High impact information on CLEC6A

• Second, ligation of dectin-2 on RAW cells induced tyrosine phosphorylation of FcRgamma, activation of NF-kappaB, internalization of a surrogate ligand, and up-regulated secretion of tumor necrosis factor alpha and interleukin-1 receptor antagonist [1].
• The carbohydrate-recognition domain of Dectin-2 is a C-type lectin with specificity for high mannose [2].
• Glycan array analysis of the carbohydrate recognition by Dectin-2 indicated specific recognition of high-mannose structures (Man(9)GlcNAc(2)) [2].
• Our findings may form the basis for understanding the function of human DECTIN-2 in innate immunity [3].
• This process yielded a cDNA encoding a C-type lectin with 66.5% amino acid sequence homology to mouse dectin-2, the same gene reported by Kanazawa et al [3].

Anatomical context of CLEC6A

• To identify human DECTIN-2, we employed degenerative polymerase chain reaction-based cDNA cloning using RNA from human Langerhans cell (LC)-like dendritic cells (DCs) [3].
• Selective binding for hyphae was also observed using RAW macrophages expressing dectin-2, the ligation of which by hyphae or cross-linking with dectin-2-specific antibody led to protein tyrosine phosphorylation [1].

Associations of CLEC6A with chemical compounds

• The carbohydrate-recognition domain (CRD) of Dectin-2 exhibited cation-dependent mannose/fucose-like lectin activity, with an IC(50) for mannose of approximately 20 mM compared to an IC(50) of 1.5 mM for the macrophage mannose receptor when assayed by similar methodology [2].

Analytical, diagnostic and therapeutic context of CLEC6A

• Molecular cloning of human dectin-2 [4].

References