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J. Biol. Chem., Vol. 262, Issue 17, 8227-8234, 06, 1987
KJ Davies and AL Goldberg
We have suggested that red blood cell proteolytic systems can degrade
oxidatively damaged proteins, and that both damage and degradation are
independent of lipid peroxidation (Davies, K. J. A., and Goldberg, A. L.
(1987) J. Biol. Chem. 262, 8220-8226. These ideas have now been tested in
cell-free extracts of rabbit erythrocytes and reticulocytes. Exposure to
oxygen radicals or H2O2 increases the degradation of endogenous proteins in
cell-free extracts, as in intact cells. Various radical-generating systems
(acetaldehyde or xanthine + xanthine oxidase, ascorbic acid + iron, H2O2 +
iron) and H2O2 alone enhanced the rates of proteolysis severalfold. Since
these extracts were free of membrane lipids, protein damage and degradation
must be independent of lipid peroxidation. An antioxidant buffer consisting
of HEPES, glycerol, and dithiothreitol inhibited the increased proteolysis
by 60- 100%. Mannitol caused a 50-80% reduction in proteolysis suggesting
that the hydroxyl radical (.OH), or a species with similar reactivity, may
be the initiator of protein damage. When casein or bovine serum albumin
were exposed to .OH (generated by H2O2 + Fe2+, or COCo radiation) these
proteins were degraded up to 50 times faster than untreated proteins during
subsequent incubations with red cell extracts. Mannitol inhibited this
increase in proteolysis only if present during .OH exposure; mannitol did
not affect the degradative system. Although ATP increased the degradation
of untreated proteins 4- to 6-fold in reticulocyte extracts, it had little
or no effect on the degradation of proteins exposed to .OH. ATP also did
not stimulate hydrolysis of .OH- treated proteins in erythrocyte extracts.
Leupeptin did not affect the degradative processes in either extract; thus
lysosomal or Ca2+- activated thiol proteases were not involved. We propose
that red cells contain a soluble, ATP-independent proteolytic pathway which
may protect against the accumulation of proteins damaged by .OH or other
active oxygen species.
Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells
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