scholarly journals Antineutrophil cytoplasmic antibodies induce monocyte IL-8 release. Role of surface proteinase-3, alpha1-antitrypsin, and Fcgamma receptors.

1997 ◽  
Vol 100 (6) ◽  
pp. 1416-1424 ◽  
Author(s):  
D R Ralston ◽  
C B Marsh ◽  
M P Lowe ◽  
M D Wewers
2018 ◽  
Vol 33 (9) ◽  
pp. 1603-1607 ◽  
Author(s):  
Hidetoshi Takedatsu ◽  
Keiichi Mitsuyama ◽  
Shuhei Fukunaga ◽  
Shinichiro Yoshioka ◽  
Ryosuke Yamauchi ◽  
...  

Gut and Liver ◽  
2022 ◽  
Vol 16 (1) ◽  
pp. 92-100
Author(s):  
So Imakiire ◽  
Hidetoshi Takedatsu ◽  
Keiichi Mitsuyama ◽  
Hideto Sakisaka ◽  
Kozo Tsuruta ◽  
...  

2020 ◽  
Vol 27 (17) ◽  
pp. 2852-2862
Author(s):  
Esther N. Pijnappel ◽  
Ger T. Rijkers ◽  
Frans J. van Overveld

Diagnosis of vasculitis is based on the presence of histologic features and serological testing for antineutrophil cytoplasmic antibodies (ANCA). In patients with vasculitis, two types of ANCA have been identified: ANCA directed against the neutrophil serine protease proteinase-3 (PR3) which results in a cytoplasmic immunofluorescence pattern (c-ANCA) and ANCA directed against the neutrophil enzyme myeloperoxidase (MPO), which results in a perinuclear immunofluorescence pattern (p-ANCA). Question is if the presence of ANCA is the consequence of abnormal neutrophil adhesion, activation, and apoptosis. Or is it, through mechanisms which are not totally clear for the moment, the cause of vasculitis. In the latter case it has to be postulated that ANCA autoantigens are expressed on the cell surface of viable, or activated, or early-apoptotic neutrophils.


2020 ◽  
Vol 11 ◽  
Author(s):  
Gwen E. Thompson ◽  
Lynn A. Fussner ◽  
Amber M. Hummel ◽  
Darrell R. Schroeder ◽  
Francisco Silva ◽  
...  

Rheumatology ◽  
2019 ◽  
Vol 58 (Supplement_2) ◽  
Author(s):  
Gwen Thompson ◽  
Lynn Fussner ◽  
Amber Hummel ◽  
Darrell Schroeder ◽  
Francisco Silva ◽  
...  

Pathology ◽  
1999 ◽  
Vol 31 (1) ◽  
pp. 38-43 ◽  
Author(s):  
W. Pollock ◽  
K. Dunster ◽  
J.M. Rolland ◽  
H. Koh ◽  
J. Savige

1996 ◽  
Vol 132 (6) ◽  
pp. 1037-1052 ◽  
Author(s):  
T Fukushima ◽  
T K Waddell ◽  
S Grinstein ◽  
G G Goss ◽  
J Orlowski ◽  
...  

In neutrophils, binding and phagocytosis facilitate subsequent intracellular killing of microorganisms. Activity of Na+/H+ exchangers (NHEs) participates in these events, especially in regulation of intracellular pH (pHi) by compensating for the H+ load generated by the respiratory burst. Despite the importance of these functions, comparatively little is known regarding the nature and regulation of NHE(s) in neutrophils. The purpose of this study was to identify which NHE(s) are expressed in neutrophils and to elucidate the mechanisms regulating their activity during phagocytosis. Exposure of cells to the phagocytic stimulus opsonized zymosan (OpZ) induced a transient cytosolic acidification followed by a prolonged alkalinization. The latter was inhibited in Na+-free medium and by amiloride analogues and therefore was due to activation of Na+/H+ exchange. Reverse transcriptase PCR and cDNA sequencing demonstrated that mRNA for the NHE-1 but not for NHE-2, 3, or 4 isoforms of the exchanger was expressed. Immunoblotting of purified plasma membranes with isoform-specific antibodies confirmed the presence of NHE-1 protein in neutrophils. Since phagocytosis involves Fcgamma (FcgammaR) and complement receptors such as CR3 (a beta2 integrin) which are linked to pathways involving alterations in intracellular [Ca2+]i and tyrosine phosphorylation, we studied these pathways in relation to activation of NHE-1. Cross-linking of surface bound antibodies (mAb) directed against FcgammaRs (FcgammaRII > FcgammaRIII) but not beta2 integrins induced an amiloride-sensitive cytosolic alkalinization. However, anti-beta2 integrin mAb diminished OpZ-induced alkalinization suggesting that NHE-1 activation involved cooperation between integrins and FcgammaRs. The tyrosine kinase inhibitors genistein and herbimycin blocked cytosolic alkalinization after OpZ or FcgammaR cross-linking suggesting that tyrosine phosphorylation was involved in NHE-I activation. An increase in [Ca2+]i was not required for NHE-1 activation because neither removal of extracellular Ca2+ nor buffering of changes in [Ca2+]i inhibited alkalinization after OpZ or Fc-gammaR cross-linking. In summary, Fc-gammaRs and beta2 integrins cooperate in activation of NHE-1 in neutrophils during phagocytosis by a signaling pathway involving tyrosine phosphorylation.


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