Stress (Heat Shock) Proteins

Circulation Research - Tập 83 Số 2 - Trang 117-132 - 1998
Ivor J. Benjamin1, D. Randy McMillan1
1From the Department of Internal Medicine and Integrative Biology Graduate Program, Molecular Cardiology Research Laboratories, The University of Texas Southwestern Medical Center, Dallas, Tex.

Tóm tắt

Abstract —How a cell responds to stress is a central problem in cardiovascular biology. Diverse physiological stresses (eg, heat, hemodynamics, mutant proteins, and oxidative injury) produce multiple changes in a cell that ultimately affect protein structures and function. Cells from different phyla initiate a cascade of events that engage essential proteins, the molecular chaperones, in decisions to repair or degrade damaged proteins as a defense strategy to ensure survival. Accumulative evidence indicates that molecular chaperones such as the heat shock family of stress proteins (HSPs) actively participate in an array of cellular processes, including cytoprotection. The versatility of the ubiquitous HSP family is further enhanced by stress-inducible regulatory networks, both at the transcriptional and posttranscriptional levels. In the present review, we discuss the regulation and function of HSP chaperones and their clinical significance in conditions such as cardiac hypertrophy, vascular wall injury, cardiac surgery, ischemic preconditioning, aging, and, conceivably, mutations in genes encoding contractile proteins and ion channels.

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Circulation Research

Tập 83 Số 2

117-132

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