Pattern of protein phosphorylation in aortic endothelial cells. Modulation by adenine nucleotides and bradykinin.
作者： D Demolle , M Lecomte , J M Boeynaems
DOI: 10.1016/S0021-9258(19)81380-7
关键词:
摘要: In bovine aortic endothelial cells, ATP (10-100 microM) and bradykinin (0.1-1.0 enhanced the phosphorylation of two major protein substrates with apparent molecular masses 95 28 kDa. The action involved P2y purinoceptors. kinetics were distinct for phosphopeptides. 95-kDa was rapid (within 30 s) but transient (maintained only 2 min). This time course agrees that observed increase cytosolic Ca2+ level induced by in these cells. Ionophore A23187 (greater than or equal to 100 nM) this a longer period (5-10 min), whereas phorbol 12-myristate 13-acetate (PMA) completely inactive. enhancement 28-kDa detectable after 5-min lag maintained at least 20 min. PMA (50 stimulated weakly protein, (100-300 even more effective bradykinin. phosphoprotein seems be related 100-kDa substrate calmodulin-dependent kinase III recently identified as elongation factor-2. which resolved three variants bidimensional gel electrophoresis, appears very similar slightly heavier from thrombin-stimulated human platelets. addition, electrophoresis allowed detection 10 (from 18 46 kDa) whose equally well ATP, bradykinin, partially PMA. conclusion, cells catalyzed mostly Ca2+-dependent kinases, C.
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