanced summary of the prizewinning discovery, including a handy glossary of terms.
• my-ap.us/2dHaipm

Honorary Professor Yoshinori Ohsumi wins Nobel Prize in Physiology or Medicine for 2016

• Tokyo Tech News. 3 October 2016
• Summary of biography and scientific work of the prizewinner.
• my-ap.us/2dHbyc6

Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction.

• Takeshige, K., Baba, M., Tsuboi, S., Noda, T. and Ohsumi, Y. (1992). Journal of Cell Biology 119, 301-311
• One of the scientific reports of the discovery.
• my-ap.us/2dHakO9

Isolation and characterization of autophagy-defective mutants of Saccharomyces cervisiae. 

• Tsukada, M. and Ohsumi, Y. (1993). FEBS Letters 333, 169-17
• One of the scientific reports of the discovery.
• my-ap.us/2dH9mkY

A protein conjugation system essential for autophagy. 

• Mizushima, N., Noda, T., Yoshimori, T., Tanaka, Y., Ishii, T., George, M.D., Klionsky, D.J., Ohsumi, M. and Ohsumi, Y. (1998). Nature 395, 395-398
• One of the scientific reports of the discovery.
• my-ap.us/2dHbd92

A ubiquitin-like system mediates protein lipidation.

• Ichimura, Y., Kirisako T., Takao, T., Satomi, Y., Shimonishi, Y., Ishihara, N., Mizushima, N., Tanida, I., Kominami, E., Ohsumi, M., Noda, T. and Ohsumi, Y. (2000).  Nature, 408, 488-492
• One of the scientific reports of the discovery.
• my-ap.us/2dH809y

Honoring the 2016 Nobel laureates with free access to selections of their research

• Elisa Nelissen Elsevier Connect. October 3, 2016
• This blog post provides links to download the most cited papers the laureates published with Elsevier, a major publisher of scientific journals and references.
• my-ap.us/2dH92T4

Hot Topic in Biochemistry: Role of Autophagy in Human Health and Disease

• Sharon Tooze. YouTube 20 December 2011
• Brief video of webcast presentation at the Biochemical Society Hot Topic event.
• youtu.be/0kiZdHhCtZQ

Some content, including illustrations,
is adapted from the press release
and other resources at Nobelprize.org

Dissolving Microneedle Vaccinations

Researchers recently demonstrated that a flu vaccine delivered using microneedles that dissolve in the skin can protect people against infection even better than the standard needle-delivered vaccine.

The new microneedle patch is made of dissolvable material, eliminating needle-related risks. Not to mention the sea change it may mean for patients with severe needle anxiety!  I suspect this approach may also be more tolerable for many patients than oral and nasal vaccination methods. It is also easy to use without the need for trained medical personnel—making it ideal for use where healthcare resources are limited.

“Our novel transcutaneous vaccination using a dissolving microneedle patch is the only application vaccination system that is readily adaptable for widespread practical use,” said Professor Shinsaku Nakagawa, one of the authors of the study from Osaka University. “Because the new patch is so easy to use, we believe it will be particularly effective in supporting vaccination in developing countries.”

The new microneedle patch – MicroHyala – is dissolvable in water. The tiny needles are made of hyaluronic acid, a naturally occurring substance in tissue matrix and the synovial fluid that cushions the joints. When the patch is applied sort of like a Band-Aid, the needles pierce the epidermis of skin and dissolve into the body, taking the vaccine with them.

The researchers compared the new system to traditional needle delivery by vaccinating two groups of people against three strains of influenza: A/H1N1, A/H3N2 and B. None of the subjects had a bad reaction to the vaccine, showing that it is safe to use in humans. The patch was also effective: people given the vaccine using the microneedles had an immune reaction that was equal to or stronger than those given the vaccine by injection.

“We were excited to see that our new microneedle patch is just as effective as the needle-delivered flu vaccines, and in some cases even more effective,” said Professor Nakagawa.

Previous research has evaluated the use of microneedles made of silicon or metal, but they were not shown to be safe. Microneedles made from these materials also run the risk of breaking off in the skin, leaving tiny fragments behind. The new dissolvable patch eliminates this risk because the microneedles are designed to dissolve in the skin.

