caa a22 4500 465764126 CHVBK 20180323111908.0 cr unu---uuuuu 170327e19900601xx s 000 0 eng 10.1007/BF00915809 doi (NATIONALLICENCE)springer-10.1007/BF00915809 Neutrophil chemotactic activity is modulated by human cystatin C, an inhibitor of cysteine proteases [Elektronische Daten] [J. Leung-Tack, C. Tavera, J. Martinez, A. Colle] Cystatin C, a cysteine proteinase inhibitor has recently been suggested to be a potent regulator of inflammatory processes and may act in defense against viral and bacterial infections. Two common forms of the protein were purified from the urine of a patient having received a renal transplant. The slow form of cystatin C possessed theN-terminal tetrapeptide Lys Pro Pro Arg, which was cleaved in the fast form. This peptide sequence, called postin, was synthesized. The three molecules, slow and fast forms of cystatin and the synthetic peptide, were tested for their effects on the migration activity of human polymorphonuclear neutrophils (PMNs). The slow form was found to display both chemotactic and chemokinetic activities, while the fast form and postin were only chemokinetic. Nevertheless, all the substances could induce a "motile” morphology. In addition, the two forms of cystatin C were powerful inhibitors of PMN chemotaxis induced by complement-derived chemotactic factors. This suggests that cystatin C in its two different cleaved forms and theN-terminal tetrapeptide can modulate PMN locomotion. Cysteine proteases may therefore play a role in neutrophil migration activity. Plenum Publishing Corporation, 1990 Leung-Tack J. Faculté de Médecine, INSERM U 133, 133 route de Narbonne, 31062, Toulouse, France aut Tavera C. Faculté de Médecine, INSERM U 133, 133 route de Narbonne, 31062, Toulouse, France aut Martinez J. Centre CNRS-INSERM de Pharmacologie-Endocrinologie, INSERM U264, rue de la Cardonille, B. P. 5055, 34094, Montpellier Cedex, France aut Colle A. Faculté de Médecine, INSERM U 133, 133 route de Narbonne, 31062, Toulouse, France aut Inflammation Kluwer Academic Publishers-Plenum Publishers 14/3(1990-06-01), 247-258 0360-3997 14:3<247 1990 14 10753 https://doi.org/10.1007/BF00915809 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00915809 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Leung-Tack J. Faculté de Médecine, INSERM U 133, 133 route de Narbonne, 31062, Toulouse, France aut NATIONALLICENCE 700 1- Tavera C. Faculté de Médecine, INSERM U 133, 133 route de Narbonne, 31062, Toulouse, France aut NATIONALLICENCE 700 1- Martinez J. Centre CNRS-INSERM de Pharmacologie-Endocrinologie, INSERM U264, rue de la Cardonille, B. P. 5055, 34094, Montpellier Cedex, France aut NATIONALLICENCE 700 1- Colle A. Faculté de Médecine, INSERM U 133, 133 route de Narbonne, 31062, Toulouse, France aut NATIONALLICENCE 773 0- Inflammation Kluwer Academic Publishers-Plenum Publishers 14/3(1990-06-01), 247-258 0360-3997 14:3<247 1990 14 10753 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer