Albumin-bound quercetin repairs vitamin E oxidized by apolipoprotein radicals in native HDL3 and LDL
Albumin-bound quercetin repairs vitamin E oxidized by apolipoprotein radicals in native HDL3 and LDL
复制标题
DOI:
10.1021/bi701419d
复制
发表时间:
2007-12-11
期刊:
影响因子:
2.9
通讯作者:
Morliere, Patrice
中科院分区:
文献类型:
--
作者:
Filipe, Paulo;Patterson, Larry K.;Morliere, Patrice
In the minor fraction of HDL3 containing alpha-tocopherol (alpha TocOH), selective one-electron oxidation of Trp and Tyr residues of apolipoproteins A-I and A-II by Br-center dot(2)- radical-anions produces the corresponding sernioxidized species, TyrO(center dot) and (center dot)Trp. Repair of TyrO(center dot) by endogenous alpha TocOH generates the a-tocopheroxyl radical (alpha TocO(center dot)). Fast spectroscopic studies show that two populations representing 80% of alpha TocO(center dot) initially formed are repaired over several seconds with rate constants of 3.0 x 10(6) and 1.5 x 10(5) M-1 s(-1) by quercetin bound to human serum albumin (HSA) at physiologically relevant concentration. Formation of HSA-bound quercetin radicals ((center dot)Q(b)) is observed. In the major fraction of HDL3 particles lacking alpha TocOH, TyrO(center dot) and (center dot)Trp are repaired by free and HSA-bound quercetin. In LDL particles which all contain alpha TocOH, alpha TocO(center dot) radicals are formed in the millisecond time scale by repair of TyrO(center dot) radicals produced in apolipoprotein B. Then, 75% of initial alpha TocO(center dot) are repaired over seconds by HSA-bound quercetin (rate constant: 2.0 x 10(6) M-1 s(-1)). HSA-bound quercetin can also repair (center dot)Trp radicals. In O-2-saturated solutions, the fraction of alpha TocO(center dot) radicals (more than 50%) not repaired by superoxide radical-anions can be repaired by HSA-bound quercetin with formation Of (center dot)Q(b) but to a much lesser extent in LDL than in HDL.