Author/Authors :
Shu، نويسنده , , En and Matsuno، نويسنده , , Hiroyuki and Akamastu، نويسنده , , Shigeru and Kanno، نويسنده , , Yosuke and Suga، نويسنده , , Hidetaka and Nakajima، نويسنده , , Keiichi and Ishisaki، نويسنده , , Akira and Takai، نويسنده , , Shinji and Kato، نويسنده , , Kanefusa and Kitajima، نويسنده , , Yasuo and Kozawa، نويسنده , , Osamu، نويسنده ,
Abstract :
αB-crystallin is the most abundant low-molecular-weight heat shock protein in heart and recent studies have demonstrated that it plays a cardioprotective role during myocardial infarction both in vivo and in vitro. On the other hand, platelet-derived growth factor (PDGF), a potent serum mitogen, has been reported to improve cardiac function after myocardial infarction. In the present study, using a mouse myocardial infarction model, we investigated whether αB-crystallin is phosphorylated during myocardial infarction and the implication of PDGF-BB. Phosphorylation of αB-crystallin at Ser-59 was time dependently induced and plasma PDGF-BB levels were concomitantly increased. Moreover, PDGF-BB-stimulated phosphorylation of αB-crystallin was suppressed by SB203580, a specific inhibitor of p38 mitogen-activated protein (MAP) kinase, in primary cultured cardiac myocytes. Our results indicate that PDGF-BB induces phosphorylation of αB-crystallin via p38 MAP kinase during myocardial infarction.
Keywords :
?B-crystallin , PDGF-BB , phosphorylation , p38 MAP kinase , Myocardial infarction
