Welcome to LabTV! If you haven’t already, take a look at this video. I hope you will enjoy meeting the first young scientist featured in this brand new series that I’ve chosen to highlight on my blog. The inspiration for LabTV comes from Jay Walker, who is the founder of PriceLine, and curator and chairman of TEDMED, an annual conference focused on new ideas in health and medicine.
A few years ago, Walker noticed that there were many talented young people across America who are interested in science, but are uncertain about what a career in biomedical research is like. His solution was to create an online video community where anyone interested in going into research could learn from the experiences of scientists who, not so long ago, walked in their shoes. As you will see from spending a few moments in the lab with Heardley Moses Murdock, whose research involves a rare immune disorder called DOCK 8 deficiency, these video profiles put a human face on science and show its everyday stories.
Bill Bement describes himself as a guy who “passionately, obsessively, and almost feverishly” loves to study cells. His excitement comes through in our final installment of the American Society for Cell Biology’s Celldance 2014. Bement, an NIH grantee at the University of Wisconsin, Madison, shares his scanning confocal microscope with us for this fascinating glimpse into the rapid response of cells to repair holes, tears, and other structural damage in their protective outer membranes.
For most people, this damage response runs on biochemical autopilot, sealing any membrane break within seconds to keep the cell viable and healthy. But some people inherit gene mutations that make sealing and patching difficult, particularly in cells that operate under repetitive mechanical stress. For example, some forms of muscular dystrophy stem specifically from an inherited inability to repair breaks in the cell membrane of skeletal muscle cells. In one type of disease that affects both skeletal and cardiac muscle, a gene mutation alters the shape of a protein called dysferlin, which normally binds annexin proteins that, as noted in the video, play a vital role in patching holes. In the presence of a glitch in dysferlin, the rapid chain of biochemical events needed to enable such repair breaks down.
There’s still an enormous amount to learn about cell membrane repair, so it will be interesting to see what Bement’s microscope and camera will show us next.
Caption: Schematic of how the clot retriever used in the reported trials is opened inside a blood vessel to surround a clot that is blocking blood flow. Once caught by the stent, the entire apparatus with the clot is removed from the body out a small puncture in the femoral artery at the groin. Credit: Covidien
Despite the recent progress we’ve made in preventing stroke by such steps as controlling weight, lowering blood pressure, and stopping smoking, nearly 700,000 Americans suffer clot-induced, or ischemic, strokes every year . So, I’m very pleased to report that, thanks to years of rigorous research and technological development, we’ve turned a major corner in the emergency treatment of this leading cause of death and disability.
The most severe strokes—those that can cause lifelong loss of independent function—are often due to blood clots that suddenly enter and block one of the main arteries supplying blood flow to the brain. No less than four large, randomized clinical trials recently reported results showing, for the first time, that using catheters to remove large clots from cerebral arteries can restore blood flow and halt further damage to the brains of patients with acute strokes. In fact, the stent-based retrievers and other mechanical approaches used to remove stroke-causing clots proved so effective, that three of the four trials were stopped early, allowing the results to be made swiftly available to medical professionals and the public.
It may surprise you to learn that the poised young woman featured in this video was a sophomore in high school at the time the film was made. Today, Emily Ashkin is a high school senior with impressive laboratory experience and science awards to her name. As it happens, she’s also introducing me when I deliver a keynote address at the Melanoma Research Alliance’s annual scientific meeting — today, here in Washington, D.C.
What struck me most when I heard Emily’s story was her fearlessness. When mentoring young students, helping some to believe in themselves can be a real challenge. Not Emily. She faces her challenges by seeking solutions, asking—as she does in the video—“Why can’t that be me?”
When Amy Gladfelter arrived at the University of Basel in Switzerland to pursue post-doctoral work in 2001, she remembers that her research interests were still a little up in the air. As she settled into the new lab, Gladfelter remembers watching movies that others had made of the filamentous fungus Ashbya gossypii and wondering how on earth its myriad nuclei could share the same cytoplasm and do different things. Now, more than a decade later, this cell biologist finds herself at Dartmouth College, Hanover, N.H., where she is leading a lab that is making its own thought-provoking movies and pushing the envelope in an effort to answer this and many other scientific questions.
As you’ll learn by watching this video, Gladfelter’s work has implications far beyond the world of fungi because the filamentous proteins called septins, which act to define territory within Ashbya cells, are very similar to certain proteins found in human cells. While such proteins are normally very flexible, they can morph into toxic, solid states in certain human disorders, including Alzheimer’s disease and Huntington’s disease. Besides illustrating the value of Ashbya for uncovering clues to neurodegenerative disorders, this video delivers a broader message about the importance of all kinds of model organisms for efforts to understand our own biology.