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Defensins are antimicrobial and cytotoxic peptides that contain 29-35 amino acid residues, including six invariant cysteines whose intromolecular disulfide bonds cyclize and stabilize them in a complexly folded, triple stranded fj-sheet configuration. Generated by the proteolytic processing of 93-95 amino acid precursor peptides, they constitute> 5% of the total cellular protein in human and rabbit neutrophils (polymorphonucleated neutrophils-PMN) and are also produced by rabbit lung macrophages and by mouse and rabbit small intestinal Paneth cells. Despite their pro minence in rat PMN, defensins are not found in murine PMN. The anti microbial spectrum of defensins includes gram positive and gram negative bacteria, mycobacteria, T. pallidum, many fungi, and some enveloped 105 0732-0582/93/0410-0105$02.00 LEHRER ET AL viruses. Defensins exert nonspecific cytotoxic activity against a wide range of normal and malignant targets, including cells resistant to TNF-a and NK-cytolytic factor. They appear to kill mammalian target ce1\s and micro organisms by a common mechanism, which involves initial electrostatic interactions with negatively charged target ce1\ surface molecules (likely the head groups of polar membrane lipids), followed by insertion into the cell membranes which they permeabilize, forming voltage-regulated channels. In addition to their antimicrobial and cytotoxic properties, some defensins act as opsonins,
Annual Review of Immunology – Annual Reviews
Published: Apr 1, 1993
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