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Revision as of 05:07, 13 January 2025 by Gacggt (talk | contribs)(diff) ← Previous revision | Latest revision (diff) | Newer revision → (diff) American biomedical scientist (born 1961)| David J. Glass | |
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| Born | 1961 (age 63–64) |
| Education | Columbia University (BS, MD) |
| Occupation | Biomedical scientist |
| Employer | Regeneron |
David J. Glass (born 1961) is a American biomedical scientist who led the skeletal muscle group, before stepping into his more recent role of VP of research, Aging/Age-Related Disorders, at Regeneron Pharmaceuticals.
Glass is a member of the National Academy of Sciences, and the holder of more than 35 patents. He is known for characterizing the mechanisms by which skeletal muscle undergoes atrophy and hypertrophy. Cite error: A <ref> tag is missing the closing </ref> (see the help page).
Earlier, he helped to identify the mechanism by which muscles connect to nerves..
He also cloned receptors for neurotrophic factors, such as TrkB, the receptor for BDNF, and showed that they were sufficient to mediate signaling without the requirement of the Low affinity Nerve Growth Factor receptor (LNGFR).
Glass and his colleagues, including George Yancopoulos discovered a receptor tyrosine kinase which they named "MuSK" (Muscle Specific Kinase, or MuSK protein). They went on to show that MuSK is required for the formation of the neuromuscular junction, the key structure which allows motor neurons to induce skeletal muscle to contract. They next demonstrated that the ligand for MuSK is agrin, a protein secreted by the motor neuron to induce formation of the neuromuscular junction.
He identified the E3 ubiquitin ligases, MuRF1 and MAFbx, which are upregulated during skeletal muscle atrophy; mouse which were null for these ligases were protected from loss of muscle under atrophic conditions. .
Key Papers
- Glass DJ, Nye SH, Hantzopoulos P, et al. (July 1991). "TrkB mediates BDNF/NT-3-dependent survival and proliferation in fibroblasts lacking the low affinity NGF receptor". Cell. 66 (2): 405–13. doi:10.1016/0092-8674(91)90629-D. PMID 1649703. S2CID 43626580.
- DeChiara TM, Bowen DC, Valenzuela DM, et al. (May 1996). "The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo". Cell. 85 (4): 501–12. doi:10.1016/S0092-8674(00)81251-9. PMID 8653786. S2CID 17455481.
- Glass DJ, Bowen DC, Stitt TN, et al. (May 1996). "Agrin acts via a MuSK receptor complex". Cell. 85 (4): 513–23. doi:10.1016/S0092-8674(00)81252-0. PMID 8653787. S2CID 14930468.
References
- Template:Cite url=https://data.the-asci.org/controllers/asci/DirectoryController.php?action=profile&entryId=500433
- "David Glass".
- Template:Cite url=https://skeletalmusclejournal.biomedcentral.com/articles/10.1186/s13395-024-00343-5
- "How Nerve Meets Muscle and Begins to Talk". New York Times. May 21, 1996. Retrieved May 1, 2011.
- Glass DJ, Nye SH, Hantzopoulos P, et al. (July 1991). "TrkB mediates BDNF/NT-3-dependent survival and proliferation in fibroblasts lacking the low affinity NGF receptor". Cell. 66 (2): 405–13. doi:10.1016/0092-8674(91)90629-D. PMID 1649703. S2CID 43626580.
- DeChiara TM, Bowen DC, Valenzuela DM, et al. (May 1996). "The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo". Cell. 85 (4): 501–12. doi:10.1016/S0092-8674(00)81251-9. PMID 8653786. S2CID 17455481.
- Glass DJ, Bowen DC, Stitt TN, et al. (May 1996). "Agrin acts via a MuSK receptor complex". Cell. 85 (4): 513–523. doi:10.1016/S0092-8674(00)81252-0. PMID 8653787. S2CID 14930468.
- https://www.science.org/doi/10.1126/science.1065874?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub%20%200pubmed.
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