Dehaye J P, Winand J, Michel P, Poloczek P, Damien C, Vandermeers-Piret M C, Vandermeers A, Christophe J
FEBS Lett. 1984 Jul 9;172(2):284-8. doi: 10.1016/0014-5793(84)81142-4.
Pancreatic secretory factor (PSF), an efficient pancreatic secretagogue recently isolated from the venom of Heloderma suspectum, is shown to exert phospholipase A2 activity towards phosphatidylcholine. This activity is strictly dependent on calcium (apparent Ka 40 nM) and has an optimum pH around 9. At pH 7.4 and in the presence of calcium, PSF retains 40% of its phospholipase A2 activity. These results are compared to the calcium dependency of the secretory effect of PSF on rat pancreatic acini. Taken collectively, the present data on PSF suggest that a similar endogenous phospholipase A2 activity might be involved in the late steps of stimulus-secretion coupling in the exocrine pancreas.
胰腺分泌因子（PSF）是最近从毒蜥毒液中分离出的一种有效的胰腺促分泌素，已证明它对磷脂酰胆碱具有磷脂酶A2活性。这种活性严格依赖于钙（表观解离常数Ka为40 nM），最适pH约为9。在pH 7.4且有钙存在的情况下，PSF保留其40%的磷脂酶A2活性。将这些结果与PSF对大鼠胰腺腺泡分泌作用的钙依赖性进行了比较。综合来看，目前关于PSF的数据表明，类似的内源性磷脂酶A2活性可能参与外分泌胰腺刺激-分泌偶联的后期步骤。
