caa a22 4500 465764002 CHVBK 20180323111908.0 cr unu---uuuuu 170327e19900201xx s 000 0 eng 10.1007/BF00914025 doi (NATIONALLICENCE)springer-10.1007/BF00914025 Modulation of human polymorphonuclear neutrophil functions by α1acid glycoprotein [Elektronische Daten] [E. Lainé, R. Couderc, M. Roch-Arveiller, M. Vasson, J. Giroud, D. Raichvarg] α1-Acid glycoprotein (α1-AGP), a naturally occurring human plasma protein and acute-phase reactant, was extracted by a two-step procedure from sera collected from four healthy men. Its activity was testedin vitro on human polymorphonuclear (PMN) functions (migration, aggregation, O 2 − generation). α1,-AGP was not chemoattractant but inhibited the PMN response to the chemoattractant formylmethionyl-leucyl-phenylalanine without affecting spontaneous migration (Boyden and agarose methods of assessment). At concentrations between 0.15 and 0.45 mg/ml, α1AGP exerted an aggregating effect with a maximal effective concentration of 0.3 mg/ml. α1-AGP inhibited superoxide generation by PMNs stimulated either by opsonized zymosan or phorbol myristate acetate. This inhibition varied according to the intensity of the stimulation. At low stimulus concentrations, a dose-dependent inhibition of membrane-associated PMN responsiveness to soluble or particulate stimuli was observed. These findings suggest that α1-AGP may be able to prevent PMN activation in the course of inflammatory processesin vivo. Plenum Publishing Corporation, 1990 Lainé E. Département de Pharmacologie, CNRS URA 595, France aut Couderc R. Département de Pharmacologie, CNRS URA 595, France aut Roch-Arveiller M. Département de Pharmacologie, CNRS URA 595, France aut Vasson M. Département de Biochimie, Faculté de Pharmacie, 28 place H. Dunand, F-63000, Clermont-Ferrand, France aut Giroud J. Département de Pharmacologie, CNRS URA 595, France aut Raichvarg D. Département de Biochimie A, Hôpital Cochin, 27 rue du Fbg St Jacques, F-75674, Paris Cedex 14, France aut Inflammation Kluwer Academic Publishers-Plenum Publishers 14/1(1990-02-01), 1-9 0360-3997 14:1<1 1990 14 10753 https://doi.org/10.1007/BF00914025 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00914025 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Lainé E. Département de Pharmacologie, CNRS URA 595, France aut NATIONALLICENCE 700 1- Couderc R. Département de Pharmacologie, CNRS URA 595, France aut NATIONALLICENCE 700 1- Roch-Arveiller M. Département de Pharmacologie, CNRS URA 595, France aut NATIONALLICENCE 700 1- Vasson M. Département de Biochimie, Faculté de Pharmacie, 28 place H. Dunand, F-63000, Clermont-Ferrand, France aut NATIONALLICENCE 700 1- Giroud J. Département de Pharmacologie, CNRS URA 595, France aut NATIONALLICENCE 700 1- Raichvarg D. Département de Biochimie A, Hôpital Cochin, 27 rue du Fbg St Jacques, F-75674, Paris Cedex 14, France aut NATIONALLICENCE 773 0- Inflammation Kluwer Academic Publishers-Plenum Publishers 14/1(1990-02-01), 1-9 0360-3997 14:1<1 1990 14 10753 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer