人胰腺磷脂酶A2刺激人胰腺癌细胞系的生长。

Human pancreatic phospholipase A2 stimulates the growth of human pancreatic cancer cell line.

作者信息

Hanada K, Kinoshita E, Itoh M, Hirata M, Kajiyama G, Sugiyama M

机构信息

First Department of Internal Medicine, Hiroshima University School of Medicine, Japan.

出版信息

FEBS Lett. 1995 Oct 2;373(1):85-7. doi: 10.1016/0014-5793(95)01005-y.

DOI:10.1016/0014-5793(95)01005-y

PMID:7589440

Abstract

Phospholipase A2 (PLA2) from human pancreas, designated hPLA2-I, functions as a digestive enzyme. Interestingly, the present study demonstrated that the mature form of hPLA2-I stimulated the growth of a human pancreatic cancer cell line MIAPaCa-2, whereas the pro-form was ineffective. PLA2s from Laticauda semifasciata fraction I, Crotalus adamanteus venom, Streptomyces violaceoruber and bee venom, showed no proliferative effect to the growth of MIAPaCa-2. The Scatchard plot analysis revealed that the MIAPaCa-2 cell had a specific binding site for the mature hPLA2-I. The equilibrium binding constant (Kd) and the maximum binding capacity (Bmax) were 2.6 nM and 0.4 fmol/10(6) cells, respectively. These results suggest that the mature hPLA2-I, but not the pro-form, may function as a growth factor of pancreas carcinoma via the specific binding site.

摘要

来自人胰腺的磷脂酶A2（PLA2），命名为hPLA2-I，作为一种消化酶发挥作用。有趣的是，本研究表明，成熟形式的hPLA2-I可刺激人胰腺癌细胞系MIAPaCa-2的生长，而前体形式则无效。来自半环扁尾海蛇组分I、眼镜王蛇毒液、紫红红链霉菌和蜂毒的PLA2对MIAPaCa-2的生长没有增殖作用。Scatchard图分析显示，MIAPaCa-2细胞对成熟的hPLA2-I有特异性结合位点。平衡结合常数（Kd）和最大结合容量（Bmax）分别为2.6 nM和0.4 fmol/10(6)个细胞。这些结果表明，成熟的hPLA2-I而非前体形式可能通过特异性结合位点作为胰腺癌的生长因子发挥作用。