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

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

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.

Publication types

  • Comparative Study

MeSH terms

  • Bee Venoms
  • Cell Division / drug effects*
  • Dose-Response Relationship, Drug
  • Enzyme Precursors / pharmacology
  • Humans
  • Kinetics
  • Pancreas / enzymology*
  • Pancreatic Neoplasms
  • Phospholipases A / isolation & purification
  • Phospholipases A / metabolism
  • Phospholipases A / pharmacology*
  • Phospholipases A2
  • Protein Binding
  • Snake Venoms
  • Tumor Cells, Cultured

Substances

  • Bee Venoms
  • Enzyme Precursors
  • Snake Venoms
  • Phospholipases A
  • Phospholipases A2