Affiliations: Department of Biochemical Sciences and Laboratory of
Clinical Biochemistry, University of Rome La Sapienza, Rome, Italy | Loges-School of Physical Medicine, Bad Harzburg,
Germany
Note: [] Address for correspondence: C. Salerno, Laboratory of Clinical
Biochemistry, via dei Sardi 58, 00185 Roma, Italy. Tel./Fax: +39 064463776;
E-mail: costantino.salerno@uniromal.it
Abstract: 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 Ca^{2+}-ATPase is strongly inhibited by
micromolar concentrations of HNE, while HNE is considerably less effective
against neutrophil Mg^{2+}-ATPase and the erythrocyte ghost
enzymes.
