Crête P, Landry J
Centre de Recherche en Cancérologie de l'Université Laval, l'Hôtel-Dieu de Québec, Canada.
Radiat Res. 1990 Mar;121(3):320-7.
Incorporation of [3H]leucine, immunochemical analyses with a specific hamster HSP27 rabbit immunoserum, and [32P]orthophosphate labeling were used to monitor synthesis, accumulation, and phosphorylation of HSP27 in Chinese hamster cells after induction of thermoresistance by arsenite, cycloheximide, A23187, and EGTA. In contrast to arsenite-induced thermotolerance, which develops in parallel to synthesis and accumulation of HSP27, enhanced thermoresistance observed immediately after incubating cells in the presence of cycloheximide, A23187, or EGTA is independent of HSP27 or other HSP accumulation. All these treatments, however, result in a rapid phosphorylation of preexisting HSP27. In view of previous results which indicated that HSP27 is involved in cell protection from thermal killing (J. Landry, P. Chrétien, H. Lambert, E. Hickey, and L. A. Weber, J. Cell Biol. 109, 7-15, 1989), it is proposed that activation of HSP27 through phosphorylation may be a key determinant in the regulation of cell thermosensitivity.
利用[3H]亮氨酸掺入、用特异性仓鼠HSP27兔免疫血清进行免疫化学分析以及[32P]正磷酸盐标记,来监测亚砷酸盐、环己酰亚胺、A23187和乙二醇双乙醚二胺四乙酸(EGTA)诱导中国仓鼠细胞产生热耐受后HSP27的合成、积累和磷酸化情况。与亚砷酸盐诱导的热耐受不同,后者与HSP27的合成和积累同时发生,在细胞于环己酰亚胺、A23187或EGTA存在的情况下孵育后立即观察到的增强的热耐受与HSP27或其他热休克蛋白(HSP)的积累无关。然而,所有这些处理都会导致预先存在的HSP27快速磷酸化。鉴于先前的结果表明HSP27参与细胞免受热杀伤的保护作用(J. 兰德里、P. 克雷蒂安、H. 兰伯特、E. 希基和L. A. 韦伯,《细胞生物学杂志》109, 7 - 15, 1989),有人提出通过磷酸化激活HSP27可能是调节细胞热敏感性的关键决定因素。