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J Biol Chem, Vol. 274, Issue 27, 18916-18924, July 2, 1999
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From the Human blood contains a form of minimally modified
low density lipoprotein (LDL), termed LDL Department of Molecular Pharmacology and
Toxicology, Washington
University School of Medicine, St. Louis, Missouri 63110, and
Karl-Franzens Universitat Graz,
Graz A8010, Austria
, whose
origin remains unknown. Exploring the mechanism of formation, we found
that LDL can be produced in plasma in the absence of
oxygen following LDL incubation with oxidized hemoglobin species. A
high degree of apolipoprotein B100 modification results from covalent
association of hemoglobin with LDL involving dityrosine formation but
not due to the malonaldehyde epitope formation. This was evidenced by
the cross-reactivity of oxidized LDL with antibodies against hemoglobin
that was accompanied by a 60-fold increase in dityrosine levels. In
this study we found significantly higher LDL levels in
the blood of hemodialysis patients, perhaps contributing to their
greatly increased risk of atherosclerosis. The mechanism of
LDL formation was studied during ex vivo
blood circulation using a model system resembling clinical hemodialysis
in terms of the induction of inflammatory responses. This circulation
increased free hemoglobin and LDL levels compared with
non-circulated blood without appreciable lipid peroxidation. Pronounced
increases in LDL were found also during circulation of
plasma supplemented with nanomolar hemoglobin levels. The increase in
dityrosine content and presence of heme in LDL after blood circulation
suggest that LDL is modified, in part, by hemoglobin-LDL conjugates
containing heme. Thus, hemoglobin-mediated reactions leading to LDL
oxidation in plasma can account for high LDL levels in
hemodialysis patients.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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