Endothelin-1에 의한 phospholipase C 활성화와 세포내 Ca2+ 이동에 미치는 protein kinase 들의 효과

• 영문명: Effects of Protein Kinases on Phospholipase C Activation and Intracellular Ca2+ Mobilization Induced by Endothelin-1
• 발행기관: 대한약학회
• 저자명: 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)
• 간행물 정보: 『약학회지』제44권 제2호 (2000년), 162~168쪽, 전체 7쪽
• 주제분류: 의약학 > 기타의약학
• 파일형태: PDF
• 발행일자: 2000.04.29

영문 초록

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.

키워드

Phospholipase C calcium mobilization protein kinase cyclic nucleotide.