MOLECULAR CHAPERONES - HEAT-SHOCK PROTEINS, FOLDASES, AND MATCHMAKERS

The term molecular chaperone includes a large family of unrelated prot eins that comprise both stress-inducible and constitutive molecules. I n recent years, molecular chaperones or heat-shock proteins (Hsps) hav e emerged as fundamentally important topics in cell biology. Living or ganisms respond to stressful conditions, such as heat shock, by rapidl y producing a relatively small class of specific proteins that functio n to stabilize cellular components against stress. Hsps or molecular c haperones function by preventing misfolding of newly synthesized prote ins, escorting proteins targeted for other cellular compartments, and modulating or regulating proteins involved in cell growth and differen tiation. Clearly these proteins are of enormous importance to cellular function but of even more importance in helping to fight disease. Fro m heart tissue protection after coronary thrombosis to the regulation of tumor suppressor activity to the use of these molecules as new diag nostic and therapeutic agents, molecular chaperones offer scientists m any potential rewards. This review provides an insider's peek at molec ular chaperones-a most indispensable set of molecules for cell growth, survival, and regulation.