Phospholipase D activation in hepatocyte growth factor‐stimulated rat hepatocytes mediates the expressions of c‐jun and c‐fos: Involvement of protein tyrosine kinase, protein kinase C, and Ca2+
T Adachi, S Nakashima, S Saji, T Nakamura, Y Nozawa – 1 November 1996 – Hepatocyte growth factor (HGF) activated phospholipase D (PLD) in primary‐cultured rat hepatocytes, as assessed by the formation of phosphatidylbutanol (PBut), a specific and stable product of PLD activity in the presence of 0.3% butanol. PLD hydrolyzes phosphatidylcholine to choline and phosphatidic acid (PA), which is further metabolized to diacylglycerol (DG) by PA phosphohydrolase (PAP). In HGF‐stimulated hepatocytes, butanol prevented the formation of PA and DG.