Title : CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions.

Pub. Date : 2017

PMID : 28539925






4 Functional Relationships(s)
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1 It was demonstrated that CXCL9(74-103) binds with high affinity to GAGs, competed with active chemokines for GAG binding and thereby inhibited CXCL8- and monosodium urate (MSU) crystal-induced neutrophil migration to joints. Glycosaminoglycans chemokine (C-X-C motif) ligand 9 Mus musculus
2 This could be explained by (1) the lower affinity of CXCL9(74-93) for CS, the most abundant GAG in joints, and (2) by reduced competition with GAG binding of CXCL1, the most abundant ELR+ CXC chemokine in this gout model. Glycosaminoglycans chemokine (C-X-C motif) ligand 9 Mus musculus
3 In summary, both CXCL9 peptides inhibited neutrophil migration in vivo through interference with GAG interactions in several animal models. Glycosaminoglycans chemokine (C-X-C motif) ligand 9 Mus musculus
4 Shortening CXCL9(74-103) from the COOH-terminus limited its GAG-binding spectrum. Glycosaminoglycans chemokine (C-X-C motif) ligand 9 Mus musculus