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  • Title: Ligation of selectin L and integrin CD11b/CD18 (Mac-1) induces release of gelatinase B (MMP-9) from human neutrophils.
    Author: Wize J, Sopata I, Smerdel A, Maśliński S.
    Journal: Inflamm Res; 1998 Aug; 47(8):325-7. PubMed ID: 9754865.
    Abstract:
    OBJECTIVE AND DESIGN: To examine whether ligation of the adhesive receptors - selectin L and Mac-1 on the neutrophil surface could induce gelatinase B exocytosis. MATERIALS: Neutrophils were isolated from fresh heparinized blood of human donors by Gradisol G centrifugation and hypotonic lysis of erythrocytes. METHODS: Integrin CD1 1b/CD18 and selectin L mediated adhesive interaction of human neutrophils were mimicked by binding antibodies to these receptors on the surface of isolated leukocytes. Neutrophils (5 x 10(6)/ml) were incubated with antibodies against selectin L (40/microg/ml) and CD18 or CDI 1b (10microg/ml). The secretion of gelatinase was examined by determination of enzyme activity and gelatin substrate zymography of cell supernatants. RESULTS: Ligation of selectin L, CD18 and CD11b integrin subunits by monoclonal antibodies induced a rapid release of 24.6+/-1.8% (p<0.005), 24.0+/-2.9% (p<0.001) and 22.7+/-2.0% (p < 0.005) of total neutrophil gelatinase, respectively as compared with 11.1+/-1.6% in the control. These values were equivalent to N-formyl-methionylleucyl-phenylalanine (fMLP)-stimulated secretion of gelatinase. Under these experimental conditions there was no significant beta-glucuronidase release from azurophilic granules. Gelatinase exocytosis elicited by selectin L and CD18 ligation was inhibited by 82.7+/-10.1% and 49.3+/-5.9%, respectively after preincubation of the neutrophils with 10 microM herbimycin A. CONCLUSIONS: Ligation of selectin L and integrin CD11b/ CD18 provides stimulatory signals to neutrophils which induce secretion of gelatinase B that may facilitate their transmigration into sites of inflammation.
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