Abstract:
:CD177 is a glycosylphosphatidylinositol (GPI)-anchored protein expressed by a variable proportion of human neutrophils that mediates surface expression of the antineutrophil cytoplasmic antibody antigen proteinase 3. CD177 associates with β2 integrins and recognizes platelet endothelial cell adhesion molecule 1 (PECAM-1), suggesting a role in neutrophil migration. However, CD177pos neutrophils exhibit no clear migratory advantage in vivo, despite interruption of in vitro transendothelial migration by CD177 ligation. We sought to understand this paradox. Using a PECAM-1-independent transwell system, we found that CD177pos and CD177neg neutrophils migrated comparably. CD177 ligation selectively impaired migration of CD177pos neutrophils, an effect mediated through immobilization and cellular spreading on the transwell membrane. Correspondingly, CD177 ligation enhanced its interaction with β2 integrins, as revealed by fluorescence lifetime imaging microscopy, leading to integrin-mediated phosphorylation of Src and extracellular signal-regulated kinase (ERK). CD177-driven cell activation enhanced surface β2 integrin expression and affinity, impaired internalization of integrin attachments, and resulted in ERK-mediated attenuation of chemokine signaling. We conclude that CD177 signals in a β2 integrin-dependent manner to orchestrate a set of activation-mediated mechanisms that impair human neutrophil migration.
journal_name
Bloodjournal_title
Bloodauthors
Bai M,Grieshaber-Bouyer R,Wang J,Schmider AB,Wilson ZS,Zeng L,Halyabar O,Godin MD,Nguyen HN,Levescot A,Cunin P,Lefort CT,Soberman RJ,Nigrovic PAdoi
10.1182/blood-2017-03-768507subject
Has Abstractpub_date
2017-11-09 00:00:00pages
2092-2100issue
19eissn
0006-4971issn
1528-0020pii
blood-2017-03-768507journal_volume
130pub_type
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