摘要
目的探讨肾上腺素受体(adrenergic receptor,AR)激动剂对培养的新生大鼠心肌细胞胞质型磷脂酶A2(cy-tosolic phospholipase A2,cPLA2)的磷酸化效应及机制。方法分别用β-AR激动剂异丙肾上腺素(10μmol/L)和α1-AR激动剂苯肾上腺素(10μmol/L)处理培养的新生大鼠心肌细胞,Western blot法检测cPLA2及丝裂原活化蛋白激酶(p38MAPK)、细胞外调节蛋白激酶1/2(ERK1/2)磷酸化水平随时间变化的效应曲线。结果α1-AR激活引起心肌细胞内cPLA2磷酸化水平显著增高,此效应可能由p38MAPK及ERK1/2的磷酸化介导;β-AR激活可引起p38MAPK及ERK1/2的磷酸化,但不伴有cPLA2的磷酸化。结论实验结果揭示了心肌细胞中α1-AR激动在调控cPLA2活性方面的重要作用。
Objective To investigate the effect of adrenergic receptor agonist on cytosolic phospholipase A2（cPLA2）phosphorylation in cultured neonatal rat cardiomyocytes. Methods The phosphorylation levels of mitogen-activated protein kinase p38 MAPK,ERK1/2 and cPLA2 cAMP were measured in cultured neonatal rat cardiomyocytes exposed to β-AR agonist isoproterenol and α1-AR agonist phenylephrine respectively at different incubation periods. Results α1-AR agonist significantly increased phosphorylated cPLA2 in cardiomyocytes,which might be mediated by phosphorylation of p38 MAPK and ERK1/2.β-AR agonist stimulated phosphorylation of p38 MAPK and ERK1/2 but not accompanied by phosphorylation of cPLA2. Conclusion This research reveals an important role of α1-AR agonist in regulating cPLA2 activity.
出处
《华中科技大学学报（医学版）》
CAS
CSCD
北大核心
2011年第5期571-573,共3页
Acta Medicinae Universitatis Scientiae et Technologiae Huazhong
