Ficolin-1

Background

Ficolins, a component of the complement lectin pathway, are classified as collectins (C-type lectins) and bind carbohydrate present on the surface of microorganisms. There are three ficolins in humans including ficolin-1 (FCN1), ficolin-2, and ficolin-3. FCN1 is synthesized in monocytes and type II alveolar epithelial cells. It is present in secretory granules of human neutrophils, but it is not known which subset of the neutrophils' secretory granules harbors FCN1. Besides, FCN1 functions locally in inflamed lesions following secretion from monocytes, macrophages, and granulocytes.

Previous researches showed that FCN1 is also present in the serum, indicating that it may play a role in systemic immunity. Furthermore, a majority of FCN1 released in response to an inflammatory stimulus such as N-formylmethionine-leucyl-phenylalanine (fMLP) binds to the outer membrane. FCN1 is produced on the cell surface by its fibrinogen-like domain and accepts sialic acid as a ligand. It has demonstrated that the survival rate following infection with Streptococcus pneumoniae is notably lower in Fcnb-deficient mice than in wild-type mice. In a recent study, scientists reported that Fcnb-knockout mice are resistant to collagen antibody-induced arthritis (CAIA) and that the complement system is engaged in the mechanism. In general, these studies suggest that Fcnb plays a crucial role in host defense against bacterial infection, as well as in onset or exacerbation of autoimmune arthritis.

Fig. 1 Structure of M-ficolin.^{1, 3}

Ficolin-1 Functional Service

Creative Biolabs offers a comprehensive suite of ficolin-1-focused products, such as anti-Ficolin-1 antibodies, ELISA kits, and human complement Ficolin-1 proteins. These carefully crafted tools play a crucial role in advancing research endeavors aimed at developing therapeutic strategies for various diseases.

Fig.2 ELISA-based quantification of serum concentrations for ficolin-1, ficolin-2, ficolin-3, and mannose-binding lectin in both patient and control groups.^{2, 3}

Researchers analyzed the clinical links between ficolins and mannose-binding lectin (MBL) in acute myeloid leukemia (AML) patients. Serum levels of FCN1, FCN2, FCN3, and MBL2, along with gene polymorphisms, were evaluated before chemotherapy. Compared to healthy controls, AML patients exhibited lower median ficolin-1 levels and elevated ficolin-2, ficolin-3, and MBL levels. Notably, high MBL predicted severe infections, while low ficolin-1 correlated with prolonged fever. G/G homozygosity in the FCN1 gene was linked to malignancy, suggesting ficolins as potential AML biomarkers, distinguishing them from other hematologic malignancies.

Creative Biolabs offers a comprehensive suite of ficolin-1-associated services, encompassing binding analyses and additional functional studies, carefully customized to assist their esteemed clients in clinical and research aims.

References

1. Ammitzbøll, Christian Gytz, et al. "Non-synonymous polymorphisms in the FCN1 gene determine ligand-binding ability and serum levels of M-ficolin." PLoS One 7.11 (2012): e50585.
2. Sokołowska, Anna, et al. "Associations of ficolins and mannose-binding lectin with acute myeloid leukaemia in adults." Scientific Reports 10.1 (2020): 10561.
3. Distributed under Open Access license CC BY 4.0, without modification.