Heat shock protein 27 controls apoptosis by regulating Akt activation.

摘要: Activation of the serine-threonine kinase Akt by cytokines, chemokines, and bacterial products delays constitutive neutrophil apoptosis, resulting in a prolonged inflammatory response. We showed previously that exists signaling complex with p38 MAPK, MAPK-activated protein kinase-2 (MAPKAPK-2), heat shock protein-27 (Hsp27); Hsp27 dissociates from upon activation. To better understand regulation this module, hypothesis phosphorylation regulates its interaction was tested. The present study shows phosphorylated on Ser-82 vitro intact cells, resulted dissociation Akt. Additionally, between necessary for activation neutrophils. Constitutive apoptosis accelerated sequestration Akt, enhanced rate reversed introduction constitutively active recombinant Our results define new mechanism which through control activity.