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{{short description|American biomedical scientist (born 1961)}} {{AfC submission|T}}{{short description|American biomedical scientist (born 1961)}}
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'''David J. Glass''' (born 1961) is a ] biomedical scientist who led the ] group, before stepping into his more recent role of VP of research, Aging/Age-Related Disorders, at ].<ref>{{cite url=https://data.the-asci.org/controllers/asci/DirectoryController.php?action=profile&entryId=500433}}</ref> '''David J. Glass''' (born 1961) is an ] biomedical scientist who led ]'s ] group, before stepping into his more recent role of VP of research, Aging/Age-Related Disorders, at ].<ref>{{cite|url=https://data.the-asci.org/controllers/asci/DirectoryController.php?action=profile&entryId=500433}}</ref>


Glass is a member of the ], and the holder of more than 35 patents.<ref>{{cite news |title=David Glass |url=https://patents.google.com/?q=(David+Glass)&assignee=Regeneron&oq=David+Glass+Regeneron}}</ref> He is known for characterizing the mechanisms by which ] undergoes ] and ]. <ref>{{cite url=https://skeletalmusclejournal.biomedcentral.com/articles/10.1186/s13395-024-00343-5}}</ref><ref>{ Glass is a member of the ], and the holder of more than 35 patents.<ref>{{cite news |title=David Glass |url=https://patents.google.com/?q=(David+Glass)&assignee=Regeneron&oq=David+Glass+Regeneron}}</ref> He is known for characterizing the mechanisms by which ] undergoes ] and ]. <ref>{{cite|url=https://skeletalmusclejournal.biomedcentral.com/articles/10.1186/s13395-024-00343-5}}</ref>
==Scientific career== ==Scientific career==
He was elected to both the ]<ref name = "SA" /> and the ]. Earlier, he was elected to the American Society for Clinical Investigation. <ref>{{Cite web|url=https://the-asci.org/controllers/asci/DirectoryController.php?action=bySpecialty&specialtyId=79}}</ref> He was elected to both the ]<ref name = "SA" /> and the ]. Earlier, he was elected to the American Society for Clinical Investigation. <ref>{{Cite web|url=https://the-asci.org/controllers/asci/DirectoryController.php?action=bySpecialty&specialtyId=79}}</ref>


Earlier, he helped to identify the mechanism by which muscles connect to nerves.<ref>{{cite news |title=How Nerve Meets Muscle and Begins to Talk |url=https://www.nytimes.com/1996/05/21/science/how-nerve-meets-muscle-and-begins-to-talk.html |newspaper=New York Times |date=May 21, 1996 |access-date=May 1, 2011}}</ref>. Glass helped to identify the mechanism by which muscles connect to nerves.<ref>{{cite news |title=How Nerve Meets Muscle and Begins to Talk |url=https://www.nytimes.com/1996/05/21/science/how-nerve-meets-muscle-and-begins-to-talk.html |newspaper=New York Times |date=May 21, 1996 |access-date=May 1, 2011}}</ref>.


