Inhibition of ion transport ATPases by HNE.
4-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.
Crifò
C
C
Department of Biochemical Sciences and Laboratory of Clinical Biochemistry, University of Rome La Sapienza, Rome, Italy.
Capuozzo
E
E
Siems
W
W
Salerno
C
C
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000447:Aldehydes / Q000494:pharmacology*; D017301:Ca(2+) Mg(2+)-ATPase / Q000037:antagonists & inhibitors; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors; D002462:Cell Membrane / Q000201:enzymology; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004910:Erythrocyte Membrane / Q000201:enzymology; D006801:Humans; D015227:Lipid Peroxidation; D009504:Neutrophils / Q000201:enzymology
D000447:Aldehydes; D004791:Enzyme Inhibitors; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases; C027576:4-hydroxy-2-nonenal