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Binding of the lipid peroxidation product 4-hydroxynonenal to human polymorphonuclear leukocytes

✍ Scribed by M. Curzio; C. Ferretti; R. J. Stephens; H. Esterbauer; M. U. Dianzani

Publisher: John Wiley and Sons
Year: 1994
Tongue: English
Weight: 397 KB
Volume: 12
Category: Article
ISSN: 0263-6484
DOI: 10.1002/cbf.290120108

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✦ Synopsis

i y ; 11 Life Sciences Division, Ceri 4-Hydroxynonenal (HNE) is produced during peroxidation of polyunsaturated fatty acids. It exerts a chemokinetic effect on human polymorphonuclear leukocytes (PMN). Investigations of this mechanism were performed. The results indicate that [3H]-HNE binding to PMN results both in non-specific bonds to the numerous SH groups of the cells and in binding to a saturable, reversible and specific HNE site. Scatchard analysis revealed that this is a single site with an apparent affinity constant of 319 nM and a density of 1.57 pmol ( lo6)-' cells. This specific binding site may be involved in the chemokinetic effect of HNE.

KEY wo~os-4-hydroxynoneno~; lipid peroxidation; human polymorphonuclear leukocytes; chemokinesis.

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Made possible by grants from Consiglio Nazionale delle Ricerche in the frame of the Strategic Project on Cellular and Oxidative Stress and of the Targeted Project on Biotechnology (contracts no. 97.01181.49 and no. 97.01126.49), from Ministry of the University in the frame of the Project Biomarkers