NDLI: Association of myeloperoxidase with heparin: Oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme

Content Provider	Springer Nature Link
Author	Daphna, Efrati Machluf Michaela, Sharabani Eynat, Peles Irit, Aviram Sara, Rimon
Copyright Year	1998
Abstract	Chromatography of human myeloperoxidase (MPO) on a heparin-agarose column demonstrated a tight association of the protein with the resin. The electrophoretic mobility of mixtures of MPO and heparin in polyacrylamide gels under nondenaturing conditions was consistent with a strong interaction of the cationic enzyme with the polyanionic polysaccharide. Purified MPO prebound to bovine aorta endothelial cells (BAEC) and supplemented with hydrogen peroxide dose- and time-dependently abrogated the interaction of coagulation factor IX (FIX) with factor IX-binding protein (FIXBP) on the surface of BAEC reflecting oxidative modification of the binding protein. This inactivation of FIXBP required the presence of chloride implicating hypochlorite in the reaction. Hypochlorite and activated neutrophils exerted a similar effect. The oxidative modification of FIXBP was only partially dependent on the addition of hydrogen peroxide and was abolished by exogenous heparin which displaced MPO from the cell surface, emphasizing the functional differences between cell-bound and free enzyme.
Starting Page	55
Ending Page	61
Page Count	7
File Format	PDF
ISSN	03008177
Journal	Molecular and Cellular Biochemistry
Volume Number	183
Issue Number	1-2
e-ISSN	15734919
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1998-01-01
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Cardiology Medical Biochemistry Oncology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Clinical Biochemistry Molecular Biology

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