Fibrinogen beta chain: Difference between revisions

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{{Infobox_gene}}
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'''Fibrinogen beta chain''', also known as '''FGB''', is a [[gene]] found in humans and most other [[vertebrate]]s with a similar system of [[blood coagulation]].
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FGB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fza.
| PDB = {{PDB2|1fza}}, {{PDB2|1fzb}}, {{PDB2|1fzc}}, {{PDB2|1fze}}, {{PDB2|1fzf}}, {{PDB2|1fzg}}, {{PDB2|1lt9}}, {{PDB2|1ltj}}, {{PDB2|1n86}}, {{PDB2|1n8e}}, {{PDB2|1re3}}, {{PDB2|1re4}}, {{PDB2|1rf0}}, {{PDB2|1rf1}}, {{PDB2|2a45}}, {{PDB2|2ffd}}, {{PDB2|2h43}}, {{PDB2|2hod}}, {{PDB2|2hpc}}, {{PDB2|2oyh}}, {{PDB2|2oyi}}
| Name = Fibrinogen beta chain
| HGNCid = 3662
| Symbol = FGB
| AltSymbols =; MGC104327; MGC120405
| OMIM = 134830
| ECnumber = 
| Homologene = 3772
| MGIid = 99501
| GeneAtlas_image1 = PBB_GE_FGB_216238_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FGB_204988_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005577 |text = fibrinogen complex}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0030168 |text = platelet activation}} {{GNF_GO|id=GO:0051258 |text = protein polymerization}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2244
    | Hs_Ensembl = ENSG00000171564
    | Hs_RefseqProtein = NP_005132
    | Hs_RefseqmRNA = NM_005141
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 155703596
    | Hs_GenLoc_end = 155711683
    | Hs_Uniprot = P02675
    | Mm_EntrezGene = 110135
    | Mm_Ensembl = ENSMUSG00000033831
    | Mm_RefseqmRNA = NM_181849
    | Mm_RefseqProtein = NP_862897
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 83128174
    | Mm_GenLoc_end = 83135736
    | Mm_Uniprot = Q3TGR2
  }}
}}
'''Fibrinogen beta chain''', also known as '''FGB''', is a human [[gene]].


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =
| summary_text = The protein encoded by this gene is the beta component of fibrinogen, a blood-borne glycoprotein comprised 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 afibrinogenemia, dysfibrinogenemia, hypodysfibrinogenemia and thrombotic tendency.<ref>{{cite web | title = Entrez Gene: FGB fibrinogen beta chain| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2244| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is the beta 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 afibrinogenemia, dysfibrinogenemia, hypodysfibrinogenemia and thrombotic tendency.<ref>{{cite web | title = Entrez Gene: FGB fibrinogen beta chain| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2244| accessdate = }}</ref>
}}
}}
==Interactions==
Fibrinogen beta chain has been shown to [[Protein-protein interaction|interact]] with [[Lipoprotein(a)]].<ref name=pmid10980194>{{cite journal |last=Klose |first=R |authorlink= |author2=Fresser F |author3=Kochl S |author4=Parson W |author5=Kapetanopoulos A |author6=Fruchart-Najib J |author7=Baier G |author8=Utermann G  |date=December 2000|title=Mapping of a minimal apolipoprotein(a) interaction motif conserved in fibrin(ogen) beta - and gamma -chains |journal=J. Biol. Chem. |volume=275 |issue=49 |pages=38206–12 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10980194 |doi = 10.1074/jbc.M003640200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==See also==
==See also==
Line 59: Line 15:


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| citations =
*{{cite journal  | author=Doolittle RF |title=Fibrinogen and fibrin. |journal=Annu. Rev. Biochem. |volume=53 |issue=  |pages= 195-229 |year= 1984 |pmid= 6383194 |doi= 10.1146/annurev.bi.53.070184.001211 }}
