Disease relevance of FGL1

• We suggest that the HFREP-1 gene is a new member of the fibrinogen family and that further data on the gene are important for a better understanding of the development of hepatocellular carcinomas [1].
• Re-expression of HNF1alpha in human hepatoma HepG2 cells reinduced HPS expression [2].

High impact information on FGL1

• The ficolin 1, 2 and 3 (derived from the FCN1, 2 and 3 genes, respectively) are homologous soluble pattern recognition molecules of importance for innate immunity, comprising collagen-like and fibrinogen-like domains, binding to sugar groups on different types of microorganisms [3].
• FCN2 promoter polymorphisms were associated with marked changes in the Ficolin-2 serum concentration, whereas two polymorphisms clustered in the exon encoding the fibrinogen-like domain were associated with increased and decreased GlcNAc binding, respectively [3].
• Genes that were overexpressed in NASH included complement component C3 and hepatocyte-derived fibrinogen-related protein, potentially contributing to impaired insulin sensitivity [4].
• A truncated monomeric Ang1 variant (i.e. DeltaAng1) containing the isolated fibrinogen-like receptor-binding domain of Ang1 was created and recombinantly produced in insect cells [5].
• These data demonstrate that the epididymis possesses a specific mechanism to identify and envelop defective spermatozoa with a protein complex containing the fibrinogen-like protein fgl2 [6].

Biological context of FGL1

• The deduced amino acid sequences revealed that both cDNAs encoded proteins that were mainly composed of fibrinogen-like and collagen-like domains [7].
• The full-length liver fibrinogen-related gene-1 (LFIRE-1) cDNA was cloned from the human normal liver cDNA library [8].
• Loss of heterozygosity (LOH) analysis revealed allelic loss of LFIRE-1/HFREP-1 on chromosome 8p22 in 57.1% (24/42) of HCC specimens [8].
• The reduction of LFIRE-1/HFREP-1 expression by antisense approach enhances cancer cell proliferation and colony formation in soft agar [8].
• Notably, the downregulation of LFIRE-1/HFREP-1 expression is frequently associated with allelic loss [8].

Anatomical context of FGL1

• These results suggest that hepassocin is a potent regulator in liver cell growth not only in rats but also in humans [9].
• Recombinant human hepassocin produced in Chinese hamster ovary (CHO) cells by the dihydrofolate reductase-methotrexate (DHFR--MTX) gene amplification method is a homodimer (68 kDa) and has mitogenic activities in hepatocytes of various animal species including rat, mouse, rabbit and dog, and the activity was lost with 2-mercaptoethanol treatment [9].
• Characterization of human fibroleukin, a fibrinogen-like protein secreted by T lymphocytes [10].
• Coagulation in the crayfish, Astacus leptodactylus: attempts to identify a fibrinogen-like factor in the hemolymph [11].
• This investigation was conducted to examine the presence of fibrinogen-like substance and thrombin-like enzyme in human semen (human seminal plasma) after liquefaction [12].

Associations of FGL1 with chemical compounds

• High-resolution NMR studies of fibrinogen-like peptides in solution: interaction of thrombin with residues 1-23 of the A alpha chain of human fibrinogen [13].
• Nuclear magnetic resonance study of fibrinogen-like peptides and their structure in dimethyl sulfoxide and water [14].
• Eptifibatide, an integrin antagonist developed to treat cardiovascular disease, served as a high-affinity, monovalent model ligand with fibrinogen-like selectivity for alphaIIbbeta3 [15].
• Ficolins present in sera have a lectin activity toward N-acetylglucosamine through their fibrinogen-like domains [16].
• BACKGROUND: Hakata antigen (Hakata) is a novel serum glycoprotein that consists of collagen- and fibrinogen-like domains, similar to ficolin/p35 [17].

Other interactions of FGL1

• We previously cloned a novel human lectin, designated P35, with both collagen-like and fibrinogen-like domains [18].
• Significant downregulations of FGG, FGL1 and SERPINF2 were also suggested in 30, 23 and 33% of cases, respectively, compared to their nonmalignant counterparts (P<0.016) [19].
• LFIRE-1/HFREP-1, a liver-specific gene, is frequently downregulated and has growth suppressor activity in hepatocellular carcinoma [8].
• The mutagenesis study indicated the domain that is responsible for the ECM association of Ang-1 is the linker peptide region between the coiled-coil and the fibrinogen-like domains [20].
• The vascular walls undergoing fibrinoid necrosis did not show any beta/A4 or cystatin C but presented with fibrinogen-like immunoreactivities, indicating invasion of plasma components [21].

Analytical, diagnostic and therapeutic context of FGL1

• Molecular cloning and initial characterization of a novel fibrinogen-related gene, HFREP-1 [1].
• By Western blotting, the product of the fibrinogen-like protein gene was identified, the recombinant protein isolated, and antibodies raised to this protein [22].

References