Calreticulin associates with stress proteins: Implications for chaperone function during heat stress

Autor:	Sunita M. Jethmalani, Kurt J. Henle
Rok vydání:	1998
Předmět:	chemistry.chemical_classification Glycosylation biology Immunoprecipitation Size-exclusion chromatography Cell Biology Biochemistry Hsp90 chemistry.chemical_compound chemistry Chaperone (protein) Heat shock protein biology.protein Glycoprotein Molecular Biology Calreticulin
Zdroj:	Journal of Cellular Biochemistry. 69:30-43
ISSN:	1097-4644 0730-2312
DOI:	10.1002/(sici)1097-4644(19980401)69:1<30::aid-jcb4>3.0.co;2-w
Popis:	Acute heat stress leads to the glycosylation of a "prompt" stress glycoprotein, P-SG67/64, identified as calreticulin. In the present study, we used immunoprecipitation to investigate the interactions of P-SG/calreticulin with other proteins during cellular recovery from heat stress. In heat-stressed CHO and M21 cells, both glycosylated and unglycosylated P-SGs interact with HSP90, GRP94, GRP78, and the other prompt stress glycoprotein, P-SG50, in an ATP-independent manner. Specificity of HSP-P-SG interactions was determined by chemical cross-linking with the homo-bifunctional agent DSP (3,3'-dithiobis[succinimidyl propionate]). Characterization of the cross-linked complexes involving calreticulin and heat shock proteins (HSPs) showed an average mass of 400-600 kDa by gel filtration chromatography. Overall, the consistent association of glycosylated and unglycosylated calreticulin with P-SG50 and unglycosylated HSPs suggests that P-SG/calreticulin is an active member of the cast of glycone/aglycone chaperones that cooperate to achieve cellular recovery from acute heat stress.
Databáze:	OpenAIRE
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