*{{cite journal  | author=Doolittle RF |title=Fibrinogen and fibrin. |journal=Annu. Rev. Biochem. |volume=53 |issue=  |pages= 195–229 |year= 1984 |pmid= 6383194 |doi= 10.1146/annurev.bi.53.070184.001211 }}
*{{cite journal  | author=Vasse M, Paysant J, Soria J, ''et al.'' |title=Regulation of fibrinogen biosynthesis by cytokines, consequences on the vascular risk. |journal=Haemostasis |volume=26 Suppl 4 |issue=  |pages= 331-9 |year= 1997 |pmid= 8979138 |doi=  }}
*{{cite journal  |vauthors=Vasse M, Paysant J, Soria J |title=Regulation of fibrinogen biosynthesis by cytokines, consequences on the vascular risk. |journal=Haemostasis |volume=26 Suppl 4 |issue=  |pages= 331–9 |year= 1997 |pmid= 8979138 |doi=  10.1159/000217313|display-authors=etal}}
*{{cite journal  | author=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=  }}
*{{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=Redman CM, Xia H |title=Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion. |journal=Ann. N. Y. Acad. Sci. |volume=936 |issue=  |pages= 480-95 |year= 2001 |pmid= 11460506 |doi= }}
*{{cite journal  |vauthors=Redman CM, Xia H |title=Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion. |journal=Ann. N. Y. Acad. Sci. |volume=936 |issue=  |pages= 480–95 |year= 2001 |pmid= 11460506 |doi=10.1111/j.1749-6632.2001.tb03535.x  }}
*{{cite journal  | author=Brennan SO, Fellowes AP, George PM |title=Molecular mechanisms of hypo- and afibrinogenemia. |journal=Ann. N. Y. Acad. Sci. |volume=936 |issue=  |pages= 91-100 |year= 2001 |pmid= 11460528 |doi=  }}
*{{cite journal  |vauthors=Brennan SO, Fellowes AP, George PM |title=Molecular mechanisms of hypo- and afibrinogenemia. |journal=Ann. N. Y. Acad. Sci. |volume=936 |issue=  |pages= 91–100 |year= 2001 |pmid= 11460528 |doi=10.1111/j.1749-6632.2001.tb03496.x }}
*{{cite journal  | author=Everse SJ |title=New insights into fibrin (ogen) structure and function. |journal=Vox Sang. |volume=83 Suppl 1 |issue=  |pages= 375-82 |year= 2003 |pmid= 12617173 |doi=  }}
*{{cite journal  | author=Everse SJ |title=New insights into fibrin (ogen) structure and function. |journal=Vox Sang. |volume=83 Suppl 1 |issue=  |pages= 375–82 |year= 2003 |pmid= 12617173 |doi=  10.1111/j.1423-0410.2002.tb05338.x}}
*{{cite journal  | author=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 }}
*{{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 }}
*{{cite journal  | author=Lord ST |title=Fibrinogen and fibrin: scaffold proteins in hemostasis. |journal=Curr. Opin. Hematol. |volume=14 |issue= 3 |pages= 236-41 |year= 2007 |pmid= 17414213 |doi= 10.1097/MOH.0b013e3280dce58c }}
*{{cite journal  | author=Lord ST |title=Fibrinogen and fibrin: scaffold proteins in hemostasis. |journal=Curr. Opin. Hematol. |volume=14 |issue= 3 |pages= 236–41 |year= 2007 |pmid= 17414213 |doi= 10.1097/MOH.0b013e3280dce58c }}
*{{cite journal  | author=Chen XC, Xu MT, Zhou W, ''et al.'' |title=A meta-analysis of relationship between beta-fibrinogen gene -148C/T polymorphism and susceptibility to cerebral infarction in Han Chinese. |journal=Chin. Med. J. |volume=120 |issue= 13 |pages= 1198-202 |year= 2007 |pmid= 17637253 |doi=  }}
*{{cite journal  |vauthors=Chen XC, Xu MT, Zhou W |title=A meta-analysis of relationship between beta-fibrinogen gene -148C/T polymorphism and susceptibility to cerebral infarction in Han Chinese. |journal=Chin. Med. J. |volume=120 |issue= 13 |pages= 1198–202 |year= 2007 |pmid= 17637253 |doi=  |display-authors=etal}}
*{{cite journal  | author=Tarakhovskiĭ IuS, Galushchenko IV, Boroviagin VL, ''et al.'' |title=[Temperature-dependent changes in the profile of the sarcoplasmic reticulum membrane hydrophobic zones] |journal=Biokhimiia |volume=44 |issue= 5 |pages= 897-902 |year= 1979 |pmid= 156564 |doi=  }}
