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Heat-shock protein 60 and cardiovascular disease: a paradoxical role
Anne A Knowlton1, Uma Srivatsa
1University of California, Molecular & Cellular Cardiology, Davis One Shields Avenue, Davis, CA 95616, USA, and Department of Veterans Affairs, Northern california Health Care System, Mather, CA, USA. aaknowlton@ucdavis.edu
Abstract:
Heat-shock proteins (HSPs) are members of a highly conserved group of proteins that are induced in response to stress and injury. These proteins have protective properties, and can protect the heart from injury. HSP60 is found in the mitochondria and cytosol, and has essential intracellular functions including folding key proteins after their import into the mitochondria. In the cytosol, HSP60 binds to proapoptotic proteins, sequestering them. HSPs are highly conserved and, thus, are similar to bacterial proteins. Many individuals have antibodies to HSP60, possibly from prior infections. HSP60 can be found in the plasma membrane and in the serum in disease states. Serum HSP60 may be a marker for coronary artery disease. Once extracellular, HSP60 can cause cell injury. Thus, this protein has dichotomous functions for which the role in disease remains to be fully elucidated.
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