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• W2097863902 startingPage "1284" @default.
• W2097863902 abstract "Abstract The adhesion of neutrophils to endothelial cells is a central event leading to diapedesis and involves the binding of the I-domain of β2 integrins (CD11/CD18) to endothelial ICAMs. In addition to the I-domain, the β2 integrin complement receptor 3 (CR3) (CD11b/CD18) contains a lectin-like domain (LLD) that can alter leukocyte functions such as chemotaxis and cytotoxicity. The present study demonstrates that, in contrast to the CR3 I-domain, Ab blockade of the CR3 LLD has no role in mediating neutrophil-induced loss of endothelial barrier function. However, activation of CR3 with the LLD agonist β-glucan protects the barrier function of endothelial cells in the presence of activated neutrophils and reduces transendothelial migration without affecting adhesion of the neutrophils to the endothelium. The LLD site-specific mAb VIM12 obviates β-glucan protection while activation of the LLD by VIM12 cross-linking mimics the β-glucan response by both preserving endothelial barrier function and reducing neutrophil transendothelial migration. β-glucan has no direct effect on endothelial cell function in the absence of activated neutrophils. These findings demonstrate that signaling through the CR3 LLD prevents neutrophil-induced loss of endothelial barrier function and reduces diapedesis. This suggests that the LLD may be a suitable target for oligosaccharide-based anti-inflammatory therapeutics." @default.
• W2097863902 created "2016-06-24" @default.
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• W2097863902 date "2004-07-15" @default.
• W2097863902 modified "2023-09-27" @default.
• W2097863902 title "The Lectin-Like Domain of Complement Receptor 3 Protects Endothelial Barrier Function from Activated Neutrophils" @default.
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• W2097863902 doi "https://doi.org/10.4049/jimmunol.173.2.1284" @default.
• W2097863902 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15240721" @default.
• W2097863902 hasPublicationYear "2004" @default.
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