PKC-dependent delayed metabolic preconditioning is independent of transient MAPK activation.
作者： James W. Mockridge , Anu Punn , David S. Latchman , Michael S. Marber , Richard J. Heads
DOI: 10.1152/AJPHEART.2000.279.2.H492
关键词: Mitogen-activated protein kinase 、 Cytoprotection 、 Glycolysis 、 Internal medicine 、 p38 mitogen-activated protein kinases 、 Protein kinase C 、 Extracellular 、 Endocrinology 、 Cell biology 、 Phosphorylation 、 Medicine 、 Kinase
摘要: In this study we used an in vitro model of delayed preconditioning to investigate activation mitogen-activated protein kinases (MAPKs) and their potential role protection. Neonatal rat cardiomyocytes were preconditioned using a buffer containing glycolytic inhibitors low pH (minimal metabolic preconditioning; MMPC) consisting modified Krebs buffer, 10 mM 2-deoxyglucose, 20 lactate, 6.8, for 2 h followed by 24 simulated reperfusion before lethal ischemia (LSI). MAPK during the MMPC protocol was determined phospho-specific antisera effect on protection following LSI. Rapid, transient phosphorylation extracellular signal-regulated 1 (ERK1/2) p38 observed each MMPC, reperfusion, LSI phases; blocked PD-98059 SB-203580, respectively, but not kinase C (PKC) inhibitor Ro31-8220. However, although Ro31-8220, treatment with did block conferred MMPC. Thus data suggest that, preconditioning, appears be PKC dependent independent ERK1/2 or activation.
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