Twomey B M, McCallum S, Isenberg D A, Latchman D S
Department of Biochemistry, University College London Medical School, UK.
Clin Exp Immunol. 1993 Aug;93(2):178-83. doi: 10.1111/j.1365-2249.1993.tb07962.x.
During the phorbol myristate acetate (PMA)-induced differentiation of U937 cells to a macrophage-like phenotype, the levels of the heat shock proteins hsp90, hsp72 and hsp65 increased dramatically to a peak level following 24 h of treatment, and then declined. In contrast, no significant increase was observed in the level of the constitutive hsp73 protein in this process. The observed increases in hsp levels were preceded by an increase in the transcription of each of the genes encoding these hsps, including both of the two genes which encode hsp90. The mechanism of this effect and the possible role of the hsps in the function of differentiated macrophages and in the differentiation process are discussed.
在佛波醇肉豆蔻酸酯乙酸酯（PMA）诱导U937细胞分化为巨噬细胞样表型的过程中，热休克蛋白hsp90、hsp72和hsp65的水平在处理24小时后急剧升高至峰值水平，然后下降。相比之下，在此过程中组成型hsp73蛋白的水平未观察到显著增加。观察到的热休克蛋白水平升高之前，编码这些热休克蛋白的每个基因的转录均增加，包括编码hsp90的两个基因。讨论了这种效应的机制以及热休克蛋白在分化巨噬细胞功能和分化过程中的可能作用。
