{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang JX"],"funding":["NIDDK NIH HHS","NCRR NIH HHS","NIAID NIH HHS","NHLBI NIH HHS","NIAMS NIH HHS"],"pagination":["1489-98"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3423786"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["120(7)"],"pubmed_abstract":["Ly6G is a glycosylphosphatidylinositol (GPI)-anchored protein of unknown function that is commonly targeted to induce experimental neutrophil depletion in mice. In the present study, we found that doses of anti-Ly6G Abs too low to produce sustained neutropenia remained capable of inhibiting experimental arthritis, leaving joint tissues free of infiltrating neutrophils. Thioglycollate-stimulated peritonitis was also attenuated. No alteration in neutrophil apoptosis was observed, implicating impaired recruitment. Indeed, Ly6G ligation abrogated neutrophil migration toward LTB(4) and other chemoattractants in a transwell system. Exploring the basis for this blockade, we identified colocalization of Ly6G and β2-integrins by confocal microscopy and confirmed close association by both coimmunoprecipitation and fluorescence lifetime imaging microscopy. Anti-Ly6G Ab impaired surface expression of β2-integrins in LTB(4)-stimulated neutrophils and mimicked CD11a blockade in inhibiting both ICAM-1 binding and firm adhesion to activated endothelium under flow conditions. Correspondingly, migration of β2-integrin-deficient neutrophils was no longer inhibited by anti-Ly6G. These results demonstrate that experimental targeting of Ly6G has functional effects on the neutrophil population and identify a previously unappreciated role for Ly6G as a modulator of neutrophil migration to sites of inflammation via a β2-integrin-dependent mechanism."],"journal":["Blood"],"pubmed_title":["Ly6G ligation blocks recruitment of neutrophils via a β2-integrin-dependent mechanism."],"pmcid":["PMC3423786"],"funding_grant_id":["R01 AI068871","3R01AI068871-04S","P30 AR042689","S10 RR027931","1R01HL097796","K01 DK089145","5R01-AI068871","P30 DK043351","R01 HL097796","1S10RR027931","P30 AR42689"],"pubmed_authors":["Huang YF","Soberman RJ","Shnayder R","Bair AM","Wang JX","Nigrovic PA","Shieh CC","Fuhlbrigge RC","King SL"],"additional_accession":[]},"is_claimable":false,"name":"Ly6G ligation blocks recruitment of neutrophils via a β2-integrin-dependent mechanism.","description":"Ly6G is a glycosylphosphatidylinositol (GPI)-anchored protein of unknown function that is commonly targeted to induce experimental neutrophil depletion in mice. In the present study, we found that doses of anti-Ly6G Abs too low to produce sustained neutropenia remained capable of inhibiting experimental arthritis, leaving joint tissues free of infiltrating neutrophils. Thioglycollate-stimulated peritonitis was also attenuated. No alteration in neutrophil apoptosis was observed, implicating impaired recruitment. Indeed, Ly6G ligation abrogated neutrophil migration toward LTB(4) and other chemoattractants in a transwell system. Exploring the basis for this blockade, we identified colocalization of Ly6G and β2-integrins by confocal microscopy and confirmed close association by both coimmunoprecipitation and fluorescence lifetime imaging microscopy. Anti-Ly6G Ab impaired surface expression of β2-integrins in LTB(4)-stimulated neutrophils and mimicked CD11a blockade in inhibiting both ICAM-1 binding and firm adhesion to activated endothelium under flow conditions. Correspondingly, migration of β2-integrin-deficient neutrophils was no longer inhibited by anti-Ly6G. These results demonstrate that experimental targeting of Ly6G has functional effects on the neutrophil population and identify a previously unappreciated role for Ly6G as a modulator of neutrophil migration to sites of inflammation via a β2-integrin-dependent mechanism.","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Aug","modification":"2026-06-04T08:17:40.057Z","creation":"2026-05-07T03:13:06.042Z"},"accession":"S-EPMC3423786","cross_references":{"pubmed":["22661700"],"doi":["10.1182/blood-2012-01-404046"]}}