A Role of Protein Kinase C in the Regulation of Cytosolic Phospholipase A2in Bradykinin-Induced PGI2Synthesis by Human Vascular Endothelial Cells

التفاصيل البيبلوغرافية
العنوان: A Role of Protein Kinase C in the Regulation of Cytosolic Phospholipase A2in Bradykinin-Induced PGI2Synthesis by Human Vascular Endothelial Cells
المؤلفون: Higaki, Tadashi, Sawada, Shohei, Kono, Yoshihito, Imamura, Hitoshi, Tada, Yusuke, Yamasaki, Seiki, Toratani, Akihisa, Sato, Toshiyuki, Komatsu, Sumio, Akamatsu, Naoaki, Tamagaki, Toshiyuki, Tsuda, Yutaka, Tsuji, Hajime, Nakagawa, Masao
المصدر: Microvascular Research; September 1999, Vol. 58 Issue: 2 p144-155, 12p
مستخلص: The purpose of this study was to elucidate the mechanism by which bradykinin (BK) enhances prostacyclin (PGI2) production in human umbilical vein endothelial cells (HUVEC). BK-induced enhancement of PGI2synthesis was observed in a dose- and time-dependent manner, and it also increased [Ca2+]ifollowed by enhancement of cytosolic phospholipase A2(cPLA2) activity. The PKC inhibitors GF109203X and H7 attenuated the BK-induced increase in [Ca2+]iand inhibited the BK-induced PGI2synthesis. Phorbol 12-myristate 13-acetate increased cPLA2activity and PGI2synthesis but failed to alter [Ca2+]i. BK increased cPLA2mRNA eightfold by 15 min, and this increase was inhibited by pretreatment with the PKC inhibitors. In response to cycloheximide pretreatment, cPLA2mRNA was superinduced. These results suggest that BK stimulates PGI2synthesis in HUVEC by activation of cPLA2by dual mechanisms: an elevation of [Ca2+]iand a PKC-dependent pathway. Moreover, changes in calcium kinetics and expression of cPLA2mRNA may underlie the BK-induced PGI2enhancement in these cells.
قاعدة البيانات: Supplemental Index
الوصف
تدمد:00262862
10959319
DOI:10.1006/mvre.1999.2163