Interleukin-1 activates phospholipase A2 in human synovial cells

Arthritis Rheum. 1988 Jan;31(1):126-30. doi: 10.1002/art.1780310118.

Abstract

Interleukin-1 (IL-1) treatment of synovial cells from rheumatoid arthritis and osteoarthritis patients resulted in a dose-dependent secretion of phospholipase A2 (PLA2). IL-1 also stimulated prostaglandin E2 and plasminogen activator synthesis, in parallel with PLA2 activation; all 3 were detectable within 6 hours of IL-1 treatment and peaked by 24 hours. Synovial cell PLA2 required calcium (5 mM) and a neutral pH (7.5) for maximal activity and appears similar to the PLA2 in synovial fluid, which has been described previously. We conclude that PLA2 can be induced by IL-1, and its secretion may contribute significantly to the inflammatory actions of IL-1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arthritis, Rheumatoid / enzymology
  • Arthritis, Rheumatoid / metabolism
  • Arthritis, Rheumatoid / pathology
  • Calcium / pharmacology
  • Dinoprostone
  • Enzyme Activation
  • Humans
  • Hydrogen-Ion Concentration
  • Interleukin-1 / pharmacology*
  • Kinetics
  • Osteoarthritis / enzymology
  • Osteoarthritis / metabolism
  • Osteoarthritis / pathology
  • Phospholipases / metabolism*
  • Phospholipases A / metabolism*
  • Phospholipases A2
  • Plasminogen Activators / metabolism
  • Prostaglandins E / metabolism
  • Synovial Membrane / enzymology*
  • Synovial Membrane / metabolism
  • Synovial Membrane / pathology

Substances

  • Interleukin-1
  • Prostaglandins E
  • Phospholipases
  • Phospholipases A
  • Phospholipases A2
  • Plasminogen Activators
  • Dinoprostone
  • Calcium