He also cloned receptors for neurotrophic factors, such as ], the receptor for BDNF, and showed that they were sufficient to mediate signaling without the requirement of the Low affinity Nerve Growth Factor receptor (]).<ref name="pmid1649703">{{cite journal |vauthors=Glass DJ, Nye SH, Hantzopoulos P, etal |title=TrkB mediates BDNF/NT-3-dependent survival and proliferation in fibroblasts lacking the low affinity NGF receptor |journal=Cell |volume=66 |issue=2 |pages=405–13 |date=July 1991 |pmid=1649703 |doi=10.1016/0092-8674(91)90629-D|s2cid=43626580 }}</ref> He also cloned receptors for neurotrophic factors, such as ], the receptor for BDNF, and showed that they were sufficient to mediate signaling without the requirement of the Low affinity Nerve Growth Factor receptor (]).<ref name="pmid1649703">{{cite journal |vauthors=Glass DJ, Nye SH, Hantzopoulos P, etal |title=TrkB mediates BDNF/NT-3-dependent survival and proliferation in fibroblasts lacking the low affinity NGF receptor |journal=Cell |volume=66 |issue=2 |pages=405–13 |date=July 1991 |pmid=1649703 |doi=10.1016/0092-8674(91)90629-D|s2cid=43626580 }}</ref>
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Glass and his colleagues, including ] discovered a ] which they named "MuSK" (Muscle Specific Kinase, or ]). They went on to show that MuSK is required for the formation of the ], the key structure which allows motor neurons to induce skeletal muscle to contract.<ref name="pmid8653786">{{cite journal |vauthors=DeChiara TM, Bowen DC, Valenzuela DM, etal |title=The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo |journal=Cell |volume=85 |issue=4 |pages=501–12 |date=May 1996 |pmid=8653786 |doi=10.1016/S0092-8674(00)81251-9|s2cid=17455481 |doi-access=free }}</ref> They next demonstrated that the ligand for MuSK is ], a protein secreted by the ] to induce formation of the neuromuscular junction.<ref name="pmid8653787">{{cite journal |vauthors=Glass DJ, Bowen DC, Stitt TN, etal |title=Agrin acts via a MuSK receptor complex |journal=Cell |volume=85 |issue=4 |pages=513–523 |date=May 1996 |pmid=8653787 |doi=10.1016/S0092-8674(00)81252-0|s2cid=14930468 |doi-access=free }}</ref> Glass and his colleagues, including ] discovered a ] which they named "MuSK" (Muscle Specific Kinase, or ]). They went on to show that MuSK is required for the formation of the ], the key structure which allows motor neurons to induce skeletal muscle to contract.<ref name="pmid8653786">{{cite journal |vauthors=DeChiara TM, Bowen DC, Valenzuela DM, etal |title=The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo |journal=Cell |volume=85 |issue=4 |pages=501–12 |date=May 1996 |pmid=8653786 |doi=10.1016/S0092-8674(00)81251-9|s2cid=17455481 |doi-access=free }}</ref> They next demonstrated that the ligand for MuSK is ], a protein secreted by the ] to induce formation of the neuromuscular junction.<ref name="pmid8653787">{{cite journal |vauthors=Glass DJ, Bowen DC, Stitt TN, etal |title=Agrin acts via a MuSK receptor complex |journal=Cell |volume=85 |issue=4 |pages=513–523 |date=May 1996 |pmid=8653787 |doi=10.1016/S0092-8674(00)81252-0|s2cid=14930468 |doi-access=free }}</ref>


He identified the ], ] and ], which are upregulated during skeletal muscle atrophy; mouse which were null for these ligases were protected from loss of muscle under atrophic conditions. <ref>{{cite web| url =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}}</ref>. He identified the ], ] and ], which are upregulated during skeletal muscle atrophy; mice which are null for these ligases were found to have less loss of muscle under atrophic conditions. <ref>{{cite web| url =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}}</ref>.

== Book ==

He is the author of a book aimed at teaching students how to design biology experiments, titled "Experimental Design for Biologists." The book is in its 2nd edition, published by ]. <ref>{{cite web| url =https://www.cshlpress.com/default.tpl?cart=1736745146262901944&fromlink=T&linkaction=full&linksortby=oop_title&--eqSKUdatarq=1020}}</ref>.

==Journal==

Glass was the founding editor-in-chief of the ] journal ''Skeletal Muscle.'' <ref>{{cite web| url =https://skeletalmusclejournal.biomedcentral.com}}</ref>.

