High impact information on Complement Pathway, Mannose-Binding Lectin

• Similar to mannose-binding lectin, L-ficolin and H-ficolin are the recognition molecules in the lectin complement pathway [1].
• Human M-ficolin is a secretory protein that activates the lectin complement pathway [1].
• These results indicate that M-ficolin, like its family members, functions as a recognition molecule of the lectin complement pathway and plays an important role in innate immunity [1].
• We have examined a role of the major soluble inhibitor of the classic and lectin complement pathways, C4b-binding protein (C4BP), in the clearance of apoptotic cells [2].
• Activation of the lectin complement pathway by H-ficolin (Hakata antigen) [3].

Biological context of Complement Pathway, Mannose-Binding Lectin

• Endothelial oxidative stress activates the lectin complement pathway: role of cytokeratin 1 [4].

Anatomical context of Complement Pathway, Mannose-Binding Lectin

• We have previously demonstrated that the lectin complement pathway (LCP), which is initiated by deposition of the mannose-binding lectin (MBL), is largely responsible for activating complement on endothelial cells following periods of oxidative stress [5].

Associations of Complement Pathway, Mannose-Binding Lectin with chemical compounds

• It recognizes specific carbohydrate residues (mannose and N-acetylglucosamine) on the surface of microorganisms and promotes the killing of microbes either by acting directly as an opsonin or by activating the lectin complement pathway [6].
• Mannan-binding lectin-associated serine protease-2 (MASP-2) is a serine protease involved in the activation of lectin complement pathway [7].

Gene context of Complement Pathway, Mannose-Binding Lectin

• Mannose-binding lectin (MBL) is a C-type lectin involved in the first line of host defense and it requires MBL-associated serine proteases (MASP) for activation of the lectin complement pathway (LCP) [8].
• The 5'-flanking regions of the genes encoding human mannose-binding lectin-associated serine protease (MASP)-1/3 and MASP-2, key enzymes in the lectin complement pathway, were isolated and characterized [9].
• Oxidative stress increases endothelial mannose-binding lectin (MBL) binding and activates the lectin complement pathway (LCP) [4].
• RT-PCR analysis showed that the expression pattern of ficolin A expression was closely similar to that of Masps, suggesting that these molecules may function in coordination as components of the lectin complement pathway [10].
• Two of three human ficolins, L-ficolin and H-ficolin, are serum lectins that form complexes with mannose-binding lectin-associated serine proteases (MASPs) and play important roles in the lectin complement pathway [10].

References