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Lower serum ficolin-3 levels were correlated with injury severity following traumatic brain injury.
this study provide novel insight in the binding and complement activating capacity of the lectin pathway initiation molecules ficolin-2 (show FCN2 Proteins) and ficolin-3 towards relevant Gram-negative pathogens of pathophysiological relevance.
Data indicate differences in the plasma concentrations of collectin liver 1 (show COLEC10 Proteins) and collectin (show MBL2 Proteins) kidney 1 (show ZNF354A Proteins), M-ficolin (show FCN1 Proteins) and H-ficol in systemic lupus erythematosus (SLE) patients compared to a group of healthy controls.
H-ficolin participates in A. fumigatus defence through the activation of the lectin complement pathway, enhanced fungus-host interactions and modulated immune responses.
data suggest that high levels of the complement activating molecule H-ficolin are associated with an increased risk of future progression to microalbuminuria in patients with newly diagnosed type 1 diabetes.
High ficolin-3 level at the time of transplantation was an independent significant risk factor for shorter graft survival.
There is lack of association of serum mannose-binding lectin (show MBL2 Proteins) or ficolins with complement activation in patients with antiphospholipid antibodies.
This study aims to investigate whether an association exists between the ficolins that are part of the lectin complement pathway and systemic lupus erythematosus.
Both ficolin-3 and MASP-2 (show MASP2 Proteins) levels correlated inversely with the time from the onset of the attack of hereditary angioedema until blood sampling
Data show that the plasmid pETb-ficolin 3 was cloned successfully and the purity of the protein His-ficolin 3 was over 90%.
Ficolins are a group of proteins which consist of a collagen-like domain and a fibrinogen-like domain. In human serum, there are two types of ficolins, both of which have lectin activity. The protein encoded by this gene is a thermolabile beta-2-macroglycoprotein found in all human serum and is a member of the ficolin/opsonin p35 lectin family. The protein, which was initially identified based on its reactivity with sera from patients with systemic lupus erythematosus, has been shown to have a calcium-independent lectin activity. The protein can activate the complement pathway in association with MASPs and sMAP, thereby aiding in host defense through the activation of the lectin pathway. Alternative splicing occurs at this locus and two variants, each encoding a distinct isoform, have been identified.
, collagen/fibrinogen domain-containing lectin 3 p35
, collagen/fibrinogen domain-containing protein 3
, ficolin 3