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흰쥐의 복강비만세포에서 ATP와 Compound 48/87에 의한 Histamine유리에 미치는 Econazole의 영향
장용운(Yong Un Jang),이윤혜(Yun Hye Lee),이승준(Seung June Lee),서무현(Moo Hyun Seo),윤정이(Jeong Yi Yoon),김창종(Chang Jong Kim),심상수(Sang Soo Sim) 대한약학회 2001 약학회지 Vol.45 No.3
3 investigate the different mechanism between ATP and compound 48/80 (C48/80)-induced histamine release, we observed effects of calcium antagonists in histamine release of rat peritoneal mast cells.Verapamil and diltiazgem (voltage-dependent calcium channel blocker) and TMB-8 (a blocker of intracellular calcium release) significantly inhibited ATP-induced histamine release, but did not inhibit C48/80 induced histamine release. Econazole (a blocker of receptor-operated calcium channel) dose-dependently inhibited both and C48/80-inducted histamine release,but inhibitory effect of econarole in ATP-induced histamine release was more potent than that in C48/80-induced histamine. EGTA dote-dependently inhibited ATP and C48/80-induced histamine release, and C48/80-induced histamine release was slightly inhibited by high concentrations (>2 mM) of EGTA. These results suggest that ATP·induced histamine release is related to both intraoellular calcium release and extracellular calcium influx via voltage-dependent calcium channel and receptor-operated calcium channel. C48/80-induced histamine release is related to extracellular calcium influx, specially recetor-operated calcium channel rather tllan voltage-dependent calcium channel.
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.