Fibrinogen gamma chain

Fibrinogen gamma chain, also known as fibrinogen gamma gene (FGG), is a human gene found on chromosome 3.^[5]

FGG
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1DUG, 1FIB, 1FIC, 1FID, 1FZA, 1FZB, 1FZC, 1FZE, 1FZF, 1FZG, 1LT9, 1LTJ, 1N86, 1N8E, 1RE3, 1RE4, 1RF0, 1RF1, 2A45, 2FFD, 2FIB, 2H43, 2HLO, 2HOD, 2HPC, 2HWL, 2OYH, 2OYI, 2Q9I, 2VDO, 2VDP, 2VDQ, 2VDR, 2VR3, 2XNX, 2XNY, 2Y7L, 2Z4E, 3BVH, 3E1I, 3FIB, 3GHG, 3H32, 3HUS, 4B60
Identifiers
Aliases	FGG, fibrinogen gamma chain
External IDs	OMIM: 134850 MGI: 95526 HomoloGene: 429 GeneCards: FGG
Gene location (Human) Chr. Chromosome 4 (human)^[1] Band 4q32.1 Start 154,604,134 bp^[1] End 154,612,967 bp^[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)^[2] Band 3 E3|3 36.94 cM Start 82,915,031 bp^[2] End 82,922,356 bp^[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver lower lobe of lung right adrenal gland gallbladder upper lobe of lung upper lobe of left lung right lung body of stomach body of pancreas fundus Top expressed in left lobe of liver lacrimal gland yolk sac gallbladder parotid gland abdominal wall sexually immature organism primitive streak atrioventricular valve incisor More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein-macromolecule adaptor activity structural molecule activity metal ion binding protein binding signaling receptor binding cell adhesion molecule binding protein homodimerization activity extracellular matrix structural constituent Cellular component cytoplasm platelet alpha granule blood microparticle plasma membrane fibrinogen complex extracellular region cell surface extracellular exosome platelet alpha granule lumen external side of plasma membrane extracellular space endoplasmic reticulum lumen collagen-containing extracellular matrix Biological process hemostasis negative regulation of endothelial cell apoptotic process positive regulation of peptide hormone secretion protein polymerization positive regulation of heterotypic cell-cell adhesion fibrinolysis platelet degranulation blood coagulation extracellular matrix organization protein secretion response to calcium ion positive regulation of substrate adhesion-dependent cell spreading negative regulation of extrinsic apoptotic signaling pathway via death domain receptors positive regulation of vasoconstriction positive regulation of protein secretion positive regulation of ERK1 and ERK2 cascade positive regulation of exocytosis blood coagulation, fibrin clot formation plasminogen activation cell-matrix adhesion platelet aggregation signal transduction platelet activation toll-like receptor signaling pathway platelet maturation cellular response to interleukin-1 cellular response to interleukin-6 negative regulation of platelet aggregation post-translational protein modification Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2266 99571 Ensembl ENSG00000171557 ENSMUSG00000033860 UniProt P02679 Q8VCM7 RefSeq (mRNA) NM_021870 NM_000509 NM_133862 NM_001317105 RefSeq (protein) NP_000500 NP_068656 NP_001304034 NP_598623 Location (UCSC) Chr 4: 154.6 – 154.61 Mb Chr 3: 82.92 – 82.92 Mb PubMed search ^[3] ^[4]
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene is the gamma component of fibrinogen, a blood-borne glycoprotein composed of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia and thrombophilia.^[6] Alternative splicing of the mRNA chain results in two transcript variants; the common γA chain and the alternatively spliced γ' chain. Approximately 10% of the total plasma fibrinogen consists of γA/γ' fibrinogen, with <1% consisting of γ'/γ' fibrinogen. Increased and decreased levels of γA/γ' fibrinogen have been associated with coronary artery disease and deep vein thrombosis respectively. In the lung parenchyma of smokers, upregulation of FGG transcript levels has been reported. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000171557 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000033860 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Emeis J (2007). "A guide to murine coagulation factor structure, function, assays, and genetic alterations". Journal of Thrombosis and Haemostasis. 5 (4): 670–679. doi:10.1111/j.1538-7836.2007.02408.x. PMID 17403201.
6. "Entrez Gene: FGG fibrinogen gamma chain".
7. Pintarelli G, Noci S, Maspero D, Pettinicchio A, Dugo M, De Cecco L, Incarbone M, Tosi D, Santambrogio L, Dragani TA, Colombo F (September 2019). "Cigarette smoke alters the transcriptome of non-involved lung tissue in lung adenocarcinoma patients". Scientific Reports. 9 (1): 13039. Bibcode:2019NatSR...913039P. doi:10.1038/s41598-019-49648-2. PMC 6736939. PMID 31506599.

Further reading

• Doolittle RF (1984). "Fibrinogen and fibrin". Annu. Rev. Biochem. 53: 195–229. doi:10.1146/annurev.bi.53.070184.001211. PMID 6383194.
• Herrick S, Blanc-Brude O, Gray A, Laurent G (1999). "Fibrinogen". Int. J. Biochem. Cell Biol. 31 (7): 741–6. doi:10.1016/S1357-2725(99)00032-1. PMID 10467729.
• Everse SJ (2003). "New insights into fibrin (ogen) structure and function". Vox Sang. 83 (Suppl 1): 375–82. doi:10.1111/j.1423-0410.2002.tb05338.x. PMID 12617173. S2CID 21813767.
• Mosesson MW (2003). "Fibrinogen gamma chain functions". J. Thromb. Haemost. 1 (2): 231–8. doi:10.1046/j.1538-7836.2003.00063.x. PMID 12871494. S2CID 40708829.
• Scott EM, Ariëns RA, Grant PJ (2005). "Genetic and environmental determinants of fibrin structure and function: relevance to clinical disease". Arterioscler. Thromb. Vasc. Biol. 24 (9): 1558–66. doi:10.1161/01.ATV.0000136649.83297.bf. PMID 15217804. S2CID 21298700.