THE 90-KDA MOLECULAR CHAPERONE FAMILY - STRUCTURE, FUNCTION, AND CLINICAL-APPLICATIONS - A COMPREHENSIVE REVIEW

The 90-kDa molecular chaperone family (which comprises, among other pr oteins, the 90-kDa heat-shock protein, hsp90 and the 94-kDa glucose-re gulated protein, grp94, major molecular chaperones of the cytosol and of the endoplasmic reticulum, respectively) has become an increasingly active subject of research in the past couple of years. These ubiquit ous, well-conserved proteins account for 1-2% of all cellular proteins in most cells. However, their precise function is still far from bein g elucidated. Their involvement in the aetiology of several autoimmune diseases, in various infections, in recognition of malignant cells, a nd in antigen-presentation already demonstrates the essential role the y likely will play in clinical practice of the next decade. The presen t review summarizes our current knowledge about the cellular functions , expression, and clinical implications of the 90-kDa molecular chaper one family and some approaches for future research. PHARMACOL. THER. 7 9(2):129-168, 1998. (C) 1998 Elsevier Science Inc.