Sakamoto K, Urushidani T, Nagao T
Graduate School of Pharmaceutical Sciences, University of Tokyo, 3-1 Hongo 7-chome, Bunkyo-ku, Tokyo, 113, Japan.
Biochem Biophys Res Commun. 1998 Oct 20;251(2):576-9. doi: 10.1006/bbrc.1998.9518.
We investigated the possible changes in the distribution of HSP27 after a brief hypoxia-reoxygenation stress in the rat myoblast cell line, H9c2, as a model of ischemic preconditioning. Cells were exposed to 4 cycles of 5 min. of hypoxia and 5 min. of reoxygenation. In the normoxic condition, HSP27 was exclusively found in the cytosolic fraction. After the hypoxia-reoxygenation cycle, HSP27 redistributed to the cytoskeletal fraction, which was blocked by 10 microM SB 203580, a specific inhibitor of p38 MAP kinase. Cells treated with the repetitive hypoxia-reoxygenation developed resistance against cell death induced by hypoxia for 24 hours. The changes in localization of HSP27 found in the present study may reflect the mechanism of preconditioning in the cardiac myocyte.
我们以大鼠成肌细胞系H9c2作为缺血预处理模型，研究了短暂缺氧复氧应激后热休克蛋白27（HSP27）分布的可能变化。细胞暴露于4个循环的5分钟缺氧和5分钟复氧过程中。在常氧条件下，HSP27仅存在于胞质部分。缺氧复氧循环后，HSP27重新分布到细胞骨架部分，这一过程被p38丝裂原活化蛋白激酶的特异性抑制剂10微摩尔SB 203580阻断。经反复缺氧复氧处理的细胞对缺氧诱导的细胞死亡产生了24小时的抗性。本研究中发现的HSP27定位变化可能反映了心肌细胞预处理的机制。
