Abstract
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.
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Lainé, E., Couderc, R., Roch-Arveiller, M. et al. Modulation of human polymorphonuclear neutrophil functions by α1acid glycoprotein. Inflammation 14, 1–9 (1990). https://doi.org/10.1007/BF00914025
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DOI: https://doi.org/10.1007/BF00914025