What can we use from this in teaching undergraduate A&P?

• Consider mentioning this advance when discussing the layers of the skin, this giving a clinical application to pique student interest.


• When discussing immunity and vaccination, consider mentioning this discovery.


• If you discuss hyaluronic acid when covering histology, this information may help students realize the importance of knowing such details because of clinical applications of materials science.

Want to know more?

• Clinical study and stability assessment of a novel transcutaneous influenza vaccination using a dissolving microneedle patch.

• Sachiko Hirobe, et al. Biomaterials. Vol 57 (July 2015), Elsevier. doi: 10.1016/j.biomaterials.2015.04.007
• The original research article.
• my-ap.us/1eXzAud

Microneedle image courtesy of S. Nakagawa

Some content adapted from an Elsevier newsroom release

Nobel Prize 2014: Super-resolved fluorescence microscopy

The Royal Swedish Academy of Sciences has decided to award the Nobel Prize in Chemistry for 2014 to

Eric Betzig

Janelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, VA, USA,

Stefan W. Hell

Max Planck Institute for Biophysical Chemistry, Göttingen, and German Cancer Research Center, Heidelberg, Germany

and

William E. Moerner

Stanford University, Stanford, CA, USA

“for the development of
super-resolved fluorescence microscopy”

Surpassing the limitations of the light microscope

For a long time optical microscopy was held back by a presumed limitation: that it would never obtain a better resolution than half the wavelength of light. Helped by fluorescent molecules the Nobel Laureates in Chemistry 2014 ingeniously circumvented this limitation. Their ground-breaking work has brought optical microscopy into the nanodimension.

In what has become known as nanoscopy, scientists visualize the pathways of individual molecules inside living cells. They can see how molecules create synapses between nerve cells in the brain; they can track proteins involved in Parkinson’s, Alzheimer’s and Huntington’s diseases as they aggregate; they follow individual proteins in fertilized eggs as these divide into embryos.

It was all but obvious that scientists should ever be able to study living cells in the tiniest molecular detail. In 1873, the microscopist Ernst Abbe stipulated a physical limit for the maximum resolution of traditional optical microscopy: it could never become better than 0.2 micrometres. Eric Betzig, Stefan W. Hell and William E. Moerner are awarded the Nobel Prize in Chemistry 2014 for having bypassed this limit. Due to their achievements the optical microscope can now peer into the nanoworld.

Two separate principles are rewarded. 

One enables the method stimulated emission depletion (STED) microscopy, developed by Stefan Hell in 2000. Two laser beams are utilized; one stimulates fluorescent molecules to glow, another cancels out all fluorescence except for that in a nanometre-sized volume. Scanning over the sample, nanometre for nanometre, yields an image with a resolution better than Abbe’s stipulated limit.

Eric Betzig and William Moerner, working separately, laid the foundation for the second method, single-molecule microscopy. The method relies upon the possibility to turn the fluorescence of individual molecules on and off. Scientists image the same area multiple times, letting just a few interspersed molecules glow each time. Superimposing these images yields a dense super-image resolved at the nanolevel. In 2006 Eric Betzig utilized this method for the first time.

Today, nanoscopy is used world-wide and new knowledge of greatest benefit to mankind is produced on a daily basis.

This video is a brief animation of how STED works and how it improves resolution of individual particles.

This video is a longer, more detailed presentation by one of the Nobel laureates (Hell).

What can we use from this in teaching undergraduate A&P?

• Discuss how this technology has enabled us to better visualize the chemicals and structures within our cells, enabling scientists to better understand the structure and function of cell, organelles, microbiome constituents, and other structures of the human body.


• If you do a brief run-through of the theory of microscopy—perhaps in your A&P lab—you can add a mention of this technology.  


• Your textbook or other learning resource may already have an example of this type of microscopy.


• A discussion of this  Nobel Prize could evolve into a meaningful example of how science works, including how incremental improvements in classical tools for observation expand the number of questions that can be answered.


• Use the links below (and images above) to use for a handout and/or teaching slides.

Want to know more?

