title: [Role of heat shock proteins in cell apoptosis].
abstract: Apoptosis is, apart from necrosis and autophagy, one of the possible cell death mechanisms eliminating needless, not normal or infected cells. This process ensures quantitative and qualitative cell control of organisms. Apoptosis is tightly regulated, it requires both activation of a large number of genes and energy input. Up-to-date two main apoptotic pathways have been recognized - external/receptor and internal, processed with the participation of mitochondria. Heat shock proteins HSPs, the molecules known from their chaperone activity and molecular conservatism, play essential functions in the course of apoptosis. Among that proteins family, i.e. HSP100, 90, 70, 60, 40 and small molecular (sHSP), there are agents mainly protective against programmed cell death. However, in some conditions some of these proteins may promote apoptosis. This review describes different key apoptotic proteins interacting with main members of HSP family and the consequence of these events for cell survival or apoptosis.
authors.affiliation: Zakład Biochemii Medycznej, Katedra Cytobiochemii, Uniwersytet Łódzki, Łódź.
authors.forename: Arleta
authors.initials: A
authors.lastname: Kaźmierczuk
authors.forename: Zofia M
authors.initials: ZM
authors.lastname: Kiliańska
mesh_terms: D017209:Apoptosis / Q000502:physiology*; D020169:Caspases / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D015398:Signal Transduction
chemical_list: D006360:Heat-Shock Proteins; D020169:Caspases