It has previously been demonstrated that CuZn-superoxide dismutase (SOD) is
secreted by several human cell lines. This suggests that the circulating e
nzyme derives from both hemolysis and peripheral tissues as a result of cel
lular secretion. In the present report, we evaluated the presence of CuZn-S
OD in human serum lipoproteins by both enzyme-linked immunosorbent assay an
d Western blot analysis of immunoprecipitated lipoprotein samples. The dist
ribution of CuZn-SOD activity among the different lipoprotein fractions was
also determined by the xanthine/xanthine oxidase method. The results demon
strated that CuZn-SOD is noticeably present in serum lipoproteins and mainl
y in low and high density lipoproteins (LDL and HDL). Moreover, experiments
performed by incubating CuZn-SOD with a lipid emulsion and subsequent sepa
ration of the lipid fraction by ultracentrifugation showed that this enzyme
associates in a saturable manner with lipids. The CuZn-SOD bound to LDL an
d HDL could exert a physiological protective role against oxidative damage
of these lipoprotein classes that carry out a crucial role in the cholester
ol transport. (C) 2000 Federation of European Biochemical Societies.