Resources from Nobelprize.org

• Popular Information 
• Handout: Overview information in plain English
• my-ap.us/1rh0fAJ
• Scientific Background
• Handout: More detailed information includes references to original research articles
• my-ap.us/ZdLJ69
• Advanced Information
• Handout
• my-ap.us/1rh0dsp
• Images
• Can be used in your course
• Abbe's diffraction limit
• my-ap.us/ZR0LA8
• The principle of STED microscopy
• my-ap.us/1ncRH2C
• The principle of single-molecule microscopy
• my-ap.us/1pQbAZ4
• Biographies
• Eric Betzig, 
• U.S. citizen. Born 1960 in Ann Arbor, MI, USA. Ph.D. 1988 from Cornell University, Ithaca, NY, USA. Group Leader at Janelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, VA, USA.
• http://janelia.org/lab/betzig-lab
• Stefan W. Hell, German citizen. 
• Born 1962 in Arad, Romania. Ph.D. 1990 from the University of Heidelberg, Germany. Director at the Max Planck Institute for Biophysical Chemistry, Göttingen, and Division head at the German Cancer Research Center, Heidelberg, Germany.
• http://www3.mpibpc.mpg.de/groups/hell
• William E. Moerner, U.S. citizen. 
• Born 1953 in Pleasanton, CA, USA. Ph.D. 1982 from Cornell University, Ithaca, NY, USA. Harry S. Mosher Professor in Chemistry and Professor, by courtesy, of Applied Physics at Stanford University, Stanford, CA, USA.
• http://web.stanford.edu/group/moerner

Diagrram cretit: Ganbaatar

Micrograph credit: Tesselkaffee

Text adapted from press release from Nobel Media

Nobel Prize 2014: The Brain's Positioning System

The Nobel Assembly at Karolinska Institutet has today decided to award

The 2014 Nobel Prize in Physiology or Medicine

with one half to

John O´Keefe

and the other half jointly to

May-Britt Moser and Edvard I. Moser

for their discoveries of cells that constitute a positioning 

system in the brain.

How do we know where we are? How can we find the way from one place to another? And how can we store this information in such a way that we can immediately find the way the next time we trace the same path? This year´s Nobel Laureates have discovered a positioning system, an “inner GPS” in the brain that makes it possible to orient ourselves in space, demonstrating a cellular basis for higher cognitive function.

In 1971, John O´Keefe discovered the first component of this positioning system. He found that a type of nerve cell in an area of the brain called the hippocampus that was always activated when a rat was at a certain place in a room. Other nerve cells were activated when the rat was at other places. O´Keefe concluded that these “place cells” formed a map of the room.

More than three decades later, in 2005, May-Britt and Edvard Moser discovered another key component of the brain’s positioning system. They identified another type of nerve cell, which they called “grid cells”, that generate a coordinate system and allow for precise positioning and pathfinding.

Their subsequent research showed how place and grid cells make it possible to determine position and to navigate.

The discoveries of John O´Keefe, May-Britt Moser and Edvard Moser have solved a problem that has occupied philosophers and scientists for centuries – how does the brain create a map of the space surrounding us and how can we navigate our way through a complex environment?

How do we experience our environment?

The sense of place and the ability to navigate are fundamental to our existence. The sense of place gives a perception of position in the environment. During navigation, it is interlinked with a sense of distance that is based on motion and knowledge of previous positions.

Questions about place and navigation have engaged philosophers and scientists for a long time. More than 200 years ago, the German philosopher Immanuel Kant argued that some mental abilities exist as a priori knowledge, independent of experience. He considered the concept of space as an inbuilt principle of the mind, one through which the world is and must be perceived. With the advent of behavioural psychology in the mid-20th century, these questions could be addressed experimentally. When Edward Tolman examined rats moving through labyrinths, he found that they could learn how to navigate, and proposed that a “cognitive map” formed in the brain allowed them to find their way. But questions still lingered - how would such a map be represented in the brain?

John O´Keefe and the place in space

John O´Keefe was fascinated by the problem of how the brain controls behaviour and decided, in the late 1960s, to attack this question with neurophysiological methods. When recording signals from individual nerve cells in a part of the brain called the hippocampus, in rats moving freely in a room, O’Keefe discovered that certain nerve cells were activated when the animal assumed a particular place in the environment (Figure 1). He could demonstrate that these “place cells” were not merely registering visual input, but were building up an inner map of the environment. O’Keefe concluded that the hippocampus generates numerous maps, represented by the collective activity of place cells that are activated in different environments. Therefore, the memory of an environment can be stored as a specific combination of place cell activities in the hippocampus.

