The presence of membrane Proteinase 3 in neutrophil lipid rafts and its colocalization with FcγRIIIb and cytochrome b558

David, Alina; Fridlich, Ram; Aviram, Irit

doi:10.1016/j.yexcr.2005.03.034

Cited by 53 publications

(53 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Such observations are consistent with recent findings that translocation of JNK toward lipid raft microdomains occurred when U937 cell was treated with UV-C. 35 In addition, redistribution of MAP kinases, including extracellular signal-regulated kinase and p38, to lipid raft structures in stimulated neutrophils has also been reported, 38 suggesting that membrane lipid rafts may play a role in action of the MAPK family, depending on the study context, such as cell type and the nature of the stimulus. Apoptosis and non-apoptotic cell death/necrosis are two distinct forms of cell death and both are closely implicated in the pathological processes of human diseases.…”

Section: Discussionsupporting

confidence: 90%

Signaling pathways from membrane lipid rafts to JNK1 activation in reactive nitrogen species-induced non-apoptotic cell death

Zhang

et al. 2007

Cell Death Differ

View full text Add to dashboard Cite

At present, the signaling pathways controlling reactive nitrogen species (RNS)-induced non-apoptotic cell death are relatively less understood. In this work, various RNS donors are found to induce caspase-independent non-apoptotic cell death in mouse embryonic fibroblasts (MEF). In search of the molecular mechanisms, we first established the role of c-Jun N-terminal kinase (JNK) in RNS-induced non-apoptotic cell death. RNS readily activate JNK, and the jnk1À/À MEF are resistant to RNS-induced cell death. Moreover, the reconstitution of JNK1 effectively restores the sensitivity to RNS. Next, we identified tumor necrosis factor receptor-associated factor 2 (TRAF2) and apoptosis signal-regulating kinase 1 (ASK1) as the essential upstream molecules for RNS-induced JNK activation and cell death. RNS fail to activate JNK and induce cell death in traf2À/À MEF; and reconstitution of TRAF2 effectively restores the responsiveness of traf2À/À MEF to RNS. Moreover, RNS-induced ASK1 activation is impaired in traf2À/À cells and overexpression of a mutant ASK1 protein suppresses RNS-induced cell death in wild-type MEF cells. Last, we explored the signaling events upstream of TRAF2 and found that translocation of TRAF2 and JNK1 onto membrane lipid rafts is required for RNS-mediated JNK1 activation and cell death. Taken together, data from our study reveal a novel signaling pathway regulating RNS-induced JNK1 activation and non-apoptotic cell death.

show abstract

Section: Discussionsupporting

confidence: 90%

Signaling pathways from membrane lipid rafts to JNK1 activation in reactive nitrogen species-induced non-apoptotic cell death

Zhang

et al. 2007

Cell Death Differ

View full text Add to dashboard Cite

show abstract

“…studies, however, suggest that PR3 has a greater role than NE in IL-1β processing and secretion. (3) PR3 is localized in the same lipid raft domains (75,76) as A1AT (5,20) and LA (77). Bilayer-bound PR3 has a reduced catalytic efficiency, whereas its inhibition by A1AT is more important than that observed for the soluble form of the enzyme.…”

Section: Resultsmentioning

confidence: 99%

α-Linoleic Acid Enhances the Capacity of α1-Antitrypsin to Inhibit Lipopolysaccharide-Induced IL-1β in Human Blood Neutrophils

Aggarwal

Korenbaum

Mahadeva

et al. 2016

Mol Med

View full text Add to dashboard Cite

“…Colocalization of mPR3 with other membrane proteins, such as ␤ 2 integrin and Fc␥ receptor (Fc␥R) type IIIb, has been reported previously (12,13). In recent studies, CD177/NB1 has been proposed as the mPR3 receptor on the neutrophil surface (14,15).…”

mentioning

confidence: 89%

“…These results suggest that CD177 is not an exclusive receptor of mPR3, and the binding sites for CD177-independent mPR3 expression are still open for discussion. It has been shown that mPR3 colocalizes with activated ␤ 2 integrin and Fc␥R in the neutrophil membrane (12,13,48). PR3 can insert into the membrane lipid bilayer via the hydrophobic region (49).…”

mentioning

confidence: 99%

Coexpression of CD177 and membrane proteinase 3 on neutrophils in antineutrophil cytoplasmic autoantibody–associated systemic vasculitis: Anti–proteinase 3–mediated neutrophil activation is independent of the role of CD177‐expressing neutrophils

Hu¹,

Westra²,

Huitema³

et al. 2009

Arthritis & Rheumatism

View full text Add to dashboard Cite

Objective. Wegener's granulomatosis (WG) is strongly associated with antineutrophil cytoplasmic autoantibodies (ANCAs) directed against proteinase 3 (PR3). Recent studies have shown that membranebound PR3 (mPR3) is differentially expressed and colocalizes with CD177/NB1 on circulating neutrophils. We undertook this study to assess the differential expression of CD177 on neutrophils from patients with ANCA-associated systemic vasculitis (ASV) in comparison with patients with systemic lupus erythematosus (SLE), patients with rheumatoid arthritis (RA), and healthy individuals, and to investigate whether colocalization of mPR3 and CD177 affects anti-PR3-mediated neutrophil activation.Methods. Expression of CD177 and mPR3 was analyzed by flow cytometry on isolated neutrophils from patients with ASV (n ‫؍‬ 53), those with SLE (n ‫؍‬ 30), those with RA (n ‫؍‬ 26), and healthy controls (n ‫؍‬ 31). Neutrophil activation mediated by anti-PR3 antibodies was assessed by measuring the oxidative burst with a dihydrorhodamine assay.Results. Percentages of CD177-expressing neutrophils were significantly higher in patients with ASV and those with SLE than in healthy controls. In 3 healthy donors, CD177 expression was not detected. After priming with tumor necrosis factor ␣, neutrophils remained negative for CD177 while mPR3 expression was induced. Neutrophils from CD177-negative donors or CD177؊ neutrophils sorted from donors with bimodal expression were susceptible to anti-PR3-mediated oxidative burst. Variation in the extent of anti-PR3-mediated neutrophil activation among different donors occurred independent of the percentage of CD177-expressing neutrophils.Conclusion. Membrane expression of CD177 on circulating neutrophils is increased in patients with ASV and in those with SLE, but not in RA patients. However, primed neutrophils from CD177-negative individuals also express mPR3 and are susceptible to anti-PR3-mediated oxidative burst, suggesting that recruitment of CD177-independent mPR3 is involved in anti-PR3-induced neutrophil activation.

show abstract

The presence of membrane Proteinase 3 in neutrophil lipid rafts and its colocalization with FcγRIIIb and cytochrome b558

Cited by 53 publications

References 54 publications

Signaling pathways from membrane lipid rafts to JNK1 activation in reactive nitrogen species-induced non-apoptotic cell death

Signaling pathways from membrane lipid rafts to JNK1 activation in reactive nitrogen species-induced non-apoptotic cell death

α-Linoleic Acid Enhances the Capacity of α1-Antitrypsin to Inhibit Lipopolysaccharide-Induced IL-1β in Human Blood Neutrophils

Coexpression of CD177 and membrane proteinase 3 on neutrophils in antineutrophil cytoplasmic autoantibody–associated systemic vasculitis: Anti–proteinase 3–mediated neutrophil activation is independent of the role of CD177‐expressing neutrophils

Contact Info

Product

Resources

About