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  • Title: Biochemical, metabolic and morphological characteristics of human neutrophil activation with pepstatin A.
    Author: Smith RJ, Bowman BJ, Iden SS, Kolaja GJ, Wiser SK.
    Journal: Immunology; 1983 Jun; 49(2):367-77. PubMed ID: 6303951.
    Abstract:
    Pepstatin A, a chemotactic pentapeptide, elicited a concentration-dependent extracellular release of granule-associated beta-glucuronidase and lysozyme from, and generation of superoxide anion (O2-) by, cytochalasin B (CB)-treated human neutrophils. Prior exposure of neutrophils to pepstatin A before the addition of CB, suppressed, in a time-dependent fashion, the subsequent production of O2- and exocytotic response. The rate and amount of enzymes released and O2- generated by pepstatin A-activated neutrophils were significantly enhanced in the presence of extracellular calcium. Pepstatin A-elicited degranulation and O2- production were suppressed by the intracellular calcium antagonist, 8-(N,N-diethylamino)-octyl-(3, 4, 5-trimethoxy) benzoate hydrochloride (TMB-8). Granule exocytosis and O2- generation by pepstatin A-treated neutrophils were suppressed by the sulphydryl reagents, N-ethylmaleimide (NEM) and iodoacetic acid (IA), and by the glycolytic inhibitor, 2-deoxy-D-glucose (2-DG). Sodium cyanide was inactive. Preincubation of neutrophils with pepstatin A "desensitized' the cells to a subsequent exposure to pepstatin A or the chemotactic tripeptide, N-formyl-methionyl-leucyl-phenylalanine (FMLP). Pepstatin A-induced desensitization of granule enzyme release and O2- generation appears to be stimulus-specific in that phorbol myristate acetate (PMA) was capable of eliciting normal responses from pepstatin A-pretreated cells. The morphological changes observed in pepstatin A-treated neutrophils are reminiscent of those seen in cells exposed to FMLP.
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