Faculty Collaboration Database

Is the oxidation of high-density lipoprotein lipids different than the oxidation of low-density lipoprotein lipids? Biochemistry 2001 Feb 13;40(6):1719-24

Date

05/01/2001

Pubmed ID

11327832

DOI

10.1021/bi0022442

Scopus ID

2-s2.0-0035852830 (requires institutional sign-in at Scopus site)   18 Citations

Abstract

This article gives detailed insight into the kinetics of high-density lipoprotein (HDL) oxidation catalyzed by azobis(2-amidinopropane).dihydrochloride (ABAP) or by copper. ABAP initialized oxidation of human HDL 3-4 times faster than non-human primate HDL with a similar composition. The oxidizability of non-human primate HDL was 1000 times lower than the oxidizability calculated from rate constants derived from liposome oxidation, suggesting that there is a slow step in HDL oxidation not present in liposomes. Saturable binding of copper to HDL was a significant feature of copper-catalyzed oxidation. Binding constants (K(m)) for non-human primate HDL were 2-3-fold lower than those for human HDL. Copper-catalyzed oxidation of non-human primate HDL was slower than that of human HDL, but human HDL(2) and HDL(3) oxidized at about the same rate. Overall, the kinetics describing the oxidation of HDL were mechanistically similar to those reported for LDL, suggesting that HDL lipids were as easily oxidized as LDL lipids and that HDL will be easily oxidized in vivo when exposed to agents that oxidize LDL.

Author List

Thomas MJ, Chen Q, Zabalawi M, Anderson R, Wilson M, Weinberg R, Sorci-Thomas MG, Rudel LL

Authors

Mary Sorci Thomas PhD Professor in the Medicine department at Medical College of Wisconsin
Michael J. Thomas PhD Professor in the Pharmacology and Toxicology department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Amidines
Animals
Binding Sites
Cholesterol Esters
Copper
Free Radicals
Humans
Lipid Peroxidation
Lipoproteins, HDL
Lipoproteins, LDL
Oxidants
Solutions