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2018
The human ficolins are homooligomers. Each subunit is composed of an N-terminal region including two cysteine residues, a collagen-like domain, a neck region and a fibrinogen-like domain. Electron microscopy of the whole proteins of human ficolin-2 and ficolin-3 show bouquet-like images, similar to those first described for C1q.
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The human ficolins are homooligomers. Each subunit is composed of an N-terminal region including two cysteine residues, a collagen-like domain, a neck region and a fibrinogen-like domain. Electron microscopy of the whole proteins of human ficolin-2 and ficolin-3 show bouquet-like images, similar to those first described for C1q.
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Histidine-regulated activity of M-ficolin
Biochemical Journal, 2008Human M-ficolin is a pathogen-associated molecular recognition molecule in the innate immune system, and it binds to some sugars, such as GlcNAc (N-acetylglucosamine), on pathogen surfaces. From previous structural and functional studies of the FD1 (M-ficolin fibrinogen-like domain), we proposed that the ligand-binding region of FD1 exists in a ...
Toshiyuki Kohno, Michikazu Tanio
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Experimental and clinical endocrinology & diabetes, 2020
Background Exercise benefits people with abnormal glucose metabolism, and serum ficolin-3 levels have been reported to be associated with diabetes. However, no relevant study has discussed the relationship between high-intensity interval training (HIIT ...
Xiaochen Liu, Gaifeng Wang
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Background Exercise benefits people with abnormal glucose metabolism, and serum ficolin-3 levels have been reported to be associated with diabetes. However, no relevant study has discussed the relationship between high-intensity interval training (HIIT ...
Xiaochen Liu, Gaifeng Wang
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Activation of the lectin complement pathway by ficolins
International Immunopharmacology, 2001Mannose-binding lectin (MBL), a serum lectin specific for mannose or N-acetylglucosamine (GlcNAc), which contains both a collagen-like domain and a carbohydrate-recognition domain (CRD), plays a role in innate immunity by acting as an opsonin and activating complement in association with MBL-associated serine protease (MASP) via the lectin pathway ...
Naotaka Hamasaki +3 more
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Infection and Immunity
Plasmodium falciparum malaria causes significant disease, especially in young children. A successful immune response to P. falciparum is a major determinant of clinical outcome.
Di Zheng +15 more
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Plasmodium falciparum malaria causes significant disease, especially in young children. A successful immune response to P. falciparum is a major determinant of clinical outcome.
Di Zheng +15 more
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Comparative study of the human ficolins reveals unique features of Ficolin-3 (Hakata antigen)
Molecular Immunology, 2008The ficolins and mannose-binding lectin (MBL) are collagen-like defence proteins that serve as recognition molecules in lectin complement pathway. Differential features that may indicate diverse functions of these proteins are poorly understood. In this study we compared important biological features of the ficolins and MBL.
Hummelshoj, Tina +4 more
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Susceptibility to Leprosy is Associated with M-ficolin Polymorphisms
Journal of Clinical Immunology, 2012Mycobacterium leprae exploits complement activation and opsonophagocytosis to infect phagocytes. M-ficolin is encoded by the FCN1 gene and initiates the lectin pathway on monocyte surfaces. We investigated FCN1 promoter polymorphisms that could be responsible for the high interindividual variability of M-ficolin levels and for modulating leprosy ...
Boldt, Angelica B W +9 more
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Molecular Immunology, 2009
We previously reported an association between relative L-ficolin deficiency and recurrent respiratory infections co-existing with allergic disorders in children. To confirm and extend this preliminary finding, we performed a prospective study on children of a similar age (mean 8.9 years) designed to establish whether the principal relationship was with
Agnieszka Szala +13 more
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We previously reported an association between relative L-ficolin deficiency and recurrent respiratory infections co-existing with allergic disorders in children. To confirm and extend this preliminary finding, we performed a prospective study on children of a similar age (mean 8.9 years) designed to establish whether the principal relationship was with
Agnieszka Szala +13 more
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Molecular organization of human Ficolin-2
Molecular Immunology, 2007Human Ficolin-2 (L-Ficolin) is an oligomeric serum protein consisting of a collagen-like stalk and fibrinogen-like recognition domains. The protein binds to arrays of sugars present on different microorganisms, enhances phagocytosis and promotes activation of the lectin complement pathway.
Gérard J. Arlaud +5 more
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Molecular Cloning and Characterization of Mouse Ficolin-A
Biochemical and Biophysical Research Communications, 1998A novel ficolin-related gene was isolated from the mouse liver lambda ZAPII cDNA library. The protein encoded by this gene consists of both collagen- and fibrinogen-like domains, which are common features of the ficolin family, and was named mouse ficolin-A. The amino acid sequence of mouse ficolin-A is 60.2, 59.8, 59.8, and 59.6% identical to those of
Yoshikazu Fujimori +6 more
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