May-Britt and Edvard Moser find the coordinates

May-Britt and Edvard Moser were mapping the connections to the hippocampus in rats moving in a room when they discovered an astonishing pattern of activity in a nearby part of the brain called the entorhinal cortex. Here, certain cells were activated when the rat passed multiple locations arranged in a hexagonal grid (Figure 2). Each of these cells was activated in a unique spatial pattern and collectively these “grid cells” constitute a coordinate system that allows for spatial navigation. Together with other cells of the entorhinal cortex that recognize the direction of the head and the border of the room, they form circuits with the place cells in the hippocampus. This circuitry constitutes a comprehensive positioning system, an inner GPS, in the brain (Figure 3).

A place for maps in the human brain

Recent investigations with brain imaging techniques, as well as studies of patients undergoing neurosurgery, have provided evidence that place and grid cells exist also in humans. In patients with Alzheimer´s disease, the hippocampus and entorhinal cortex are frequently affected at an early stage, and these individuals often lose their way and cannot recognize the environment. Knowledge about the brain´s positioning system may, therefore, help us understand the mechanism underpinning the devastating spatial memory loss that affects people with this disease.

The discovery of the brain’s positioning system represents a paradigm shift in our understanding of how ensembles of specialized cells work together to execute higher cognitive functions. It has opened new avenues for understanding other cognitive processes, such as memory, thinking and planning.

What can we use from this in teaching undergraduate A&P?

• The role of the hippocampus and it's place cells could be briefly discussed as you explore the cognitive functions of the brain.


• A discussion of this year's Nobel Prize could evolve into a meaningful example of how science works, including the use of discoveries in animals that can later be applied to learning more about human structure and function.


• Information revealed by this discovery could be discussed when discussing human disorders, such as Alzheimer disease, that involve impairments of spatial orientation and/or place memory.

Want to know more?

Here's a video in which May-Britt Moser and Edvard I. Moser explain their research, which you can use in your course discussion.

2014 Nobel Prize announcement

• Official announcement, which includes photos of the laureates and links to related information.
• my-ap.us/1oJH82y

Scientific Background: The Brain’s Navigational Place and Grid Cell System

• Nobelprize.org accessed 6 October 2014
• Plain English hand-out that can be used with your students.  Illustrated with clear diagrams.
• my-ap.us/1pGLVlm

Nobel Prize in Medicine Is Awarded for Discovery of Brain’s ‘Inner GPS’

• L. Altman The New York Times. OCT. 6, 2014
• Plain English article summarizing the discoveries.
• my-ap.us/10ELy5h

The hippocampus as a spatial map. Preliminary evidence from unit activity in the freely‐moving rat.

• O'Keefe, J., and Dostrovsky, J. (1971). Brain Research 34, 171-175.
• Original research paper describing key discoveries for which this prize is given.
• my-ap.us/1s4fi5Z

Place units in the hippocampus of the freely moving rat.

• O´Keefe, J. (1976). Experimental Neurology 51, 78-109.
• Original research paper describing key discoveries for which this prize is given.
• my-ap.us/1s2NYGd

Spatial representation in the entorhinal cortex.

• Fyhn, M., Molden, S., Witter, M.P., Moser, E.I., Moser, M.B. (2004)  Science 305, 1258-1264.
• Original research paper describing key discoveries for which this prize is given.
• my-ap.us/1BIvdI4

Microstructure of spatial map in the entorhinal cortex.

• Hafting, T., Fyhn, M., Molden, S., Moser, M.B., and Moser, E.I. (2005). Nature 436, 801-806.
• Original research paper describing key discoveries for which this prize is given.
• my-ap.us/1nX0jLe

Article adapted from Nobel Media press release

New knee ligament confirmed

It's been there all along.  In most of us, at least.  Back in 1879, French surgeon Paul Ferdinand Segond first described it as it related to a particular type of avulsion fracture of the knee—the Segond fracture. But it was never really confirmed as separate from the joint capsule and named as a normal ligament of the human knee.  Until now.

