Fibrinogen-like protein 1 (FGL-1) is a
protein that is structurally related to
fibrinogen. In humans, FGL-1 is encoded by the FGL1gene.[5][6] It is classified as a
hepatokine. Four
splice variants exist for this gene.
Function
Fibrinogen-like protein 1 is a member of the fibrinogen family of proteins, which also includes fibrinogen,
fibrinogen-like protein 2, and clotting factors
V,
VIII, and
XIII. FGL-1 is homologous to the
carboxy terminus of the fibrinogen
beta- and
gamma- subunits which contains the four conserved
cysteines of that are common to all members of the fibrinogen family. However, FGL-1 lacks the platelet-binding site, cross-linking region, and
thrombin-sensitive site which allow the other members of the fibrinogen family to aid in
fibrin clot formation.[6]
FGL-1 has also been observed to strongly bind to and activate
LAG-3, a regulatory protein expressed on
T cells. As LAG-3 has an important role in controlling
activated T cells, manipulating FGL-1 binding to T cells has been proposed for both
cancer immunotherapy and
anti-inflammatory treatments.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Yamamoto T, Gotoh M, Sasaki H, Terada M, Kitajima M, Hirohashi S (Jul 1993). "Molecular cloning and initial characterization of a novel fibrinogen-related gene, HFREP-1". Biochem Biophys Res Commun. 193 (2): 681–7.
doi:
10.1006/bbrc.1993.1678.
PMID8390249.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
Hara H, Yoshimura H, Uchida S, et al. (2001). "Molecular cloning and functional expression analysis of a cDNA for human hepassocin, a liver-specific protein with hepatocyte mitogenic activity". Biochim. Biophys. Acta. 1520 (1): 45–53.
doi:
10.1016/s0167-4781(01)00249-4.
PMID11470158.
Yan J, Yu Y, Wang N, et al. (2004). "LFIRE-1/HFREP-1, a liver-specific gene, is frequently downregulated and has growth suppressor activity in hepatocellular carcinoma". Oncogene. 23 (10): 1939–49.
doi:
10.1038/sj.onc.1207306.
PMID14981537.
S2CID9243597.
Fibrinogen-like protein 1 (FGL-1) is a
protein that is structurally related to
fibrinogen. In humans, FGL-1 is encoded by the FGL1gene.[5][6] It is classified as a
hepatokine. Four
splice variants exist for this gene.
Function
Fibrinogen-like protein 1 is a member of the fibrinogen family of proteins, which also includes fibrinogen,
fibrinogen-like protein 2, and clotting factors
V,
VIII, and
XIII. FGL-1 is homologous to the
carboxy terminus of the fibrinogen
beta- and
gamma- subunits which contains the four conserved
cysteines of that are common to all members of the fibrinogen family. However, FGL-1 lacks the platelet-binding site, cross-linking region, and
thrombin-sensitive site which allow the other members of the fibrinogen family to aid in
fibrin clot formation.[6]
FGL-1 has also been observed to strongly bind to and activate
LAG-3, a regulatory protein expressed on
T cells. As LAG-3 has an important role in controlling
activated T cells, manipulating FGL-1 binding to T cells has been proposed for both
cancer immunotherapy and
anti-inflammatory treatments.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Yamamoto T, Gotoh M, Sasaki H, Terada M, Kitajima M, Hirohashi S (Jul 1993). "Molecular cloning and initial characterization of a novel fibrinogen-related gene, HFREP-1". Biochem Biophys Res Commun. 193 (2): 681–7.
doi:
10.1006/bbrc.1993.1678.
PMID8390249.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
Hara H, Yoshimura H, Uchida S, et al. (2001). "Molecular cloning and functional expression analysis of a cDNA for human hepassocin, a liver-specific protein with hepatocyte mitogenic activity". Biochim. Biophys. Acta. 1520 (1): 45–53.
doi:
10.1016/s0167-4781(01)00249-4.
PMID11470158.
Yan J, Yu Y, Wang N, et al. (2004). "LFIRE-1/HFREP-1, a liver-specific gene, is frequently downregulated and has growth suppressor activity in hepatocellular carcinoma". Oncogene. 23 (10): 1939–49.
doi:
10.1038/sj.onc.1207306.
PMID14981537.
S2CID9243597.