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J Biol Chem, Vol. 274, Issue 8, 4985-4994, February 19, 1999
§,¶,§,
,§¶
From the Departments of Concentrations of up to 1.5 milliunits/ml
xanthine oxidase (XO) (1.1 µg/ml) are found circulating in plasma
during diverse inflammatory events. The saturable, high affinity
binding of extracellular XO to vascular endothelium and the effects of
cell binding on both XO catalytic activity and differentiated vascular
cell function are reported herein. Xanthine oxidase purified from
bovine cream bound specifically and with high affinity
(Kd = 6 nM) at 4 °C to bovine aortic
endothelial cells, increasing cell XO specific activity up to 10-fold.
Xanthine oxidase-cell binding was not inhibited by serum or albumin and
was partially inhibited by the addition of heparin. Pretreatment of
endothelial cells with chondroitinase, but not heparinase or
heparitinase, diminished endothelial binding by ~50%, suggesting
association with chondroitin sulfate proteoglycans. Analysis of rates
of superoxide production by soluble and cell-bound XO revealed that
endothelial binding did not alter the percentage of univalent reduction
of oxygen to superoxide. Comparison of the extent of CuZn-SOD
inhibition of native and succinoylated cytochrome c
reduction by cell-bound XO indicated that XO-dependent
superoxide production was occurring in a cell compartment inaccessible
to CuZn-SOD. This was further supported by the observation of a shift
of exogenously added XO from extracellular binding sites to
intracellular compartments, as indicated by both protease-reversible
cell binding and immunocytochemical localization studies.
Endothelium-bound XO also inhibited nitric oxide-dependent
cGMP production by smooth muscle cell co-cultures in an SOD-resistant
manner. This data supports the concept that circulating XO can bind to
vascular cells, impairing cell function via oxidative mechanisms, and
explains how vascular XO activity diminishes vasodilatory responses to
acetylcholine in hypercholesterolemic rabbits and atherosclerotic
humans. The ubiquity of cell-XO binding and endocytosis as a
fundamental mechanism of oxidative tissue injury is also affirmed by
the significant extent of XO binding to human vascular endothelial
cells, rat lung type 2 alveolar epthelial cells, and fibroblasts.
Biochemistry and Molecular
Genetics and ¶ Anesthesiology and the § Center for Free
Radical Biology, University of Alabama at Birmingham, Birmingham,
Alabama 35233 and the Department of Clinical Chemistry, Umeå
University Hospital, Umeå, Sweden
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