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. 1986 Feb;77(2):645–648. doi: 10.1172/JCI112350

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

J M Dayer, B de Rochemonteix, B Burrus, S Demczuk, C A Dinarello
PMCID: PMC423407  PMID: 3003163

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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