| Phosphatidylinositol 3-kinase in myogenesis. | |
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MedLine Citation:
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PMID: 21235885 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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Phosphatidylinositol 3-kinase (PI 3-kinase) has been cloned and characterized in a wide range of organisms. PI 3-kinases are activated by a diversity of extracellular stimuli and are involved in multiple cell processes such as cell proliferation, protein trafficking, cell motility, differentiation, regulation of cytoskeletal structure, and apoptosis. It has recently been shown that PI 3-kinase is a crucial second messenger in the signaling of myogenesis. Two structurally unrelated highly specific inhibitors of PI 3-kinase-wortmannin and LY294002-block the morphological and biochemical differentiation program of different skeletal-muscle cell models. Moreover, L6E9 myoblasts overexpressing a dominant-negative mutant of PI 3-kinase p85 regulatory subunit (Δp85) are unable to differentiate. Furthermore, PI 3-kinase is specifically involved in the insulinlike growth factor (IGF)-dependent myogenic pathway. Indeed, the ability of IGF-I, des-1,3-IGF-I, and IGF-II to promote cell fusion and muscle-specific protein expression is impaired after treatment with PI 3-kinase inhibitors or in cells overexpressing Δp85. The identification of additional key downstream elements of the IGF/PI 3-kinase myogenic cascade is crucial to a detailed understanding of the process of muscle differentiation and may generate new tools for skeletal and cardiac muscle regeneration therapies. (Trends Cardiovasc Med 1997;7:198-202). © 1997, Elsevier Science Inc. |
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Authors:
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P Kaliman; A Zorzano |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Trends in cardiovascular medicine Volume: 7 ISSN: 1050-1738 ISO Abbreviation: Trends Cardiovasc. Med. Publication Date: 1997 Aug |
Date Detail:
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Created Date: 2011-01-17 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9108337 Medline TA: Trends Cardiovasc Med Country: United States |
Other Details:
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Languages: eng Pagination: 198-202 Citation Subset: - |
Copyright Information:
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Copyright © 1997 Elsevier Inc. All rights reserved. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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