== Key Papers == == Key Papers ==


*{{cite journal |vauthors=Glass DJ, Nye SH, Hantzopoulos P, etal |title=TrkB mediates BDNF/NT-3-dependent survival and proliferation in fibroblasts lacking the low affinity NGF receptor |journal=Cell |volume=66 |issue=2 |pages=405–13 |date=July 1991 |pmid=1649703 |doi=10.1016/0092-8674(91)90629-D|s2cid=43626580 }} *{{cite journal |vauthors=Glass DJ, Nye SH, Hantzopoulos P, etal |title=TrkB mediates BDNF/NT-3-dependent survival and proliferation in fibroblasts lacking the low affinity NGF receptor |journal=Cell |volume=66 |issue=2 |pages=405–13 |date=July 1991 |pmid=1649703 |doi=10.1016/0092-8674(91)90629-D|s2cid=43626580 }}
*{{cite journal |vauthors=DeChiara TM, Bowen DC, Valenzuela DM, etal |title=The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo |journal=Cell |volume=85 |issue=4 |pages=501–12 |date=May 1996 |pmid=8653786 |doi=10.1016/S0092-8674(00)81251-9|s2cid=17455481 |doi-access=free }} *{{cite journal |vauthors=DeChiara TM, Bowen DC, Valenzuela DM, etal |title=The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo |journal=Cell |volume=85 |issue=4 |pages=501–12 |date=May 1996 |pmid=8653786 |doi=10.1016/S0092-8674(00)81251-9|s2cid=17455481 |doi-access=free }}
*{{cite journal |vauthors=Glass DJ, Bowen DC, Stitt TN, etal |title=Agrin acts via a MuSK receptor complex |journal=Cell |volume=85 |issue=4 |pages=513–23 |date=May 1996 |pmid=8653787 |doi=10.1016/S0092-8674(00)81252-0|s2cid=14930468 |doi-access=free }} *{{cite journal |vauthors=Glass DJ, Bowen DC, Stitt TN, etal |title=Agrin acts via a MuSK receptor complex |journal=Cell |volume=85 |issue=4 |pages=513–23 |date=May 1996 |pmid=8653787 |doi=10.1016/S0092-8674(00)81252-0|s2cid=14930468 |doi-access=free }}
*{{cite journal |vauthors=Bodine S, Stitt TN, Gonzalez M, Kline WO, Stover GL, Bauerlein R, Zlotchenko E, Scrimgeour A, Lawrence JC, Glass DJ, Yancopoulos GD|title=Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo |journal=Nat Cell Biology. |volume=3 |issue=1 |pages=1014-1019 |date=2001 |pmid=11715023 |doi=10.1038/ncb1101-1014}}
*{{cite journal |vauthors=Bodine SC, Latres E, Baumhueter S, Lai VK, Nunez L, Clarke BA, Poueymirou WT, Panaro FJ, Na E, Dharmarajan K, Pan ZQ, Valenzuela DM, DeChiara TM, Stitt TN, Yancopoulos GD, Glass DJ.|title=Identification of ubiquitin ligases required for skeletal muscle atrophy |journal=Science. |volume=294 |issue=5547 |pages=1704-1708 |date=2001 |pmid=11679633 |doi=10.1126/science.1065874}}

=== Honors & Awards ===
'''Honors''' – elected member

* ] (2004),
⚫ * ] (2023)
⚫ * ] (2024)


==References == ==References ==
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{{DEFAULTSORT:Glass, David J.}} {{DEFAULTSORT:Glass, David J.}}


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American biomedical scientist (born 1961)
David J. Glass
Born1961 (age 63–64)
EducationColumbia University (BS, MD)
OccupationBiomedical scientist
EmployerRegeneron

David J. Glass (born 1961) is an American biomedical scientist who led Regeneron's 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.

Scientific career

He was elected to both the National Academy of Sciences and the American Association for the Advancement of Science. Earlier, he was elected to the American Society for Clinical Investigation.

Glass 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; mice which are null for these ligases were found to have less loss of muscle under atrophic conditions. .

Book

He is the author of a book aimed at teaching students how to design biology experiments, titled "Experimental Design for Biologists." The book is in its 2nd edition, published by Cold Spring Harbor Laboratory Press. .

Journal

Glass was the founding editor-in-chief of the Elsevier journal Skeletal Muscle. .

Key Papers

Honors & Awards

Honors – elected member

References

  1. https://data.the-asci.org/controllers/asci/DirectoryController.php?action=profile&entryId=500433 {{citation}}: Missing or empty |title= (help)
  2. "David Glass".
  3. https://skeletalmusclejournal.biomedcentral.com/articles/10.1186/s13395-024-00343-5 {{citation}}: Missing or empty |title= (help)
  4. Cite error: The named reference SA was invoked but never defined (see the help page).
  5. https://the-asci.org/controllers/asci/DirectoryController.php?action=bySpecialty&specialtyId=79. {{cite web}}: Missing or empty |title= (help)
  6. "How Nerve Meets Muscle and Begins to Talk". New York Times. May 21, 1996. Retrieved May 1, 2011.
  7. 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.
  8. 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.
  9. 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.
  10. 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. {{cite web}}: Missing or empty |title= (help)
  11. https://www.cshlpress.com/default.tpl?cart=1736745146262901944&fromlink=T&linkaction=full&linksortby=oop_title&--eqSKUdatarq=1020. {{cite web}}: Missing or empty |title= (help)
  12. https://skeletalmusclejournal.biomedcentral.com. {{cite web}}: Missing or empty |title= (help)



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