Characterization of the in vitro binding and inhibition kinetics of primary amine oxidase/vascular adhesion protein-1 by glucosamine.

Hdl Handle:
http://hdl.handle.net/10147/291083
Title:
Characterization of the in vitro binding and inhibition kinetics of primary amine oxidase/vascular adhesion protein-1 by glucosamine.
Authors:
Olivieri, Aldo; Tipton, Keith F; O'Sullivan, Jeff
Affiliation:
School of Biochemistry and Immunology, Trinity College Dublin, Ireland. oliviera@tcd.ie
Citation:
Characterization of the in vitro binding and inhibition kinetics of primary amine oxidase/vascular adhesion protein-1 by glucosamine. 2012, 1820 (4):482-7 Biochim. Biophys. Acta
Journal:
Biochimica et biophysica acta
Issue Date:
Apr-2012
URI:
http://hdl.handle.net/10147/291083
DOI:
10.1016/j.bbagen.2011.12.009
PubMed ID:
22202180
Abstract:
Primary-amine oxidase (PrAO) catalyzes the oxidative deamination of endogenous and exogenous primary amines and also functions, in some tissues, as an inflammation-inducible endothelial factor, known as vascular adhesion protein-1. VAP-1 mediates the slow rolling and adhesion of lymphocytes to endothelial cells in a number of inflammatory conditions, including inflammation of the synovium.
Item Type:
Article
Language:
en
MeSH:
Amine Oxidase (Copper-Containing); Animals; Cattle; Cell Adhesion; Deamination; Endothelial Cells; Glucosamine; Hydrogen Peroxide; Leukocyte Rolling; Lymphocytes; Osteoarthritis; Oxidation-Reduction
ISSN:
0006-3002

Full metadata record

DC FieldValue Language
dc.contributor.authorOlivieri, Aldoen_GB
dc.contributor.authorTipton, Keith Fen_GB
dc.contributor.authorO'Sullivan, Jeffen_GB
dc.date.accessioned2013-05-14T11:43:46Z-
dc.date.available2013-05-14T11:43:46Z-
dc.date.issued2012-04-
dc.identifier.citationCharacterization of the in vitro binding and inhibition kinetics of primary amine oxidase/vascular adhesion protein-1 by glucosamine. 2012, 1820 (4):482-7 Biochim. Biophys. Actaen_GB
dc.identifier.issn0006-3002-
dc.identifier.pmid22202180-
dc.identifier.doi10.1016/j.bbagen.2011.12.009-
dc.identifier.urihttp://hdl.handle.net/10147/291083-
dc.description.abstractPrimary-amine oxidase (PrAO) catalyzes the oxidative deamination of endogenous and exogenous primary amines and also functions, in some tissues, as an inflammation-inducible endothelial factor, known as vascular adhesion protein-1. VAP-1 mediates the slow rolling and adhesion of lymphocytes to endothelial cells in a number of inflammatory conditions, including inflammation of the synovium.en_GB
dc.language.isoenen
dc.rightsArchived with thanks to Biochimica et biophysica actaen_GB
dc.subject.meshAmine Oxidase (Copper-Containing)-
dc.subject.meshAnimals-
dc.subject.meshCattle-
dc.subject.meshCell Adhesion-
dc.subject.meshDeamination-
dc.subject.meshEndothelial Cells-
dc.subject.meshGlucosamine-
dc.subject.meshHydrogen Peroxide-
dc.subject.meshLeukocyte Rolling-
dc.subject.meshLymphocytes-
dc.subject.meshOsteoarthritis-
dc.subject.meshOxidation-Reduction-
dc.titleCharacterization of the in vitro binding and inhibition kinetics of primary amine oxidase/vascular adhesion protein-1 by glucosamine.en_GB
dc.typeArticleen
dc.contributor.departmentSchool of Biochemistry and Immunology, Trinity College Dublin, Ireland. oliviera@tcd.ieen_GB
dc.identifier.journalBiochimica et biophysica actaen_GB
dc.description.provinceLeinsteren

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