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Caspase-10-Mediated Heat Shock Protein 90β Cleavage Promotes UVB Irradiation-Induced Cell Apoptosis

机译:Caspase-10-介导的热休克蛋白90β裂解促进UVB辐射诱导的细胞凋亡。

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Heat shock protein 90β (Hsp90β) is involved in many cellular functions. However, the posttranslational modification of Hsp90β, especially in response to apoptotic stimulation, is not well understood. In this study, we found that Hsp90β was cleaved by activated caspase-10 under UVB irradiation. Caspase-10 activation, in turn, depended on caspase-8, which cleaved caspase-10 directly. Autocrine secretion of FAS ligand and upregulated FAS expression induced by UVB irradiation contributed to activation of caspase-10, which cleaved Hsp90β at D278, P293, and D294. The downregulation of Hsp90β mediated by caspase-8-dependent caspase-10 activation promoted UVB-induced cell apoptosis.
机译:热激蛋白90β(Hsp90β)参与许多细胞功能。但是,Hsp90β的翻译后修饰,尤其是对凋亡刺激的响应,尚不十分清楚。在这项研究中,我们发现Hsp90β在UVB照射下被活化的caspase-10裂解。反过来,caspase-10激活取决于caspase-8,后者直接裂解caspase-10。 FAS配体的自分泌分泌和UVB辐射诱导的FAS表达上调有助于caspase-10的活化,该酶在D278,P293和D294处切割Hsp90β。 caspase-8依赖性caspase-10激活介导的Hsp90β的下调促进了UVB诱导的细胞凋亡。

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