Record Details


Field	Value

Title	Hsp90 mediates activation of the heme regulated eIF-2 kinase during oxidative stress

Creator	Kulkarni, A P Mittal, S P Devasagayam, T P A Pal, J K

Subject	eIF-2 Kinase Hsp70 Hsp90 Protein synthesis Oxidative stress

Description	67-74 The heme-regulated inhibitor (HRI), a member of the eIF-2 kinase family is crucial for regulating protein synthesis during stress. In addition to heme, stress proteins Hsp90 and Hsp70 are known to regulate HRI. The present study aims to determine the physical association of these Hsps in the regulation of HRI activation during oxidative stress using human K562 cells as a model. Extracts from the stress-induced cells were used for determining HRI kinase activity by measuring eIF-2 phosphorylation, and Hsp-HRI interaction by immunoprecipitation and immunoblot analyses. The results indicate a significant increase in both Hsp70 and Hsp90 expression during AAPH (2, 2’-azobis (2-amidinopropane) dihydrochloride)-induced oxidative stress. Further, their interaction with HRI, which correlates well with its increased HRI kinase activity leads to inhibition of protein synthesis. Thus, we demonstrate that Hsps play an important role in the regulation of initiation of protein synthesis during oxidative stress.

Date	2010-04-23T04:14:20Z 2010-04-23T04:14:20Z 2010-04

Type	Article

Identifier	0975-0959 (Online); 0301-1208 (Print) http://hdl.handle.net/123456789/8272

Language	en_US

Publisher	CSIR

Source	IJBB Vol.47(2) [April 2010]

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