title: Shock the heat shock network.
abstract: The targeting of tumors is made possible through establishing protein signatures specific for each cancer type. The recent recognition of the higher expression levels of HSP90 and its accumulation in tumor cell mitochondria has made the HSP90 network a feasible target for neutralization. HSP90 antagonizes the mitochondrial permeability transition,blocking cytochrome c release and apoptosis. In this issue of the JCI, Kang et al. report the synthesis of Gamitrinibs, which target mitochondrially localized HSP90, specifically killing human cancer cell lines, and provide a fresh approach for cancer treatment.
authors.affiliation: Department of Molecular Biology and Genetics, Apoptosis and Cancer Immunology Laboratory (AKIL), Bogaziçi University, Bebek, Istanbul, Turkey.
authors.forename: Cigdem
authors.initials: C
authors.lastname: Atay
authors.forename: Serkan
authors.initials: S
authors.lastname: Ugurlu
authors.forename: Nesrin
authors.initials: N
authors.lastname: Ozören
mesh_terms: D000818:Animals; D000970:Antineoplastic Agents / Q000627:therapeutic use*; D001692:Biological Transport; D045744:Cell Line, Tumor; D045304:Cytochromes c / Q000037:antagonists & inhibitors / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors* / Q000187:drug effects; D006801:Humans; D008928:Mitochondria / Q000187:drug effects / Q000502:physiology; D009363:Neoplasm Proteins / Q000378:metabolism; D009369:Neoplasms / Q000378:metabolism*
chemical_list: D000970:Antineoplastic Agents; D018841:HSP90 Heat-Shock Proteins; D009363:Neoplasm Proteins; D045304:Cytochromes c