Uteroglobin inhibits phospholipase A2 activity

Life Sci. 1986 May 19;38(20):1813-9. doi: 10.1016/0024-3205(86)90135-9.

Abstract

Although progesterone is known to produce quiescence in the mammalian uterus, the mechanism of this effect is not clearly understood. Here, we report that uteroglobin, a progesterone-induced small molecular weight (16K) protein, inhibits phospholipase A2(PLA2) derived from porcine pancreas as well as from the RAW 264.7 macrophage cell line. We speculate that progesterone may exert its antimotility effects on the uterus via uteroglobin which, by inhibiting PLA2, decreases arachidonic acid release and subsequently reduces prostaglandin levels in this organ. This may explain why progesterone is so vital for the maintenance of pregnancy in almost all mammals.

MeSH terms

  • Animals
  • Arachidonic Acid
  • Arachidonic Acids / physiology
  • Calcium / pharmacology
  • Dose-Response Relationship, Drug
  • Female
  • Glycoproteins / pharmacology*
  • Hydrogen-Ion Concentration
  • Phospholipases / antagonists & inhibitors*
  • Phospholipases A / antagonists & inhibitors*
  • Phospholipases A2
  • Progesterone / pharmacology
  • Swine
  • Uterine Contraction / drug effects
  • Uteroglobin / pharmacology*

Substances

  • Arachidonic Acids
  • Glycoproteins
  • Arachidonic Acid
  • Progesterone
  • Uteroglobin
  • Phospholipases
  • Phospholipases A
  • Phospholipases A2
  • Calcium