Publication: Xanthine oxidoreductase and xanthine oxidase in human cornea
Authors
Cejkova, J. ; Ardan, T. ; Filipec, M. ; Midelfart, A.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Xanthine oxidoreductase (xanthine
dehydrogenase + xanthine oxidase) is a complex enzyme
that catalyzes the oxidation of hypoxanthine to xanthine,
subsequently producing uric acid. The enzyme complex
exists in separate but interconvertible forms, xanthine
dehydrogenase and xanthine oxidase, which generate
reactive oxygen species (ROS), a well known causative
factor in ischemia/reperfusion injury and also in some
other pathological states and diseases. Because the
enzymes had not been localized in human corneas until
now, the aim of this study was to detect xanthine
oxidoreductase and xanthine oxidase in the corneas of
normal post-mortem human eyes using histochemical
and immunohistochemical methods. Xanthine
oxidoreductase activity was demonstrated by the
tetrazolium salt reduction method and xanthine oxidase
activity was detected by methods based on cerium ion
capture of hydrogen peroxide. For immunohistochemical
studies, we used rabbit antibovine xanthine oxidase
antibody, rabbit antihuman xanthine oxidase antibody
and monoclonal mouse antihuman xanthine
oxidase/xanthine dehydrogenase/aldehyde oxidase
antibody. The results show that the enzymes are present
in the corneal epithelium and endothelium. The activity
of xanthine oxidoreductase is higher than that of
xanthine oxidase, as clearly seen in the epithelium.
Further studies are necessary to elucidate the role of
these enzymes in the diseased human cornea. Based on
the findings obtained in this study (xanthine
oxidoreductase/xanthine oxidase activities are present in
normal human corneas), we hypothesize that during
various pathological states, xanthine oxidase-generated
ROS might be involved in oxidative eye injury.
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