热休克蛋白构成了对脂多糖和GroEL作出反应的危险信号级联反应的一部分。
Heat shock proteins form part of a danger signal cascade in response to lipopolysaccharide and GroEL.
作者信息
Davies E L, Bacelar M M F V G, Marshall M J, Johnson E, Wardle T D, Andrew S M, Williams J H H
机构信息
Chester Centre for Stress Research, Biological Sciences, University of Chester, Chester, UK.
出版信息
Clin Exp Immunol. 2006 Jul;145(1):183-9. doi: 10.1111/j.1365-2249.2006.03109.x.
An increasing number of cell types, including peripheral blood mononuclear cells (PBMCs), have been demonstrated to release heat shock proteins (Hsps). In this paper we investigate further the hypothesis that Hsps are danger signals. PBMCs and Jurkat cells released Hsp70 (0.22 and 0.7 ng/10(6) cells, respectively) into medium over 24 h at 37 degrees C. Release of Hsp70 was stimulated 10-fold by GroEL (P < 0.001) and more than threefold by lipopolysaccharide (LPS) (P < 0.001). Although Hsp60 could be detected in the medium of cells cultured at 37 degrees C for 24 h, the low rates of release were due probably to cell damage. Significant release of Hsp60 was observed when Jurkat cells were exposed to GroEL (2.88 ng/10(6) cells) or LPS (1.40 ng/10(6) cells). The data are consistent with the hypothesis that Hsp70 and Hsp60 are part of a danger signalling cascade in response to bacterial infection.
越来越多的细胞类型，包括外周血单核细胞（PBMCs），已被证明能释放热休克蛋白（Hsps）。在本文中，我们进一步研究了Hsps是危险信号这一假说。PBMCs和Jurkat细胞在37℃下24小时内分别向培养基中释放Hsp70（分别为0.22和0.7 ng/10⁶个细胞）。GroEL刺激Hsp70的释放增加了10倍（P < 0.001），脂多糖（LPS）刺激其释放增加了三倍多（P < 0.001）。尽管在37℃培养24小时的细胞培养基中可检测到Hsp60，但其低释放率可能是由于细胞损伤。当Jurkat细胞暴露于GroEL（2.88 ng/10⁶个细胞）或LPS（1.40 ng/10⁶个细胞）时，观察到Hsp60有显著释放。这些数据与Hsp70和Hsp60是响应细菌感染的危险信号级联反应的一部分这一假说一致。
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