Molecular Cloning and Characterization of Mouse Ficolin-A

Fujimori, Yoshikazu; Harumiya, Satoru; Fukumoto, Yuki; Miura, Yutaka; Yagasaki, Kazumi; Tachikawa, Hiroyuki; Fujimoto, Daisaburo

doi:10.1006/bbrc.1998.8344

Cited by 67 publications

(36 citation statements)

References 20 publications

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“…FcnA is a plasma/serum-type ficolin, which is mainly expressed in the liver, suggesting that FcnA plays its defensive role in the circulation. It is possible that FcnA has a latent defensive ability in the lung, because the Fcna gene is expressed at low level in the lung (34). Expression of the Fcna gene in tissues overlaps to that of the FCN2 gene (35).…”

Section: Discussionmentioning

confidence: 99%

Mice Deficient in Ficolin, a Lectin Complement Pathway Recognition Molecule, Are Susceptible to Streptococcus pneumoniae Infection

Endo

Takahashi

Iwaki

et al. 2012

The Journal of Immunology

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Mannose-binding lectin (MBL) and ficolin are complexed with MBL-associated serine proteases, key enzymes of complement activation via the lectin pathway, and act as soluble pattern recognition molecules in the innate immune system. Although numerous reports have revealed the importance of MBL in infectious diseases and autoimmune disorders, the role of ficolin is still unclear. To define the specific role of ficolin in vivo, we generated model mice deficient in ficolins. The ficolin A (FcnA)–deficient (Fcna−/−) and FcnA/ficolin B double-deficient (Fcna−/−b−/−) mice lacked FcnA-mediated complement activation in the sera, because of the absence of complexes comprising FcnA and MBL-associated serine proteases. When the host defense was evaluated by transnasal infection with a Streptococcus pneumoniae strain, which was recognized by ficolins, but not by MBLs, the survival rate was significantly reduced in all three ficolin-deficient (Fcna−/−, Fcnb−/−, and Fcna−/−b−/−) mice compared with wild-type mice. Reconstitution of the FcnA-mediated lectin pathway in vivo improved survival rate in Fcna−/− but not in Fcna−/−b−/− mice, suggesting that both FcnA and ficolin B are essential in defense against S. pneumoniae. These results suggest that ficolins play a crucial role in innate immunity against pneumococcal infection through the lectin complement pathway.

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Section: Discussionmentioning

confidence: 99%

Mice Deficient in Ficolin, a Lectin Complement Pathway Recognition Molecule, Are Susceptible to Streptococcus pneumoniae Infection

Endo

Takahashi

Iwaki

et al. 2012

The Journal of Immunology

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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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“…In humans, L-and H-ficolins have been characterized in serum whereas Mficolin is mainly expressed by the monocytic cell lineage (5)(6)(7). In addition to humans, ficolins have been identified in different mammalian species including rodents and pigs (8,9), which have two related ficolin genes called A and B and ␣ and ␤, respectively, orthologous to the human L-and M-ficolin genes, respectively (10). To date, H-ficolin has only been identified in humans and it has been reported recently that the mouse and rat homologues of the H-ficolin gene are pseudogenes, which accounts for the absence of the corresponding protein in rodents (10).…”

mentioning

confidence: 99%

Residue Lys57 in the Collagen-Like Region of Human L-Ficolin and Its Counterpart Lys47 in H-Ficolin Play a Key Role in the Interaction with the Mannan-Binding Lectin-Associated Serine Proteases and the Collectin Receptor Calreticulin

Lacroix

Dumestre-Pérard

Schoehn

et al. 2009

The Journal of Immunology

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F icolins are members of the defense collagen family that comprises oligomeric proteins with globular recognition domains able to sense danger signals, such as pathogen-or apoptotic cell-associated molecular patterns, and collagen-like stalks providing the link with immune effectors (1, 2). Ficolins are assembled from homotrimeric subunits comprising a collagen-like triple helix and a lectin-like domain composed of three fibrinogenlike (FBG) 3 domains. Two cysteines at the N-terminal end of the polypeptide chains form interchain disulfide bonds that mediate assembly into higher oligomerization structures (3, 4). In humans, L-and H-ficolins have been characterized in serum whereas Mficolin is mainly expressed by the monocytic cell lineage (5-7). In addition to humans, ficolins have been identified in different mammalian species including rodents and pigs (8, 9), which have two related ficolin genes called A and B and ␣ and ␤, respectively, orthologous to the human L-and M-ficolin genes, respectively (10). To date, H-ficolin has only been identified in humans and it has been reported recently that the mouse and rat homologues of the H-ficolin gene are pseudogenes, which accounts for the absence of the corresponding protein in rodents (10). Like mannan-binding lectin (MBL), ficolins are able to activate the lectin complement pathway in response to recognition of neutral carbohydrates and N-acetyl groups on pathogens and damaged cells. This results from the ability of MBL and ficolins to associate with and trigger activation of MBL-associated serine protease (MASP)-2. Activated MASP-2 cleaves the complement proteins C2 and C4, thereby triggering the complement cascade (11-13). Three other MBL/ficolins-associated proteins have been described, the MASP-1 and MASP-3 proteases (14, 15) and a truncated form of MASP-2 called MAp19 (19-kDa MBL-associated protein) or sMAp (16,17). MASP-3 has no known physiological substrates whereas MASP-1 cleaves with a low efficiency a few protein substrates, among which are fibrinogen and coagulation factor XIII (18). It has been proposed recently that MASP-1 might contribute to the activation of the lectin pathway, but this issue is still controversial (19,20). Complement activation results in opsonization of microbes and apoptotic cells with C3-derived fragments, thus promoting their clearance through interaction with C3 receptors on The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.1 This work was supported by the Commissariat à l'Energie Atomique, the Centre National de la Recherche Scientifique, the Université Joseph Fourier (Grenoble, France).

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Molecular Cloning and Characterization of Mouse Ficolin-A

Cited by 67 publications

References 20 publications

Mice Deficient in Ficolin, a Lectin Complement Pathway Recognition Molecule, Are Susceptible to Streptococcus pneumoniae Infection

Mice Deficient in Ficolin, a Lectin Complement Pathway Recognition Molecule, Are Susceptible to Streptococcus pneumoniae Infection

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

Residue Lys57 in the Collagen-Like Region of Human L-Ficolin and Its Counterpart Lys47 in H-Ficolin Play a Key Role in the Interaction with the Mannan-Binding Lectin-Associated Serine Proteases and the Collectin Receptor Calreticulin

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