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Oxidation of alpha1-proteinase inhibitor by the myeloperoxidase-hydrogen peroxidase system promotes binding to immunoglobulin A.

Abstract：

:We have demonstrated previously that patients with rheumatoid arthritis (RA) show an increase in serum and synovial fluid levels of complexes between alpha1-proteinase inhibitor (alpha1PI) and IgA. These are believed to form through disulfide binding between the Cys232 residue on alpha1PI and the penultimate cysteine residue (Cys471) of the IgA alpha chain. The mechanism for this has not been elucidated. We show here that alpha1PI oxidized by the myeloperoxidase-hydrogen peroxide (MPO-H2O2) system promotes the formation of IgA-alpha1PI complexes when incubated with IgA and that such complexes have no inhibitory activity against porcine pancreatic elastase (PPE). The activity of alpha1PI was considerably reduced also in IgA-alpha1PI complexes isolated from serum of an RA patient. We suggest that formation of IgA-alpha1PI complexes in inflammation may involve oxidation of alpha1PI, and as a consequence the alpha1PI in such complexes has reduced elastase inhibitory activity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Scott LJ,Russell GI,Nixon NB,Dawes PT,Mattey DL

doi

10.1006/bbrc.1999.0247

subject

Has Abstract

pub_date

1999-02-24 00:00:00

pages

562-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(99)90247-4

journal_volume

255

pub_type

杂志文章

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