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

2.50
Hdl Handle:
http://hdl.handle.net/10541/90775
Title:
Oxidation of alpha1-proteinase inhibitor by the myeloperoxidase-hydrogen peroxidase system promotes binding to immunoglobulin A.
Authors:
Scott, Linda J; Russell, G I; Nixon, N B; Dawes, P T; Mattey, D L
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.
Affiliation:
Department of Haemopoeitic Cell and Gene Therapy, Paterson Institute for Cancer Research, Christie Hospital, Wilmslow Road, Manchester, M20 4BX, United Kingdom.
Citation:
Oxidation of alpha1-proteinase inhibitor by the myeloperoxidase-hydrogen peroxidase system promotes binding to immunoglobulin A. 1999, 255 (3):562-7 Biochem. Biophys. Res. Commun.
Journal:
Biochemical and Biophysical Research Communications
Issue Date:
24-Feb-1999
URI:
http://hdl.handle.net/10541/90775
DOI:
10.1006/bbrc.1999.0247
PubMed ID:
10049750
Type:
Article
Language:
en
ISSN:
0006-291X
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorScott, Linda Jen
dc.contributor.authorRussell, G Ien
dc.contributor.authorNixon, N Ben
dc.contributor.authorDawes, P Ten
dc.contributor.authorMattey, D Len
dc.date.accessioned2010-01-28T09:56:55Z-
dc.date.available2010-01-28T09:56:55Z-
dc.date.issued1999-02-24-
dc.identifier.citationOxidation of alpha1-proteinase inhibitor by the myeloperoxidase-hydrogen peroxidase system promotes binding to immunoglobulin A. 1999, 255 (3):562-7 Biochem. Biophys. Res. Commun.en
dc.identifier.issn0006-291X-
dc.identifier.pmid10049750-
dc.identifier.doi10.1006/bbrc.1999.0247-
dc.identifier.urihttp://hdl.handle.net/10541/90775-
dc.description.abstractWe 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.en
dc.language.isoenen
dc.subject.meshAnimals-
dc.subject.meshArthritis, Rheumatoid-
dc.subject.meshHumans-
dc.subject.meshHydrogen Peroxide-
dc.subject.meshImmunoglobulin A-
dc.subject.meshInflammation-
dc.subject.meshOxidation-Reduction-
dc.subject.meshPancreas-
dc.subject.meshPancreatic Elastase-
dc.subject.meshPeroxidase-
dc.subject.meshProtein Binding-
dc.subject.meshSerine Proteinase Inhibitors-
dc.subject.meshSwine-
dc.subject.meshalpha 1-Antitrypsin-
dc.titleOxidation of alpha1-proteinase inhibitor by the myeloperoxidase-hydrogen peroxidase system promotes binding to immunoglobulin A.en
dc.typeArticleen
dc.contributor.departmentDepartment of Haemopoeitic Cell and Gene Therapy, Paterson Institute for Cancer Research, Christie Hospital, Wilmslow Road, Manchester, M20 4BX, United Kingdom.en
dc.identifier.journalBiochemical and Biophysical Research Communicationsen
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