, Volume 14, Issue 1, pp 1–9 | Cite as

Modulation of human polymorphonuclear neutrophil functions by α1acid glycoprotein

  • E. Lainé
  • R. Couderc
  • M. Roch-Arveiller
  • M. P. Vasson
  • J. P. Giroud
  • D. Raichvarg
Original Articles


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.


Myristate Myristate Acetate Phorbol Myristate Acetate Polymorphonuclear Neutrophil Human Plasma Protein 


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Copyright information

© Plenum Publishing Corporation 1990

Authors and Affiliations

  • E. Lainé
    • 1
    • 2
  • R. Couderc
    • 1
    • 2
  • M. Roch-Arveiller
    • 1
  • M. P. Vasson
    • 3
  • J. P. Giroud
    • 1
  • D. Raichvarg
    • 2
    • 3
  1. 1.Département de PharmacologieCNRS URA 595France
  2. 2.Département de Biochimie AHôpital CochinParis Cedex 14France
  3. 3.Département de Biochimie, Faculté de PharmacieClermont-FerrandFrance

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