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CIT ID: 6729
Program date: Tuesday, May 06, 2008, 8:00:00 AM
Presented by: NIH

Abstract:

The goal of the symposium is to understand the current state of basic and clinical pluripotent stem cell biology to help the National Institutes of Health (NIH) prioritize research with the greatest potential for clinical benefit. The symposium will enable NIH to determine which areas of high-priority research need to be emphasized and to develop additional Funding Opportunity Announcements to increase research in these areas.

For more information, visit
http://guest.cvent.com/EVENTS/Info/Summary.aspx?e=40331195-f7f7-44cb-80c9-4a4a87330300

Audio Podcasts				Video Podcasts
	Description	Runtime			Description	Runtime
	Enhanced Audio Podcast - Part 1	1:59:06			Enhanced Video Podcast - Part 1	1:59:06
	Enhanced Audio Podcast - Part 2	2:20:04			Enhanced Video Podcast - Part 2	2:20:04
	Enhanced Audio Podcast - Part 3	2:26:05			Enhanced Video Podcast - Part 3	2:26:05

CIT ID: 6189
Program date: Monday, May 05, 2008, 12:00:00 PM
Presented by: E.J. Chichilnisky, Ph.D., The Salk Institute

Abstract:

Dr. Chichilnisky is an associate professor in the Systems Neurobiology Laboratories at the Salk Institute for Biological Studies. His laboratory focuses on how the retina processes visual information and transmits this information to the brain. This is accomplished by using a state-of-the-art 512-electrode recording system that allows the monitoring of hundreds of cells at once while stimulating the retina with spatial and temporal patterns of light. A key current area of interest is how retinal neurons collectively communicate visual motion information to areas of the brain responsible for motion perception and behavior guided by motion. A long-term goal of the research is to contribute to development of visual prosthetics, devices that could be implanted in the eye and substitute for retinal tissue damaged by disease or other trauma.

NIH Neuroscience Seminar Series

Audio Podcasts				Video Podcasts
	Description	Runtime			Description	Runtime
	Enhanced Audio Podcast	1:06:10			Enhanced Video Podcast	1:06:10

CIT ID: 6221
Program date: Wednesday, April 30, 2008, 3:00:00 PM
Presented by: Elaine Fuchs, Rockefeller University

Abstract:

Stem cells can self-renew and differentiate along multiple lineages to generate different tissues. In the embryo, multipotent stem cells respond to various cues to undergo morphogenesis and produce these tissues. The epidermis of the skin is an excellent model to explore how multipotent stem cells are able to respond to different cues to generate three functional tissues: epidermis, sebaceous gland and hair follicles. In the adult, stem cells reside in the epidermal basal layer, at the base of the sebaceous gland and in a niche within the hair follicle known as the bulge. Despite intensive studies, we still know very little about how stem cells and these niches become established and maintained. Genetic marking and molecular approaches stem cells within the bulge typically cycle infrequently. In response to a skin injury, these stem cells can be mobilized to move upward, proliferate and repair epidermal wounds or replenish the sebaceous gland. In normal homeostasis, these stem cells fuel the hair cycle, where they become activated to proliferate and regenerate the hair follicle with each new anagen phase. It has been known for nearly a decade that that the transition from dormant to activated follicle stem cells involves changes in signaling by Wnts, BMPs, and other factors but the molecular details of the activation and commitment steps are still unfolding. My laboratory has used a combination of molecular, cellular continues to study the molecular mechanisms that underlie follicle stem cell activation, and in so doing have begun to realize that when sustained through genetic mutations, the pathways involved in stem cell activation lead to tumo igenesis and skin cancers

Elaine Fuchs is internationally recognized for her contributions to skin biology and its human genetic disorders, including skin cancers and life-threatening genetic syndromes such as blistering skin disorders. For nearly three decades, Fuchs has focused on the molecular mechanisms that underlie the morphogenesis of the epidermis and its appendages, and how perturbations of these mechanisms result in disease. She has systematically and skillfully devised innovative molecular approaches to tackle these problems. She is credited for her pioneering use of “reverse genetics,” an approach to start with a specific protein, study its biology and then use mice as a means to ultimately identify the genes responsible for inherited human disorders. A classical geneticist would start with a specific genetic disorder. Instead, Fuchs has employed this creative cell biological strategy to solve the genetic bases of a number of dermatological disorders in humans. The method has since broadly benefited human medical genetics. Fuchs is widely recognized as having brought the field of dermatological research into modern day science. Her contributions range from the identification of proteins and signal transduction pathways important in epidermal and hair functions to uncovering of the molecular nature of skin diseases in humans. Fuchs and coworkers identified genetic defects in several disorders from perturbations of cytoskeletal proteins related to those present in the skin, but whose expression resides outside the skin, particularly in the muscle and the nervous system. An elegant example is reverse genetics to uncover the underlying genetic basis of blistering human skin disorder that arises from defects in epidermal keratin genes. Her 10 years of prior research set the groundwork for this discovery, which uncovered a key function of intermediate filament (IF) proteins as mechanical integrators of the cytoskeleton. The work also set the paradigm for >20 different human disorders of IF genes that affect many different tissues of the body. Her ground-breaking research is often used in biolgy and medical textbooks as a landmark

