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J. Biol. Chem., Vol. 262, Issue 20, 9914-9920, 07, 1987
KJ Davies, SW Lin and RE Pacifici
Proteolytic degradation of oxidatively damaged [3H] bovine serum albumin [(
3H]BSA) was studied during incubation with cell-free erythrocyte extracts
and a wide variety (14) of purified proteases. [3H]BSA was pretreated by
exposure (60Co radiation) to the hydroxyl radical (.OH), the superoxide
anion radical (O2-), or the combination of .OH + O2- + oxygen. Treated (and
untreated) samples were dialyzed and then incubated with erythrocyte
extract or proteases for measurements of proteolytic susceptibility
(release of acid-soluble counts). Both .OH and .OH + O2- + caused
severalfold increases in proteolytic susceptibility (with extract and
proteases), but O2- alone had no effect. Proteolytic susceptibility reached
a maximum at 15 nmol of .OH/nmol of BSA and declined thereafter. In
contrast, proteolytic susceptibility was still increasing at an .OH +
O2-/BSA molar ratio of 100 (50% .OH + 50% O2-). Degradation in erythrocyte
extracts was conducted by a novel ATP- and Ca2+-independent pathway, with
maximal activity at pH 7.8. Inhibitor profiles indicate that this pathway
may involve metalloproteases and serine proteases. Comparisons of
proteolytic susceptibility with multiple modifications to BSA primary,
secondary, and tertiary structure revealed a high correlation (r = 0.98)
with denaturation/increased hydrophobicity by low concentrations of .OH.
Covalent aggregation reactions (BSA cross-linking) may explain the
declining proteolytic susceptibility observed at .OH/BSA molar ratios
greater than 20. Protein denaturation may also have caused the increased
proteolytic susceptibility induced by .OH + O2- + O2, but no simple
correlation could be obtained. Results with .OH + O2- + O2 appear to have
been complicated by direct BSA fragmentation reactions involving
(.OH-induced) protein radicals and oxygen. These data indicate a direct and
quantitative relationship between protein damage by oxygen radicals and
increased proteolytic susceptibility. Oxidative denaturation may exemplify
a simple, yet effective inherent mechanism for intracellular proteolysis.
Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein
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