| Overexpression of GRP78 protects glial cells from endoplasmic reticulum stress. | |
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MedLine Citation:
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PMID: 21970967 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Endoplasmic reticulum (ER) stress induces apoptotic cell death by causing the accumulation of structurally abnormal proteins. The 78-kDa glucose-regulated protein (GRP78) is an ER chaperone that regulates protein folding in the ER and has been suggested to contribute to cell survival. Using the rat C6 glioma cell line and flow cytometry, we assessed GRP78 expression following tunicamycin- and glutamate-induced ER stress. The results showed that GRP78 expression is upregulated following ER stress and has protective effects on injured glial cells. Annexin V and propidium iodide labeling revealed cells transiently expressing GRP78 prior to injury were protected against high-concentrations of tunicamycin and glutamate within 72h. Our findings support the hypothesis that GRP78 inhibits cell death associated with ER stress. |
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Authors:
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Kaori Suyama; Masahiko Watanabe; Kou Sakabe; Yoshinori Okada; Daisuke Matsuyama; Masahiro Kuroiwa; Joji Mochida |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-9-28 |
Journal Detail:
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Title: Neuroscience letters Volume: - ISSN: 1872-7972 ISO Abbreviation: - Publication Date: 2011 Sep |
Date Detail:
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Created Date: 2011-10-5 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7600130 Medline TA: Neurosci Lett Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011. Published by Elsevier Ireland Ltd. |
Affiliation:
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Department of Anatomy and Cellular Biology, Basic Medical Science, Tokai University School of Medicine, 143 Shimokasuya, Isehara, Kanagawa 259-1193, Japan. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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