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Ficolins and the lectin complement pathway
1Department of Biochemistry, Fukushima Medical University School of Medicine, Japan. mmatsu@fmu.ac.jp
Immunological Reviews
|June 21, 2001
Summary
Serum ficolins, like mannose-binding lectin (MBL), bind N-acetylglucosamine and activate the complement system. These findings highlight ficolins
Area of Science:
- Immunology
- Biochemistry
- Molecular Biology
Background:
- Ficolins are proteins with collagen-like and fibrinogen-like domains, found in various tissues.
- Serum ficolins function as lectins with specificity for N-acetylglucosamine (GlcNAc).
- Mannose-binding lectin (MBL) is a similar collagenous lectin involved in innate immunity.
Purpose of the Study:
- To investigate the structural and functional similarities between serum ficolins and MBL.
- To determine the role of ficolins in innate immunity and complement activation.
Main Methods:
- Characterization of human serum ficolins (ficolin/P35 and Hakata antigen).
- Investigation of associations between ficolins, MBL-associated serine proteases (MASPs), and sMAP.
- Assessment of complement activation by ficolins.
Main Results:
- Ficolins possess a fibrinogen-like domain responsible for carbohydrate binding.
- Serum ficolins associate with MASPs and sMAP, similar to MBL.
- Ficolins activate the complement system, indicating a role in innate immunity.
Conclusions:
- Serum ficolins are structurally and functionally analogous to MBL.
- Ficolins activate the lectin pathway of complement.
- Ficolins contribute to innate immunity through complement activation.