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Blood, Vol. 110, Issue 12, 4086-4095, December 1, 2007
Proteinase 3, the Wegener autoantigen, is externalized during neutrophil apoptosis: evidence for a functional association with phospholipid scramblase 1 and interference with macrophage phagocytosis
Blood Kantari et al.
110: 4086
Supplemental materials for: Kantari et al
Files in this Data Supplement:
- Document 1. Supplemental methods (PDF, 11.7 KB)
- Figure S1. Comparison between RBL/PR3 and neutrophils human macrophage phagocytosis (PDF, 49.6 KB) -
(A) Confocal fluorescence-microscopy analysis of human macrophages phagocytosis of apoptotic RBL-2H3 (left) and human neutrophils (right). TAMRA-labeled apoptotic cells (red) were incubated with FITC-conjugated anti-CD14-labeled macrophages derived from human monocytes (green). Phagocytosis yielded a red-labeled apoptotic cell engulfed by a green-labeled macrophage. (B) Apoptosis-induced PR3 membrane expression in RBL/PR3 and neutrophils. Apoptosis was induced by etoposide in RBL/PR3 and by overnight incubation at 37°C (so called “physiologic apoptosis”) in neutrophils. This representative experiment shows PR3 membrane expression on RBL/PR3 and neutrophils measured by flow cytometry. (C) Quantification of annexin-V positive cells after apoptosis. Both apoptotic RBL/PR3 and apoptotic neutrophils showed significantly enhanced PS externalization ( P < .01, ANOVA) as compared to the basal state. However, there was no significant difference in PS externalization between RBL/PR3 and neutrophils. (D) Quantification of phagocytosis as in Fig. 7D. Phagocytosis rates of apoptotic RBL/PR3 or neutrophils were comparable. Data are mean ± SEM from 6 independent experiments.
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