http://www.hhmi.org/research/investigators/fuchs_bio.html

WALS

Audio Podcasts				Video Podcasts
	Description	Runtime			Description	Runtime
	Enhanced Audio Podcast	1:14:14			Enhanced Video Podcast	1:14:14

CIT ID: 6732
Program date: Monday, April 28, 2008, 3:00:00 PM
Presented by: Aaron Ciechanover, 2004 Nobel Prize in Chemistry

Abstract:

Special WALS on Monday

Between the sixties and eighties, most life scientists focused their attention on studies of nucleic acids and the translation of the coded information. Protein degradation was a neglected area, considered to be a non-specific, dead-end process. While it was known that proteins do turn over, the large extent and high specificity of the process - whereby distinct proteins have half-lives that range from a few minutes to several days - was not appreciated. The discovery of the lysosome by Christian de Duve did not significantly change this view, as it was clear that this organelle is involved mostly in the degradation of extracellular proteins, and their proteases cannot be substrate-specific. The discovery of the complex cascade of the ubiquitin pathway revolutionized the field. It is clear now that degradation of cellular proteins is a highly complex, temporally controlled, and tightly regulated process that plays major roles in a variety of basic pathways during cell life and death, and in health and disease. With the multitude of substrates targeted, and the myriad processes involved, it is not surprising that aberrations in the pathway are implicated in the pathogenesis of many diseases, certain malignancies and neurodegeneration among them. Degradation of a protein via the ubiquitin/proteasome pathway involves two successive steps: (a) conjugation of multiple ubiquitin moieties to the substrate, and (b) degradation of the tagged protein by the downstream 26S proteasome complex. Despite intensive research, the unknown still exceeds what we currently know on intracellular protein degradation, and major key questions remain unsolved.

Among these are the modes of specific and timed recognition for the degradation of the many substrates, and the mechanisms that underlie aberrations in the system that lead to pathogenesis of diseases. The recent discovery of modification by ubiquitin-like proteins along with identification of “non-canonical” polyubiquitin chains that serve non-proteolytic functions, have broadened the scope of the system beyond proteolysis and set new challenges in for biologists and proteomic experts. Major challenges in the field are clearly (i) identification of the cellular proteins tagged by ubiquitin and ubiquitin-like proteins, (ii) identification of the downstream elements recognized by these chains, and (iii) deciphering the structure of the different ubiquitin and ubiquitin-like chains that tag the different proteins.

Aaron Ciechanover was born in Haifa, Israel in 1947. He is currently a Distinguished Research Professor in the Faculty of Medicine of the Technion-Israel Institute of technology in Haifa, Israel. He received his M.Sc. (1971) and M.D. (1975) from the Hebrew University in Jerusalem, Israel, and his D.Sc. (1982) from the Technion. There, as a graduate student with Dr. Avram Hershko and in collaboration with Dr. Irwin A. Rose from the Fox Chase Cancer Center in Philadelphia, Pennsylvania, USA, they discovered that covalent attachment of ubiquitin to the target substrate signals it for degradation. They deciphered the mechanism of conjugation in a cell-free system, described the general proteolytic function of the system in cells, and proposed a model according to which this modification serves as a recognition signal for a specific downstream protease. As a post doctoral fellow with Dr. Harvey Lodish at M.I.T., he continued his studies on the ubiquitin system and made additional important discoveries. Among the many prizes that Dr. Ciechanover received are the 2000 Albert Lasker Award for Basic Medical Research, the 2003 Israel Prize in Biology and the 2004 Nobel Prize in Chemistry.

http://www.technion.ac.il/_root/Pages/Nobel/nobel.html

WALS

Audio Podcasts				Video Podcasts
	Description	Runtime			Description	Runtime
	Enhanced Audio Podcast	1:07:57			Enhanced Video Podcast	1:07:57

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