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The Hsp90-specific inhibitor, geldanamycin, blocks CD28-mediated activation of human T lymphocytes.

机译:Hsp90特异性抑制剂格尔德霉素可阻止CD28介导的人类T淋巴细胞活化。

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摘要

The 90 kDa heat shock protein (Hsp90) is a molecular chaperone aiding the folding of nuclear hormone receptors and protein kinases. Hsp90-mediated folding can be disrupted by the Hsp90-specific drug, geldanamycin. Here we provide evidence for the inhibition of the CD28-specific BW 828 antibody-mediated activation of human T lymphocyte proliferation, IL-2 secretion and IL-2 receptor expression by geldanamycin. Our results suggest that the major cytoplasmic chaperone, Hsp90, plays an important role in CD28-mediated T lymphocyte activation.
机译:90 kDa热休克蛋白(Hsp90)是一种分子伴侣,可帮助折叠核激素受体和蛋白激酶。 Hsp90特异性药物格尔德霉素可破坏Hsp90介导的折叠。在这里,我们为格尔德霉素抑制CD28特异性BW 828抗体介导的人类T淋巴细胞增殖,IL-2分泌和IL-2受体表达的活化提供了证据。我们的结果表明,主要的细胞质伴侣Hsp90在CD28介导的T淋巴细胞活化中起重要作用。

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