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Endothelin-1에 의한 phospholipase C 활성화와 세포내 Ca2+ 이동에 미치는 protein kinase 들의 효과
조중형(Jung Hyung Cho),김현준(Hyun Jun Kim),이윤혜(Yun Hye Lee),박진형(Jin Hyoung Park),장용운(Youn Un Jang),이승준(Seung June Lee),이준한(June Han Lee),윤정이(Jeong Yi Yoon),김창종(Chang Jong Kim),심상수(Sang Soo Sim) 대한약학회 2000 약학회지 Vol.44 No.2
To investigate the effects of protein kinases on endothelin-l-induced phospholipase C activation and Ca2+ mobilization in Rat-2 fibroblast, we measured the formation of inositol phosphates and intracellular Ca2+ concentration with [3H]inositol and Fura-2/AM, respectively. Endothelin-1 dose-dependently activated phospholipase C and increased intracellular Ca2+ concentration. Protein kinase C activator, PMA, significantly inhibited both phospholipase C activity and Ca2+ mobilization induced by endothelin-1. Tyrosine kinase inhibitor, genistein, inhibited both. On the other hand, cyclic nucleotide (cAMP and cGMP) did not have any influence on the signaling pathway of phospholipase C-Ca2+ mobilization induced by endothelin-1. These results suggest that protein kinase C and tyrosine kinase counteract on the signaling pathway of phospholipase C-Ca2+ mobilization induced by endothelin-1 in Rat-2 fibroblast.