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doi:10.1016/0014-5793(95)01073-N 
Copyright © 1995 Published by Elsevier Science B.V.
Research letter
Bimodal distribution of proteinase 3 (PR3) surface expression reflects a constitutive heterogeneity in the polymorphonuclear neutrophil pool
L. Halbwachs-Mecarellia, 
, G. Bessoua, P. Lesavrea, S. Lopeza and V. Witko-Sarsatb
a INSERM U90, Hôpital Necker, 161 rue de Sèvres, 75015, Paris, France
b INSERM U25, Hôpital Necker, 161 rue de Sèvres, 75015, Paris, France
Received 7 September 1995.
Abstract
Proteinase 3, which is known as an intracellular serine protease of neutrophils, was detected at the surface of a subpopulation of freshly isolated PMN. The proportion of PR3-positive and -negative PMN, observed by flow cytometry with anti-PR3 mAbs or ANCA autoantibodies, varies among individuals but is extremely stable for each individual over prolonged time periods. After PMN degranulation by FMLP with cyt. B, membrane PR3 expression increases but the proportion of low and high PR3-expressing cells remains stable. The existence of a subset of PMN which spontaneously expresses PR3 and varies among individuals, may be relevant to the pathogenesis of anti-PR3 ANCA autoantibody-related vasculitis.
Author Keywords: Proteinase 3; Polymorphonuclear neutrophil; PMN serine protease; ANCA; Vasculitis
Abbreviations: PR3, proteinase 3; PMN, polymorphonuclear neutrophils; ANCA, antineutrophil cytoplasmic autoantibodies; WG, Wegener's granulomatosis; HBSS, Hanks' balanced salt solution; cyt. B, cytochalasin B; fMLP, N-formyl-methionyl-leucyl-phenylalanine
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