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- W1996190710 abstract "Background and Objectives:We investigated the delayed protection capability of a brief heat shock on day one against lethal heat stress on day two in a rat-derived H9c2 cardiomyoblast cell line with reference to the role of the heat shock proteins 25/27, and 70i and the p38MAPK signaling pathway. Materials, Method and Results:Heat preconditioning (Heat P;20 min at 42±0.1°C) and the administration of adenosine (ADO) on day 1 were found to provide protection against cell death under lethal heat challenge (75 min at 42±0.1°C) on day 2 as measured by the MTT test:(% cell viability:Heat P:79.9±3.23%, ADO:71.9±4.10% vs. control:52.7±1.65% respectively). This protection was canceled by treatment with SB203580 or cytochalasine D prior to the protective stimulus on day 1 (SB203580:64.1±4.37%, cytochalasine D:73.1±4.33% vs. Heat P). Western blotting analysis indicated a significant accumulation of hsp70i in Heat P and SB203580-treated Heat P cells compared to the adenosine-, and SB203580-treated cells and to the control. Phosphorylation of hsp25 was significantly increased in Heat P cells compared to control cells. Fragmentation of F-actin and formation of F-actin aggregates in cells exposed to lethal heat challenge was also observed. In contrast, the delayed cytoprotection preserved the F-actin bundles under the lethal heat challenge. The Hsp27-overexpressed, stable clones were more resistant to lethal heat shock than the control cells transfected with the vector alone. Conclusion:These data suggest an important role for the p38MAPK/hsp25/27 pathway as a potential distal effector of heat-induced delayed protection. (Korean Circulation J 2001;31(10):1049-1058)" @default.
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- W1996190710 date "2001-01-01" @default.
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- W1996190710 title "The Delayed Phase of Protection in Heat-Induced Preconditioning: Role of the Heat Shock Protein associated with cytoskeleton" @default.
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- W1996190710 doi "https://doi.org/10.4070/kcj.2001.31.10.1049" @default.
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