Isolation and characterization of a thermolabile β-2 macroglycoprotein (‘thermolabile substance’ or ‘Hakata antigen’) detected by precipitating (auto) antibody in sera of patients with systemic lupus erythematosus

Yae, Yoshiaki; Inaba, Shinji; Sato, Hiroyuki; Okochi, Kazuo; Tokunaga, Fuminori; Iwanaga, Sadaaki

doi:10.1016/0167-4838(91)90158-v

Cited by 62 publications

(60 citation statements)

References 17 publications

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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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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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“…We document that affinity chromatography on acetylated surfaces may be used for purification of H-ficolin from serum. The presented method does not require large amounts of monoclonal anti-H-ficolin antibody, as was used in a method described previously (26), and selects for actively binding forms of H-ficolin.…”

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confidence: 99%

“…Although similar in structure, H-ficolin (gi: 27754776) is quite different at the amino acid sequence level as compared with L-ficolin and M-ficolin with a sequence identity of only 45 and 46%, respectively. H-ficolin is synthesized by hepatocytes and bile duct epithelial cells where the protein is then secreted into the bloodstream and bile, respectively (25,26). H-ficolin is also found in the mucosa of the lung where it originates from bronchial epithelial cells and alveolar type II epithelial cells (25).…”

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confidence: 99%

Studies of the Pattern Recognition Molecule H-ficolin

Zacho

Jensen

Terp

et al. 2012

Journal of Biological Chemistry

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Background: H-ficolin is a pattern recognition molecule of the human innate immune system. Results: The ligand specificity of H-ficolin is explored, and a purification procedure is developed. Conclusion: H-ficolin binds to patterns of acetyl groups and activates complement upon binding. Significance: The findings expand and emphasize the differences of the specificities of the three human ficolins (H-, L-, and M-ficolin).

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“…Compared with MBL the main structural difference is the lack of an ␣-helical region and a globular domain which is a fibrinogen-like (fbg) domain rather than the C-type lectin domain of MBL (11). Like MBL, L-ficolin and H-ficolin are capable of forming trimeric subunits, which associate into oligomers comprised of up to 4 and 6 trimers, respectively (12,13). Like MBL, L-ficolin and H-ficolin circulate in complex with MASPs and are capable of activating the complement system (14 -16).…”

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confidence: 99%

L-ficolin Is a Pattern Recognition Molecule Specific for Acetyl Groups

Krarup

Thiel

Hansen

et al. 2004

Journal of Biological Chemistry

185

154

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L-ficolin and H-ficolin are molecules of the innate immune system. Upon recognition of a suitable target they activate the complement system. The ligand recognition structure of ficolins is contained within a fibrinogen-like domain. We examined the selectivity of the ficolins through inhibiting the binding to bacteria or to beads coupled with N-acetylglucosamine. The binding of L-ficolin to Streptococcus pneumoniae 11F and the beads was inhibited by N-acetylated sugars and not by non-acetylated sugars. However, it was also inhibited by other acetylated compounds. Based on this selectivity L-ficolin is not easily defined as a lectin. The binding of H-ficolin to Aerococcus viridans was not inhibited by any of the sugars or other compounds examined. Based on the selectivity of L-ficolin we developed a new purification procedure involving affinity chromatography on N-acetylcysteine-derivatized Sepharose. The column was loaded in the presence of EDTA and high salt, and L-ficolin was eluted by decreasing the salt concentration. Further purification was achieved by ion exchange chromatography.

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Isolation and characterization of a thermolabile β-2 macroglycoprotein (‘thermolabile substance’ or ‘Hakata antigen’) detected by precipitating (auto) antibody in sera of patients with systemic lupus erythematosus

Cited by 62 publications

References 17 publications

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

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

Studies of the Pattern Recognition Molecule H-ficolin

L-ficolin Is a Pattern Recognition Molecule Specific for Acetyl Groups

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