文摘
In this study, we investigated the ability of prostaglandin F2α (PGF2α) to induce tyrosine phosphorylation of phospholipase C-γ1 (PLC-γ1) in cat iris sphincter smooth muscle (CISM) cells. PGF2α(1μM) stimulated PLC-γ1 tyrosine phosphorylation in a time- and dose-dependent manner with a maximum increase of 3-fold at 0.5min. The protein tyrosine kinase inhibitors, genistein, and tyrphostin A-25, blocked the stimulatory effects of PGF2α, suggesting involvement of protein tyrosine kinase activity in the physiological actions of the PGF2α. Furthermore, PGF2α-induced p42/p44 MAP kinase activation was also completely blocked by protein tyrosine kinase inhibitors. In summary, these findings show that PGF2α stimulates tyrosine phosphorylation of PLC-γ1 in CISM cells and indicate that PGF2α-stimulated tyrosine phosphorylation is responsible for an early signal transduction event.