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

✍ Scribed by Sunita M. Jethmalani; Kurt J. Henle

• Book ID: 102656358
• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 545 KB
• Volume: 69
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/(sici)1097-4644(19980401)69:1<30::aid-jcb4>3.0.co;2-w

✦ Synopsis

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.