Purification, cloning, expression and biological characterization of an interleukin-1 receptor antagonist protein.

Abstract:

:A human myelomonocytic cell line, U937, produced an interleukin-1 (IL-1) receptor antagonist protein (IRAP) which was purified and partially sequenced. A complementary DNA coding for IRAP was cloned and sequenced. The mature translation product of the cDNA has been expressed in Escherichia coli and was an active competitive inhibitor of the binding of IL-1 to the T-cell/fibroblast form of the IL-1 receptor. Recombinant IRAP specifically inhibited IL-1 bioactivity on T cells and endothelial cells in vitro and was a potent inhibitor of IL-1 induced corticosterone production in vivo.

journal_name

Nature

journal_title

Nature

authors

Carter DB,Deibel MR Jr,Dunn CJ,Tomich CS,Laborde AL,Slightom JL,Berger AE,Bienkowski MJ,Sun FF,McEwan RN

doi

10.1038/344633a0

subject

Has Abstract,Author List Incomplete

pub_date

1990-04-12 00:00:00

pages

633-8

issue

6267

eissn

0028-0836

issn

1476-4687

journal_volume

344

pub_type

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