J Biol Chem 1994 Jun 03;26922:15718-23.

hsc70 moderates the heat shock (stress) response in Xenopus laevis oocytes and binds to denatured protein inducers.

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Injections of hsc70 protein into Xenopus oocytes lowered the stress response to both a thermal shock and to co-injected protein inducers. Binding of hsc70 to native and modified forms of bovine serum albumin (BSA) were tested by two assays. In one, nitrocellulose-bound proteins were incubated with hsc70, cross-linked with glutaraldehyde, and then bound hsc70 was probed with a monoclonal anti-hsc70 antibody. In the second, peroxidase-conjugated hsc70 was employed as a more direct probe for binding to proteins displayed on nitrocellulose membranes. hsc70 binding to the BSA derivatives correlated with their abilities to induce a stress response upon microinjection into oocytes. Reduced and carboxymethylated (rcm) BSA, the most potent stress inducer tested, was bound most tightly by hsc70, whereas hsc70 had moderate affinity for N-methylated rcm-BSA and very little affinity for the native protein. No binding was observed with iodinated BSA. The results suggest a mechanism whereby the cell employs hsc70 or other proteins of the hsp70 family both to trigger the response to an environmental stress and to provide a feedback mechanism to attenuate the response.

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Species referenced: Xenopus laevis
Genes referenced: alb hsp70 hspa1l hspa8