Lipid-bound apolipoproteins in tyrosyl radical-oxidized HDL stabilize ABCA1 like lipid-free apolipoprotein A-I |
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| Authors: | Mohammad A Hossain Sereyrath Ngeth Teddy Chan Michael N Oda and Gordon A Francis |
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| Institution: | (1) Department of Medicine, UBC James Hogg Research Centre, Heart and Lung Institute, St. Paul’s Hospital, Vancouver, British Columbia, V6Z 1Y6, Canada;(2) Children’s Hospital Oakland Research Institute, Oakland, CA USA, 94609 |
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| Abstract: | Background ATP-binding cassette transporter A1 (ABCA1) mediates the lipidation of exchangeable apolipoproteins, the rate-limiting step
in the formation of high density lipoproteins (HDL). We previously demonstrated that HDL oxidized ex vivo by peroxidase-generated
tyrosyl radical (tyrosylated HDL, tyrHDL) increases the availability of cellular cholesterol for efflux and reduces the development
of atherosclerosis when administered to apolipoprotein E-deficient mice as compared to treatment with control HDL. |
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