Dubbed the anterolateral ligament (ALL), it originates at the prominence of the lateral femoral epicondyle (just anterior to the lateral collateral ligament) and running obliquely to the anterolateral part of the tibia (attached at the lateral meniscus).

Segond

So maybe we should pencil the ALL into our anatomic atlases, eh?  And wait for some research to confirm its biomechanical function—probably related to controlling internal rotation of the tibia.

This might also provide a good opportunity to talk about the dynamic nature of anatomical science—and the fact that human anatomy is not "finished."



Want to know more?

Anatomy of the anterolateral ligament of the knee

• Steven Claes et al. Journal of Anatomy. Volume 223, Issue 4, pages 321–328, October 2013 (First published online: 1 AUG 2013) DOI: 10.1111/joa.12087
• This the original journal article (free abstract).
• my-ap.us/1aFUVV3

The Anterolateral Ligament of the Knee: Anatomy, Radiology, Biomechanics and Clinical Implications

• Steven Claes, et al. American Academy of Orthopedic Surgeons (AAOS) Annual Meeting, SE73, 20 March 2013
• This is an abstract (with image) of a preliminary presentation giving prior to journal publication.
• my-ap.us/1b7bU0Q

Photo of the ALL

• Steven Claes, et al. American Academy of Orthopedic Surgeons (AAOS) Annual Meeting, SE73, 20 March 2013
• my-ap.us/1cF4sgC

Diagram of ALL

• Kevin Patton, The A&P Professor Image Library, published 7 Nov 2013
• Diagram you can use in your course to highlight the ALL
• theapprofessor.org/graphics/ALL_Kpatton.fw.png

Virginia Johnson Masters, sex research pioneer, dead at 88

On Wednesday of this week, just a few miles from my home in Missouri, Virginia Johnson Masters passed away at age 88.

Most of you are aware of the pioneering work in human sexual physiology she and her late ex-husband, William Masters, undertook at Washington University in St. Louis during the mid-20th century.  I briefly underscored that work in several of my textbooks:

"The study of human reproduction, and especially sexual function, has many cultural implications. So it is no wonder that American researchers William Masters and Virginia Johnson encountered a great deal of controversy during their decades of pioneering work in the field of human sex and reproduction. They were the first to study human sexual physiology in the laboratory. William Masters was a gynecologist (physician specializing in women's health) and Virginia Johnson was a psychologist. In 1966, their book Human Sexual Response clearly explained the physiology of sex for the first time. Besides making discoveries in the physiology of human sex and reproduction, they also developed therapies for treating sex-related conditions, and they trained therapists from around the world. In addition to the broad fields of biology, medicine, psychology, and the behavioral sciences, the pioneering work of Masters and Johnson paved the way for advances in such diverse and specialized areas of knowledge as comparative neuroscience and social dynamics. Today, there are many opportunities to apply knowledge of reproductive science in a variety of professions."

You may also recall my previous article Masters of Sex, in which I related some of my experiences with Johnson's late ex-husband and collaborator, Bill Masters.

With the Showtime network about to debut their new miniseries Masters of Sex, in which the character of Virginia Johnson plays a pivotal role, students will likely be bringing their curiosity about Masters and Johnson's work to their A&P courses.

Want to know more?

Virginia Johnson, Widely Published Collaborator in Sex Research, Dies at 88

• By MARGALIT FOX
• The New York Times Published: July 25, 2013
• Detailed obituary
• my-ap.us/13jaA4r

Masters of Sex

• by Kevin Patton
• The A&P Professor May 12, 2009
• Brief article about Masters, Johnson, the recent book about them (on which the Showtime series is based), and Masters's unforgettable presentation at the HAPS Conference in 1995
• my-ap.us/18HBhYx

Masters of Sex

• by Thomas Maier
• Basic Books April 13, 2009 432 p.
• An amazing book about Masters and Johnson's story.  HIGHLY recommended reading for all A&P teachers!
• amzn.to/12sLRQb

Related textbook content

• Anatomy & Physiology 8th ed.  Chapters 34 and 35 my-ap.us/QZTbK1
• Essentials of Anatomy & Physiology Chapters 24 and 25 my-ap.us/SCfNlj  
• The Human Body in Health and Disease 6th ed. Chapter 23 (see bio on p. 610-611) my-ap.us/X71LJO 
• Structure & Function of the Body 14th ed. Chapter 23 (see bio on p. 459) http://my-ap.us/10s50MH

Rita Levi-Montalcini, growth factor pioneer

Yesterday, the scientific community lost another of its great people, Rita Levi-Montalcini.

