Title : Inhibitory affinity modulation of FcγRIIA ligand binding by glycosphingolipids by inside-out signaling.

Pub. Date : 2021 May 18

PMID : 34010642






3 Functional Relationships(s)
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1 beta-glucan reduces the effective 2D affinity of FcgammaRIIA for IgG via Lyn and SHP-1 and, in vivo, inhibits FcgammaRIIA-mediated neutrophil recruitment to intravascular IgG deposited in the kidney glomeruli in a glycosphingolipid- and Lyn-dependent manner. beta-Glucans LYN proto-oncogene, Src family tyrosine kinase Homo sapiens
2 beta-glucan reduces the effective 2D affinity of FcgammaRIIA for IgG via Lyn and SHP-1 and, in vivo, inhibits FcgammaRIIA-mediated neutrophil recruitment to intravascular IgG deposited in the kidney glomeruli in a glycosphingolipid- and Lyn-dependent manner. beta-Glucans LYN proto-oncogene, Src family tyrosine kinase Homo sapiens
3 In summary, we have identified a pathway for modulating the 2D affinity of FcgammaRIIA for ligand that relies on LacCer-Lyn-SHP-1-mediated inhibitory signaling triggered by beta-glucan, a previously described activator of innate immunity. beta-Glucans LYN proto-oncogene, Src family tyrosine kinase Homo sapiens