NB1 mediates surface expression of the ANCA antigen proteinase 3 on human neutrophils

Antineutrophil cytoplasmic antibodies (ANCAs) with specificity for proteinase 3 (PR3) are central to a form of ANCA-associated vasculitis. Membrane PR3 (mPR3) is expressed only on a subset of neutrophils. The aim of this study was to determine the mechanism of PR3 surface expression on human neutrop...

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Veröffentlicht in:Blood 2007-05, Vol.109 (10), p.4487-4493
Hauptverfasser: von Vietinghoff, Sibylle, Tunnemann, Gisela, Eulenberg, Claudia, Wellner, Maren, Cristina Cardoso, M., Luft, Friedrich C., Kettritz, Ralph
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container_end_page 4493
container_issue 10
container_start_page 4487
container_title Blood
container_volume 109
creator von Vietinghoff, Sibylle
Tunnemann, Gisela
Eulenberg, Claudia
Wellner, Maren
Cristina Cardoso, M.
Luft, Friedrich C.
Kettritz, Ralph
description Antineutrophil cytoplasmic antibodies (ANCAs) with specificity for proteinase 3 (PR3) are central to a form of ANCA-associated vasculitis. Membrane PR3 (mPR3) is expressed only on a subset of neutrophils. The aim of this study was to determine the mechanism of PR3 surface expression on human neutrophils. Neutrophils were isolated from patients and healthy controls, and hematopoietic stem cells from cord blood served as a model of neutrophil differentiation. Surface expression was analyzed by flow cytometry and confocal microscopy, and proteins were analyzed by Western blot experiments. Neutrophil subsets were separated by magnetic cell sorting. Transfection experiments were carried out in HEK293 and HL60 cell lines. Using neutrophils from healthy donors, patients with vasculitis, and neutrophilic differentiated stem cells we found that mPR3 display was restricted to cells expressing neutrophil glycoprotein NB1, a glycosylphosphatidylinositol (GPI)–linked surface receptor. mPR3 expression was decreased by enzymatic removal of GPI anchors from cell membranes and was absent in a patient with paroxysmal nocturnal hemoglobinuria. PR3 and NB1 coimmunoprecipitated from and colocalized on the neutrophil plasma membrane. Transfection with NB1 resulted in specific PR3 surface binding in different cell types. We conclude that PR3 membrane expression on neutrophils is mediated by the NB1 receptor.
doi_str_mv 10.1182/blood-2006-10-055327
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Membrane PR3 (mPR3) is expressed only on a subset of neutrophils. The aim of this study was to determine the mechanism of PR3 surface expression on human neutrophils. Neutrophils were isolated from patients and healthy controls, and hematopoietic stem cells from cord blood served as a model of neutrophil differentiation. Surface expression was analyzed by flow cytometry and confocal microscopy, and proteins were analyzed by Western blot experiments. Neutrophil subsets were separated by magnetic cell sorting. Transfection experiments were carried out in HEK293 and HL60 cell lines. 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source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection
subjects Antibodies, Antineutrophil Cytoplasmic - immunology
Antigens, Surface - metabolism
Biological and medical sciences
Cell Membrane - metabolism
Cells, Cultured
Fetal Blood - cytology
Glycosylphosphatidylinositols - metabolism
GPI-Linked Proteins
Hematologic and hematopoietic diseases
Hematopoietic Stem Cells - metabolism
Humans
Immunoprecipitation
In Vitro Techniques
Isoantigens - physiology
Medical sciences
Membrane Glycoproteins - physiology
Myeloblastin - immunology
Myeloblastin - metabolism
Neutrophils - enzymology
Neutrophils - metabolism
Receptors, Cell Surface - physiology
Transfection
title NB1 mediates surface expression of the ANCA antigen proteinase 3 on human neutrophils
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