In The Human Body in Health & Disease and Structure & Function of the Body, I wrote this about Levi-Montalcini:

Rita Levi-Montalcini had just finished a medical degree in her native Italy when in 1938 the Fascist government under Mussolini barred all “non-Aryans” from working in academic and professional careers. Being Jewish, Levi-Montalcini was forced to move to Belgium to work. But when Belgium was about to be invaded by the Nazis, she decided to return home to Italy and work in secret. Her home laboratory was very crude, but in it she made some important discoveries about how the nervous system develops during embryonic development. After World War II, she was invited to Washington University in St. Louis to work. There, she discovered the existence of nerve growth factor (NGF), for which she later won the 1986 Nobel Prize. Her discovery of a chemical that regulates the growth of new nerves during early brain development has led to many different paths of investigation. For example, by learning more about growth regulators we now know more about how the nervous system develops, as well as other tissues, organs, and systems of the body.

Note that I put in a little plug for my hometown of St. Louis, where we continue to be proud of this remarkable woman and her pioneering work.

As I said in a recent post about the passing of transplant pioneer Joseph Murray, I think the occasional story of a pioneer in the history of human science adds a lot to the A&P course.  Such stories give a human dimension to the pursuit of science and provide the context needed for students to understand how we know what we know.  Levi-Montalcini's story gives us the further opportunities to weave into our courses the themes of global collaboration among the scientific community as the role of women in science.

Want to know more?

• Nobel Scientist Rita Levi-Montalcini Dies in Rome
• U.S. News & World Report online December 30, 2012
• [Plain-English obituary]
• http://my-ap.us/S1RKyW
  
  
• Oldest Nobel winner Rita Levi-Montalcini dies at 103
• Euronews at YouTube accessed 31 Dec 2012
• [Very brief video announcing the death and her contributions.]
• http://youtu.be/SXjt5GI5qEQ
  
  
• Nobel Lecture by Rita Levi-Montalcini 
• Media Player at Nobelprize.org
• [Full video (in English) of Nobel lecture by Rita Levi-Montalcini in which she fully credits "good luck"; 57 minutes]
• http://my-ap.us/Vf6sPz
  
  
• Rita Levi-Montalcini Interview
• Adam Smith, Editor-in-Chief of Nobelprize.org.
• Nobel Interview, November 2008
• [Video interview with Rita Levi-Montalcini, who talks about her daily work, why she had to make a laboratory in her bedroom to conduct research during World War II (3:06), the benefits of working in isolation (5:03), her post-war move to the United States (6:25), her work with Stanley Cohen and the discovery of nerve growth factor (7:15), the roles of intuition and chance in biological research (15:14), her current research (16:58), her advice to young scientists (17:41), and why this period of her life has been the best so far (28:10).]
• http://my-ap.us/Ug6gA5
  
  
• The Nobel Prize in Physiology or Medicine 1986 Press Release
• Nobelprize.org
• [Detailed news release that includes some simple diagrams that help illustrate the concepts involved.]
• http://my-ap.us/ZPyacv
  

• In Praise of Imperfection: My Life and Work

• Rita Levi-Montalcini
• Sloan Foundation Science Series, October 1989
• [Her autobiography]
• http://amzn.to/Wgjk7b

Related textbook content

• Anatomy & Physiology 8th ed.  p. 409, 1111-1113, A&P Connect: The Nobel Legacy my-ap.us/QZTbK1

• Essentials of Anatomy & Physiology p. 231-232, 241, 610-612 my-ap.us/SCfNlj  

• The Human Body in Health and Disease 5th ed. p. 236-237, 644-645, 658 my-ap.us/fNN00N 

• Structure & Function of the Body 14th ed. p. 168-169, 472-473 my-ap.us/X6QxqE

Photo: Presidenza della Repubblica Italiana