Hsp90 (he at shock protein 90) is needed for folding, maturation, transport, and degradation of various proteins, particularly signaling molecules, steroid receptors, and transcription factors. Hsp90b (Hsp90 β) is secreted by various cells and works as a chaperone for selected surface-associated or secreted proteins. It acts as a chaperone for matrix metalloproteinases and extracellular matrix proteins, and helps in cell motility. Suppression of the Hsp90b activity is suggested as a therapeutic approach for various cancers and inflammatory diseases.
