Proliferative effect of phospholipase A2 in rat chondrocyte via its specific binding sites

Biochem Biophys Res Commun. 1992 Jul 31;186(2):1025-31. doi: 10.1016/0006-291x(92)90849-g.

Abstract

We studied the presence of specific binding sites for pancreatic-type group I phospholipase A2 (PLA2-I), EC 3.1.1.4, and a PLA2-I action on the DNA synthesis of rat chondrocytes. Rat chondrocytes, derived from the xiphisternum of adult rats, had a single class of PLA2-I binding site with an equilibrium binding constant value of 0.9 nM and a maximum binding capacity of 53.9 fmol/10(6) cells. PLA2-I alone did not show any proliferative effect, however, PLA2-I dose-dependently stimulated thymidine incorporation in DNA in the presence of basic fibroblast growth factor (bFGF). The mammalian mature type of PLA2s-I specifically recognized the binding sites in these cells and had a synergistic effect on DNA synthesis with bFGF, whereas its inactive zymogen and group II PLA2 showed much lesser activities. The type-specific action of PLA2s implicated the involvement of PLA2-I specific binding sites in this activation process.

MeSH terms

  • Animals
  • Binding Sites
  • Cartilage / cytology*
  • Cartilage / drug effects
  • Cartilage / metabolism
  • Cell Division / drug effects
  • Cells, Cultured
  • DNA Replication / drug effects*
  • Indomethacin / pharmacology
  • Kinetics
  • Phospholipases A / metabolism*
  • Phospholipases A / pharmacology*
  • Phospholipases A2
  • Rats
  • Rats, Inbred Strains
  • Swine

Substances

  • Phospholipases A
  • Phospholipases A2
  • Indomethacin