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J Biol Chem, Vol. 274, Issue 34, 23787-23793, August 20, 1999
,
From the Laboratory of Food and Biodynamics, Oxidative stress is associated with
important pathophysiological events in a variety of diseases. It has
been postulated that free radicals and lipid peroxidation products
generated during the process may be responsible for these effects
because of their ability to damage cellular components such as
membranes, proteins, and DNA. In the present study, we provide evidence
that oxidative stress causes a transient impairment of intracellular
proteolysis via covalent binding of 4-hydroxy-2-nonenal (HNE), a major
end product of lipid peroxidation, to proteasomes. A single
intraperitoneal treatment with the renal carcinogen, ferric
nitrilotriacetate, caused oxidative stress, as monitored by
accumulation of lipid peroxidation products and
8-hydroxy-2'-deoxyguanosine, in the kidney of mice. In addition,
transient accumulation of HNE-modified proteins in the kidney was also
found by competitive enzyme-linked immunosorbent assay and
immunohistochemical analyses. This and the observation that the
HNE-modified proteins were significantly ubiquitinated suggested a
crucial role of proteasomes in the metabolism of HNE-modified proteins.
In vitro incubation of the kidney homogenates with HNE
indeed resulted in a transient accumulation of HNE-modified proteins,
whereas the proteasome inhibitor significantly suppressed the
time-dependent elimination of HNE-modified proteins. We
found that, among three proteolytic activities (trypsin, chymotrypsin, and peptidylglutamyl peptide hydrolase activities) of proteasomes, both
trypsin and peptidylglutamyl peptide hydrolase activities in the kidney
were transiently diminished in accordance with the accumulation of
HNE-modified proteins during oxidative stress. The loss of proteasome
activities was partially ascribed to the direct attachment of HNE to
the protein, based on the detection of HNE-proteasome conjugates by an
immunoprecipitation technique. These results suggest
that HNE may contribute to the enhanced accumulation of oxidatively
modified proteins via an impairment of ubiquitin/proteasome-dependent
intracellular proteolysis.
Department of Pathology and Biology of Diseases,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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