Abstract
Lipid peroxidation results in release of 4-hydroxy-2,3- trans-nonenal (HNE), which is known to conjugate to specific amino acids of proteins and may alter their function. The effect of HNE on the activities of Na +/K +-ATPase, Mg 2+-ATPase, Ca 2+-ATPase, and calmodulin-stimulated Ca 2+-ATPase has been studied both in erythrocyte ghosts and in neutrophil membrane preparations. Neutrophil Ca 2+-ATPase was strongly inhibited by micromolar concentrations of HNE (IC 50 = 12 μM), that means in the range of pathophysiologically relevant HNE levels. The IC 50 value for neutrophil Na +/K +-ATPase was about 40 μM. HNE was considerably less effective against neutrophil Mg 2+-ATPase and the erythrocyte ghost enzymes (IC 50 values range from 91 to 240 μM). The data suggest that HNE may play a specific role in the regulation of neutrophil calcium homeostasis in response to oxidative stress.
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