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.
MeSH Terms
Animals
Arthritis, Rheumatoid/metabolism
Cells, Cultured
Chromatography
DNA, Recombinant
Dinoprostone
Escherichia coli/genetics
Humans
Interleukin-1/genetics,physiology
Lymphocyte Activation
Mice
Mice, Inbred C3H
Microbial Collagenase/biosynthesis
Monocytes/metabolism
Prostaglandins E/biosynthesis
Recombinant Proteins
Synovial Membrane/metabolism
Chemicals
DNA, Recombinant
Interleukin-1
Prostaglandins E
Recombinant Proteins
Microbial Collagenase
Dinoprostone
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Dayer J M
de Rochemonteix B
Burrus B
Demczuk S
Dinarello C A
References (12)
12 references, click to expand
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