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Oxidized low-density lipoprotein (Ox-LDL) impacts on erythrocyte viscoelasticity and its molecular mechanism.

Abstract：

: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.

journal_name

J Biomech

journal_title

Journal of biomechanics

authors

Wang X,Yang L,Liu Y,Gao W,Peng W,Sung KL,Sung LA

doi

10.1016/j.jbiomech.2009.05.026

subject

Has Abstract

pub_date

2009-10-16 00:00:00

pages

2394-9

issue

14

eissn

0021-9290

issn

1873-2380

pii

S0021-9290(09)00319-4

journal_volume

42

pub_type

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