Titlebook: Heat Shock Proteins in Cancer; Stuart K. Calderwood,Michael Y. Sherman,Daniel R. Book 2007 Springer Science+Business Media B.V. 2007 Anti

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,Anti-apoptotic, Tumorigenic and Metastatic Potential of Hsp27 (HspB1) and αB-crystallin (HspB5): Em share dynamic phosphorylation and oligomeric properties suggesting that different functional forms of these proteins exist. Elevated levels of expression of these sHsps counteract both necrotic and apoptotic cell deaths induced by various stimuli including heat shock, oxidative stress, inflammatory

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Involvement of Heat Shock Proteins in Protection of Tumor Cells from Genotoxic Stresses,lly relevant doses induce apoptosis mostly in lymphoid cells, while in epithelial tumors they evoke different type of response, mainly senescence and mitotic catastrophe, which leads to loss of clonogenic potential of cells. Here we review old and new data showing that upregulation of Hsp27 or Hsp70

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Hsp70 in Tumors: Friend or Foe?,p70 promotes growth and survival of tumor cells by engaging misfolded or aggregated proteins and proteins involved in cell proliferation. As such, it endows tumor cells with stress resistance. However, Hsp70 can also promote tumor immunity by stimulating innate immune mechanisms and enhancing cross-

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Heat Shock Protein 90: The Cancer Chaperone, signaling proteins, as well as multiple mutated, chimeric, and/or over-expressed signaling proteins, that promote cancer cell growth and/or survival. Hsp90 inhibitors are unique in that, although they are directed towards a specific molecular target, they simultaneously inhibit multiple cellular si