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Overexpression of GRP78 protects glial cells from endoplasmic reticulum stress |
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| Authors: | Suyama Kaori Watanabe Masahiko Sakabe Kou Okada Yoshinori Matsuyama Daisuke Kuroiwa Masahiro Mochida Joji |
| Affiliation: | a Department of Anatomy and Cellular Biology, Basic Medical Science, Tokai University School of Medicine, 143 Shimokasuya, Isehara, Kanagawa 259-1193, Japan b Department of Orthopaedic Surgery, Surgical Science, Tokai University School of Medicine, 143 Shimokasuya, Isehara, Kanagawa 259-1193, Japan c Tokai University Teaching and Research Support Center, 143 Shimokasuya, Isehara, Kanagawa 259-1193, Japan |
| Abstract: | 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 72 h. Our findings support the hypothesis that GRP78 inhibits cell death associated with ER stress. |
| Keywords: | AP-positive cells, allophycocyanin-conjugated Annexin V-propidium iodide-labeled cells ER, endoplasmic reticulum FACS, fluorescence-activated cell sorter GRP78, 78-kDa glucose-regulated protein GFP, green fluorescent protein |
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