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lüll Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis Tsutsumi S; Neckers LCancer Sci 2007[Oct]; 98 (10): 1536-9Heat shock protein 90 (Hsp90) is a molecular chaperone whose association is required for the stability and function of multiple mutated, chimeric and over-expressed signaling proteins that promote the growth and/or survival of cancer cells. Hsp90 client proteins include mutated p53, Bcr-Abl, Raf-1, Akt, HER2/Neu (ErbB2) and HIF-1alpha. Hsp90 inhibitors, by interacting specifically with a single molecular target, cause the destabilization and eventual degradation of Hsp90 client proteins, and the first-in-class Hsp90 inhibitor, 17-allylamino-17 demethoxygeldanamycin (17AAG), is currently in phase II clinical trials. A fraction of Hsp90 has been identified at the cell surface and its presence has recently been shown to correlate with melanoma progression. Inhibition of cell-surface Hsp90 with antibodies or cell-impermeable Hsp90 inhibitors blocks cell motility and invasion in vitro and cancer metastasis in vivo. Thus, cell-surface Hsp90 may play a unique role in tumor metastasis, distinct from but perhaps overlapping with its intracellular function. In addition, because cell-surface Hsp90 may be the point of contact between some viruses and host cells, this pool of the chaperone may play a distinct role in initiation of infectious disease.|*Cell Movement[MESH]|*Neoplasm Metastasis/drug therapy/pathology[MESH]|Animals[MESH]|Antineoplastic Agents/*pharmacology[MESH]|HSP90 Heat-Shock Proteins/*antagonists & inhibitors/*metabolism[MESH]|Humans[MESH]|Molecular Chaperones[MESH]|Neoplasms/drug therapy/*metabolism[MESH] |