Human recombinant interleukin 1 stimulates collagenase and prostaglandin E2 production by human synovial cells.
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.
D000818:Animals; D001172:Arthritis, Rheumatoid / Q000378:metabolism*; D002478:Cells, Cultured; D002845:Chromatography; D004274:DNA, Recombinant; D015232:Dinoprostone; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D007375:Interleukin-1 / Q000235:genetics / Q000502:physiology*; D008213:Lymphocyte Activation; D051379:Mice; D008809:Mice, Inbred C3H; D003012:Microbial Collagenase / Q000096:biosynthesis*; D009000:Monocytes / Q000378:metabolism; D011458:Prostaglandins E / Q000096:biosynthesis*; D011994:Recombinant Proteins; D013583:Synovial Membrane / Q000378:metabolism*
D004274:DNA, Recombinant; D007375:Interleukin-1; D011458:Prostaglandins E; D011994:Recombinant Proteins; D003012:Microbial Collagenase; D015232:Dinoprostone