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Blood, Vol. 94 No. 7 (October 1), 1999:
pp. 2487-2496
Presence of Proteinase 3 in Secretory Vesicles: Evidence of a Novel,
Highly Mobilizable Intracellular Pool Distinct From Azurophil Granules
Véronique Witko-Sarsat,
Elisabeth M. Cramer,
Corinne Hieblot,
Josette Guichard,
Patrick Nusbaum,
Sandra Lopez,
Philippe Lesavre, and
Lise Halbwachs-Mecarelli
From INSERM U507, Hôpital Necker, Paris, France; and INSERM
U474, Hôpital Henri Mondor, Créteil, France.
Proteinase 3 (PR3), which is also called myeloblastin, the target
autoantigen for antineutrophil cytoplasmic antibodies (ANCA) in
Wegener's granulomatosis, is a serine proteinase stored in azurophil
granules of human neutrophils. We have previously shown that, in
contrast to elastase or myeloperoxidase, PR3 is also expressed at the
plasma membrane of a subset of unactivated neutrophils and that a high
proportion of neutrophils expressing membrane PR3 is a risk factor for
vasculitis. The present study demonstrates that the association of PR3
with the plasma membrane is not an ionic interaction and seems to be
covalent. Fractionation of neutrophils shows that, besides the
azurophil granules, PR3 could be detected both in specific granules and
in the plasma membrane-enriched fraction containing secretory vesicles,
whereas elastase and myeloperoxidase were exclusively located in
azurophil granules. Electron microscopy confirms that PR3 is present
along with CR1 in secretory vesicles as well as in some specific
granules. In neutrophils stimulated with an increasing dose of FMLP,
membrane PR3 expression increased with the degranulation of secretory
vesicles, followed by specific granules, and culminated after azurophil
granules mobilization. The presence of a readily plasma
membrane-mobilizable pool of PR3 contained in the secretory vesicles
might play a relevant role in the pathophysiological mechanisms of
ANCA-associated vasculitis.
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