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Ficolin-3 plasma levels are associated with the presence and progression of abdominal aortic aneurysm (AAA (zeige APP Proteine)), suggesting its potential role as a biomarker of AAA (zeige APP Proteine)
results suggest that anti-ficolin-3 antibodies could be useful for the diagnosis of active nephritis in SLE patients
this study shows that H-ficolin may aid clearance of influenza A virus by promoting monocyte uptake of the virus, while reducing viral replication and virus-induced TNF-a (zeige TNF Proteine) responses in these cells
These results suggest that polymorphisms in the FCN3 gene cooperate to increase ficolin-3 concentration and that it might contribute to leprosy susceptibility by favoring Mycobacterium leprae infection.
subjects that were heterozygote carriers of both FCN2 (zeige FCN2 Proteine) + 6424 and FCN3 + 1637delC were sufficient mannan-binding lectin (zeige MBL2 Proteine) producers
in patients with systemic lupus erythematosus, there was no significant association between ficolin-1 (zeige FCN1 Proteine) and ficolin-3 with lupus nephritis
Monitoring serum H-ficolin levels was shown to be of no benefit in terms of predicting severe infection.
Serum levels of ficolin-2 (zeige FCN2 Proteine) and ficolin-3 were significantly lower in the cardiac syndrome X patients compared to controls.
LPS induces a tissue-specific recruitment of ficolin-3 and ficolin-1 in the lung and systemic compartment, respectively, suggesting an important role of distinct lectin complement pathway initiators in the local pulmonary and systemic host defence.
Lower serum ficolin-3 levels were correlated with injury severity following traumatic brain injury.
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