Human recombinant interleukin 1 stimulates collagenase and prostaglandin E2 production by human synovial cells

J Clin Invest. 1986 Feb;77(2):645-8. doi: 10.1172/JCI112350.

Abstract

The pathogenesis and progression of rheumatoid arthritis involves the production of biologically active lymphokines and monokines. Of these, interleukin 1 (IL-1) has been somewhat of a controversial molecule because it seems to evoke various biological responses in several different tissues. In these studies we demonstrate that three biological properties of human monocyte-derived IL-1 (T-lymphocyte activation and human synovial cell prostaglandin E2 and collagenase production) co-purify. The complementary DNA for the prominent pI 7 form of human IL-1 was expressed, purified, and tested. Any controversy now appears resolved since homogeneous recombinant human IL-1 stimulates prostaglandin E2 and collagenase from human synovial cells as well as activates T cells in vitro.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Arthritis, Rheumatoid / metabolism*
  • Cells, Cultured
  • Chromatography
  • DNA, Recombinant
  • Dinoprostone
  • Escherichia coli / genetics
  • Humans
  • Interleukin-1 / genetics
  • Interleukin-1 / physiology*
  • Lymphocyte Activation
  • Mice
  • Mice, Inbred C3H
  • Microbial Collagenase / biosynthesis*
  • Monocytes / metabolism
  • Prostaglandins E / biosynthesis*
  • Recombinant Proteins
  • Synovial Membrane / metabolism*

Substances

  • DNA, Recombinant
  • Interleukin-1
  • Prostaglandins E
  • Recombinant Proteins
  • Microbial Collagenase
  • Dinoprostone