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Meprin A and meprin alpha generate biologically functional IL-1beta from pro-IL-1beta.

Abstract：

:The present study demonstrates that both oligomeric metalloendopeptidase meprin A purified from kidney cortex and recombinant meprin alpha are capable of generating biologically active IL-1beta from its precursor pro-IL-1beta. Amino-acid sequencing analysis reveals that meprin A and meprin alpha cleave pro-IL-1beta at the His(115)-Asp(116) bond, which is one amino acid N-terminal to the caspase-1 cleavage site and five amino acids C-terminal to the meprin beta site. The biological activity of the pro-IL-1beta cleaved product produced by meprin A, determined by proliferative response of helper T-cells, was 3-fold higher to that of the IL-1beta product produced by meprin beta or caspase-1. In a mouse model of sepsis induced by cecal ligation puncture that results in elevated levels of serum IL-1beta, meprin inhibitor actinonin significantly reduces levels of serum IL-1beta. Meprin A and meprin alpha may therefore play a critical role in the production of active IL-1beta during inflammation and tissue injury.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Herzog C,Haun RS,Kaushal V,Mayeux PR,Shah SV,Kaushal GP

doi

10.1016/j.bbrc.2008.12.161

subject

Has Abstract

pub_date

2009-02-20 00:00:00

pages

904-8

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)02568-0

journal_volume

379

pub_type

杂志文章

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