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Surface expression of Hsp70B’ in response to proteasome inhibition in human colon cells

机译:Hsp70B'在人结肠细胞中响应蛋白酶体抑制的表面表达

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摘要

Hsp70B’ was expressed on the surface of HT-29 and CRL-1809 but not SW-480 human colon cell lines in response to proteasome inhibition as detected using flow cytometry. Surface expression was not detected under non-stress conditions nor was heat shock an inducer of surface expression in the three cell lines tested. Phylogenetic analysis indicated that the Hsp70B’ protein sequence was most closely related to another major inducible human Hsp70, Hsp72. Hsp70B’ appeared to be recently diverged, as homologs for Hsp70B’ have not been found in rodents. Hsp72 and Hsp70B’ shared 100% amino acid sequence identity in their predicted peptide-binding regions suggesting that they bind the same peptide substrates, perhaps in extracellular antigen presentation. Amino acid sequence differences were concentrated in the lid regions and the C-terminal domains raising the possibility that Hsp72 and Hsp70B’ bind different co-chaperones or cell surface receptors.
机译:Hsp70B'在流式细胞仪检测到的蛋白酶体抑制反应中在HT-29和CRL-1809的表面表达,但不在SW-480人结肠细胞系表达。在非胁迫条件下未检测到表面表达,在三种测试的细胞系中热激也未诱导表面表达。系统发育分析表明,Hsp70B的蛋白质序列与另一种主要的可诱导人Hsp70 Hsp72密切相关。 Hsp70B'似乎最近有所分歧,因为在啮齿动物中未发现Hsp70B'的同系物。 Hsp72和Hsp70B'在其预测的肽结合区具有100%的氨基酸序列同一性,这表明它们可能在细胞外抗原呈递中结合相同的肽底物。氨基酸序列差异集中在盖区和C末端结构域,增加了Hsp72和Hsp70B'结合不同的伴侣蛋白或细胞表面受体的可能性。

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