Inhibition of ion transport ATPases by HNE

被引：8

作者：

Crifò, C

Capuozzo, E

Siems, W

Salerno, C

机构：

[1] Univ Roma La Sapienza, Lab Clin Biochem, I-00185 Rome, Italy

[2] Univ Roma La Sapienza, Dept Biochem Sci, I-00185 Rome, Italy

[3] Loges Sch Phys Med, Bad Harzburg, Germany

来源：

BIOFACTORS | 2005年 / 24卷 / 1-4期

关键词：

4-hydroxynonenal; lipid peroxidation; calcium pump; neutrophil membrane; erythrocyte ghosts;

D O I：

10.1002/biof.5520240116

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Hydroxy-2,3-trans-nonenal (HNE), a major lipid peroxidation product, has been shown to react with specific amino acid residues of proteins and alter their function. In vitro exposure of erythrocyte ghosts and neutrophil membranes to HNE results in the inhibition of ion transport ATPases. Neutrophil membrane Ca2+-ATPase is strongly inhibited by micromolar concentrations of HNE, while HNE is considerably less effective against neutrophil Mg2+-ATPase and the erythrocyte ghost enzymes.

引用

页码：137 / 140

页数：4

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[22] Succinylpurinemic autism:: increased sensitivity of defective adenylosuccinate lyase towards 4-hydroxy-2-nonenal [J].