Oxidized low-density lipoprotein (Ox-LDL) impacts on erythrocyte viscoelasticity and its molecular mechanism.
The oxidized low-density lipoprotein (Ox-LDL) plays an important role in atherosclerosis, yet it remains unclear if it damages circulating erythrocytes. In this study, erythrocyte deformability and its membrane proteins after Ox-LDL incubations are investigated by micropipette aspiration, thiol radical measurement, and sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Results show that Ox-LDL incubation reduces the erythrocyte deformability, decreases free thiol radical contents in erythrocytes, and induces the cross-linking among membrane proteins. SDS-PAGE analysis reveals a high molecular weight (HMW) complex as well as new bands between spectrins and band 3 and reduced ratios between band 3 and other major membrane skeletal proteins. Analyses indicate that Ox-LDL makes erythrocytes harder to deform through a molecular mechanism by which the oxidation of free thiol radicals forms disulfide bonds among membrane skeletal proteins.
Wang
Xiang
X
Key Laboratory of Biorheological Science and Technology (Chongqing University), Ministry of Education, College of Bioengineering, Chongqing 400044, PR China. xwangchn@cqu.edu.cn
Yang
Li
L
Liu
Yao
Y
Gao
Wei
W
Peng
Weiyan
W
Sung
K-L Paul
KL
Sung
Lanping Amy
LA
D002478:Cells, Cultured; D003198:Computer Simulation; D055119:Elastic Modulus / Q000187:drug effects / Q000502:physiology; D004912:Erythrocytes / Q000187:drug effects* / Q000502:physiology*; D006801:Humans; D008077:Lipoproteins, LDL / Q000494:pharmacology*; D008955:Models, Cardiovascular; D014783:Viscosity / Q000187:drug effects
D008077:Lipoproteins, LDL; C099252:oxidized low density lipoprotein