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Fibrinogen gamma chain

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{{Short description|Protein-coding gene in the species Homo sapiens}}

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Fibrinogen gamma chain, also known as the fibrinogen gamma gene (FGG), is a human gene found on chromosome 3.{{cite journal |last1=Emeis |first1=J |title=A guide to murine coagulation factor structure, function, assays, and genetic alterations |journal=Journal of Thrombosis and Haemostasis |date=2007 |volume=5 |issue=4 |pages=670–679|doi=10.1111/j.1538-7836.2007.02408.x |pmid=17403201 |doi-access=free }}

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.{{cite web | title = Entrez Gene: FGG fibrinogen gamma chain| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2266}} 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. {{cite journal | vauthors = Pintarelli G, Noci S, Maspero D, Pettinicchio A, Dugo M, De Cecco L, Incarbone M, Tosi D, Santambrogio L, Dragani TA, Colombo F | title = Cigarette smoke alters the transcriptome of non-involved lung tissue in lung adenocarcinoma patients | journal = Scientific Reports | volume = 9 | issue = 1 | pages = 13039 | date = September 2019 | pmid = 31506599 | pmc = 6736939 | doi = 10.1038/s41598-019-49648-2 | bibcode = 2019NatSR...913039P }}

References

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Further reading

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  • {{cite journal | author=Doolittle RF |title=Fibrinogen and fibrin. |journal=Annu. Rev. Biochem. |volume=53 |pages= 195–229 |year= 1984 |pmid= 6383194 |doi= 10.1146/annurev.bi.53.070184.001211 }}
  • {{cite journal | vauthors=Herrick S, Blanc-Brude O, Gray A, Laurent G |title=Fibrinogen. |journal=Int. J. Biochem. Cell Biol. |volume=31 |issue= 7 |pages= 741–6 |year= 1999 |pmid= 10467729 |doi=10.1016/S1357-2725(99)00032-1 }}
  • {{cite journal | author=Everse SJ |title=New insights into fibrin (ogen) structure and function. |journal=Vox Sang. |volume=83 |pages= 375–82 |year= 2003 |issue=Suppl 1 |pmid= 12617173 |doi= 10.1111/j.1423-0410.2002.tb05338.x|s2cid=21813767 }}
  • {{cite journal | author=Mosesson MW |title=Fibrinogen gamma chain functions. |journal=J. Thromb. Haemost. |volume=1 |issue= 2 |pages= 231–8 |year= 2003 |pmid= 12871494 |doi=10.1046/j.1538-7836.2003.00063.x |s2cid=40708829 |doi-access=free }}
  • {{cite journal | vauthors=Scott EM, Ariëns RA, Grant PJ |title=Genetic and environmental determinants of fibrin structure and function: relevance to clinical disease. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 9 |pages= 1558–66 |year= 2005 |pmid= 15217804 |doi= 10.1161/01.ATV.0000136649.83297.bf |s2cid=21298700 |doi-access= }}

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