Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9

Lu, Jinhua; Tay, Puei Nam; Kon, Oi Lian; Reid, Kenneth B.M.

doi:10.1042/bj3130473

Cited by 105 publications

(63 citation statements)

References 24 publications

(21 reference statements)

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“…Two of these (Cys 13 and Cys 18 ) are involved in forming cross-links within a trimer, and Cys 6 mediates association of trimers into multimers of 1-4 trimers (32). MBP-A Cys 6 is thus similar to Cys 24 of ficolin. Only one or two of the three Cys 6 residues per trimer could participate in bonding between trimers.…”

Section: Ficolin Multimerizationmentioning

confidence: 68%

The Disulfide Bonding Pattern in Ficolin Multimers

Ohashi

Erickson

2004

Journal of Biological Chemistry

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Ficolin is a plasma lectin, consisting of a short Nterminal multimerization domain, a middle collagen domain, and a C-terminal fibrinogen-like domain. The collagen domains assemble the subunits into trimers, and the N-terminal domain assembles four trimers into 12-mers. Two cysteine residues in the N-terminal domain are thought to mediate multimerization by disulfide bonding. We have generated three mutants of ficolin ␣ in which the N-terminal cysteines were substituted by serines (Cys 4 , Cys 24 , and Cys 4 /Cys 24 ). The N-terminal cysteine mutants were produced in a mammalian cell expression system, purified by affinity chromatography, and analyzed under nondenaturing conditions to resolve the multimer structure of the native protein and under denaturing conditions to resolve the disulfidelinked structure. Glycerol gradient sedimentation and electron microscopy in nondenaturing conditions showed that plasma and recombinant wild-type protein formed 12-mers.

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Section: Ficolin Multimerizationmentioning

confidence: 68%

The Disulfide Bonding Pattern in Ficolin Multimers

Ohashi

Erickson

2004

Journal of Biological Chemistry

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“…Three types of ficolins have recently been identified in human, L-ficolin/P35 (FCN2 or ficolin 2) (12), M-ficolin (FCN1 or ficolin 1) (13,14), and H-ficolin/Hakata antigen (FCN3 or ficolin 3) (15)(16)(17), and two types of ficolins, ficolins A and B, have been identified in mice (18,19). The fibrinogen-like domain of L-ficolin, forming a globular structure like the CRD of MBL, is the pattern of carbohydrate structures.…”

Section: Introductionmentioning

confidence: 99%

Specifically Binding of L-ficolin to N-glycans of HCV Envelope Glycoproteins E1 and E2 Leads to Complement Activation

Liu

Ali

et al. 2009

Cell Mol Immunol

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L-ficolin, one of lectin families, is a recently identified complement factor that initiates lectin pathway of complement. Little is known about its role in viral hepatitis. In the present study, we found that L-ficolin in serum from 103 patients with hepatitis C virus (HCV), were significantly higher than that in 150 healthy controls. We further found that L-ficolin expressions were significantly increased in vitro study by HCV JFH-1 infected human hepatocyte cell line Huh7.5.

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“…The amino acid sequence showed that ficolins consist of a short N-terminal domain, a middle collagen-like domain, and a C-terminal fibrinogen-like (fbg) 1 domain (2,(5)(6)(7). A similar three-domain structure applies to complement protein C1q and the collectins, which include mannose binding protein, conglutinin, and pulmonary surfactant proteins A and D (SP-A and SP-D) (9 -12).…”

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confidence: 99%

Two Oligomeric Forms of Plasma Ficolin Have Differential Lectin Activity

Ohashi

Erickson

1997

Journal of Biological Chemistry

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Ficolins are plasma proteins with binding activity for carbohydrates, elastin, and corticosteroids. The ficolin polypeptide has a collagen-like domain that presumably brings three subunits together in a triple helical rod, a C-terminal fibrinogen-like domain (fbg) similar to that of tenascin, which presumably has the binding activities, and a small N-terminal domain that we find to be the primary site for forming the ficolin oligomer. By sedimentation equilibrium we determined that the main plasma form, which we call big ficolin, had mass of 827,000 Da, consistent with 24 subunits. Little ficolin, about half this size, was obtained after binding to a GlcNAc affinity column. Electron microscopy of little ficolin showed a parachute-like structure, with a small globe at one end, corresponding to the 12 N-terminal domains, and the fbg domains clustered together at the ends of the collagen rods. Big ficolin was formed by the face to face fusion of the fbg domains of two little ficolins, leaving the rods and N-terminal domains projecting at opposite ends. Little ficolin maintained a high affinity for the GlcNAc column, and big ficolin had a low affinity or none. The binding sites for ligands may be obscured in this big ficolin oligomer, providing a regulation of their activity.Ficolin was originally isolated as a protein from pig uterus membrane extracts that bound transforming growth factor-␤ (1). Two cDNA clones with very similar sequences, ficolin-␣ and -␤, were obtained by screening a pig uterus cDNA library (2). More recently, ficolins have been identified from human blood as a corticosteroid binding protein, termed hucolin (3), an elastin binding protein, termed EBP-37 (4), and a GlcNAc binding lectin, termed P35 (5). Ficolin cDNAs, termed human ficolin (6), ficolin-1 (7), and P35-related gene (8), were also cloned. cDNA sequences (some of them are partial) suggest that there are two human ficolin genes. One gene codes for human ficolin, ficolin-1, and P35-related gene (which are different names given to this gene product), and the other codes for P35, EBP-37, and hucolin. It is not yet clear how these relate to the two pig genes for ␣ and ␤ ficolins.The amino acid sequence showed that ficolins consist of a short N-terminal domain, a middle collagen-like domain, and a C-terminal fibrinogen-like (fbg) 1 domain (2, 5-7). A similar three-domain structure applies to complement protein C1q and the collectins, which include mannose binding protein, conglutinin, and pulmonary surfactant proteins A and D (SP-A and SP-D) (9 -12). These proteins differ from ficolin in that their C-terminal domain is a C-type lectin instead of fbg, but they all have a middle collagen domain and a small N-terminal domain. The collagen domains assemble these proteins into trimers, and electron microscopy shows that four or six trimers are connected together by the N-terminal domain, leaving the Cterminal lectin domains to project in a multimeric array (13-17).Complement proteins like C1q and collectins play roles in immune defense. Collectin...

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Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9

Cited by 105 publications

References 24 publications

The Disulfide Bonding Pattern in Ficolin Multimers

The Disulfide Bonding Pattern in Ficolin Multimers

Specifically Binding of L-ficolin to N-glycans of HCV Envelope Glycoproteins E1 and E2 Leads to Complement Activation

Two Oligomeric Forms of Plasma Ficolin Have Differential Lectin Activity

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