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the influence of hsp60 on the maturation of autophagic structures is particularly interesting in relation to its ability to prevent the initial steps of apoptosis. in particular, hsp60 seems to affect mom permeabilization and to interfere with proapoptotic signal transduction pathways such as those involving bax and bak ( 639, 41, 674 ), puma and daxx ( 680, 681 ), and the mitochondrial depolarization of the outer membrane potential ( 641, 642 ).
clade a of the hsp60s interacts with the extracellular hsp60 of cardiac myocytes (643). this interaction may be mediated by association with sialoglycoprotein receptors of the endothelial cells (646). in this scenario, extracellularly generated hsp60 would function as an endogenous cardioprotective protein. in heart failure, adaptive up-regulation of the hsp60 expression results in activation of survival kinases, including akt and erk1/2, which contribute to antiapoptotic effects at the molecular level (645). strikingly, in myocytes, the hsp60clade a may directly prevent the activation of the apoptosis-inducing factor (aif) via its binding to sialoglycoprotein receptors, thereby blocking the release of proapoptotic proteins into the nucleus (646).