*{{cite journal  |author1=Tarakhovskiĭ IuS |author2=Galushchenko IV |author3=Boroviagin VL |title=[Temperature-dependent changes in the profile of the sarcoplasmic reticulum membrane hydrophobic zones] |journal=Biokhimiia |volume=44 |issue= 5 |pages= 897–902 |year= 1979 |pmid= 156564 |doi=  |display-authors=etal}}
*{{cite journal  | author=Watt KW, Takagi T, Doolittle RF |title=Amino acid sequence of the beta chain of human fibrinogen. |journal=Biochemistry |volume=18 |issue= 1 |pages= 68-76 |year= 1979 |pmid= 420779 |doi=  }}
*{{cite journal  |vauthors=Watt KW, Takagi T, Doolittle RF |title=Amino acid sequence of the beta chain of human fibrinogen. |journal=Biochemistry |volume=18 |issue= 1 |pages= 68–76 |year= 1979 |pmid= 420779 |doi=10.1021/bi00568a011 }}
*{{cite journal  | author=Gårdlund B, Hessel B, Marguerie G, ''et al.'' |title=Primary structure of human fibrinogen. Characterization of disulfide-containing cyanogen-bromide fragments. |journal=Eur. J. Biochem. |volume=77 |issue= 3 |pages= 595-610 |year= 1977 |pmid= 891553 |doi=  }}
*{{cite journal  |vauthors=Gårdlund B, Hessel B, Marguerie G |title=Primary structure of human fibrinogen. Characterization of disulfide-containing cyanogen-bromide fragments. |journal=Eur. J. Biochem. |volume=77 |issue= 3 |pages= 595–610 |year= 1977 |pmid= 891553 |doi=10.1111/j.1432-1033.1977.tb11704.x |display-authors=etal}}
*{{cite journal  | author=Blombäck B, Hessel B, Hogg D |title=Disulfide bridges in nh2 -terminal part of human fibrinogen. |journal=Thromb. Res. |volume=8 |issue= 5 |pages= 639-58 |year= 1976 |pmid= 936108 |doi=  }}
*{{cite journal  |vauthors=Blombäck B, Hessel B, Hogg D |title=Disulfide bridges in nh2 -terminal part of human fibrinogen. |journal=Thromb. Res. |volume=8 |issue= 5 |pages= 639–58 |year= 1976 |pmid= 936108 |doi=10.1016/0049-3848(76)90245-0 }}
*{{cite journal  | author=Koopman J, Haverkate F, Grimbergen J, ''et al.'' |title=Abnormal fibrinogens IJmuiden (B beta Arg14----Cys) and Nijmegen (B beta Arg44----Cys) form disulfide-linked fibrinogen-albumin complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 8 |pages= 3478-82 |year= 1992 |pmid= 1565641 |doi=  }}
*{{cite journal  |vauthors=Koopman J, Haverkate F, Grimbergen J |title=Abnormal fibrinogens IJmuiden (B beta Arg14----Cys) and Nijmegen (B beta Arg44----Cys) form disulfide-linked fibrinogen-albumin complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 8 |pages= 3478–82 |year= 1992 |pmid= 1565641 |doi=  10.1073/pnas.89.8.3478| pmc=48891  |display-authors=etal}}
*{{cite journal  | author=Koopman J, Haverkate F, Lord ST, ''et al.'' |title=Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of B beta 68 Ala----Thr. |journal=J. Clin. Invest. |volume=90 |issue= 1 |pages= 238-44 |year= 1992 |pmid= 1634610 |doi=  }}
*{{cite journal  |vauthors=Koopman J, Haverkate F, Lord ST |title=Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of B beta 68 Ala----Thr. |journal=J. Clin. Invest. |volume=90 |issue= 1 |pages= 238–44 |year= 1992 |pmid= 1634610 |doi=10.1172/JCI115841 | pmc=443086  |display-authors=etal}}
*{{cite journal  | author=Wu C, Chung AE |title=Potential role of entactin in hemostasis. Specific interaction of entactin with fibrinogen A alpha and B beta chains. |journal=J. Biol. Chem. |volume=266 |issue= 28 |pages= 18802-7 |year= 1991 |pmid= 1680863 |doi=  }}
*{{cite journal  |vauthors=Wu C, Chung AE |title=Potential role of entactin in hemostasis. Specific interaction of entactin with fibrinogen A alpha and B beta chains. |journal=J. Biol. Chem. |volume=266 |issue= 28 |pages= 18802–7 |year= 1991 |pmid= 1680863 |doi=  }}
*{{cite journal  | author=Yoshida N, Wada H, Morita K, ''et al.'' |title=A new congenital abnormal fibrinogen Ise characterized by the replacement of B beta glycine-15 by cysteine. |journal=Blood |volume=77 |issue= 9 |pages= 1958-63 |year= 1991 |pmid= 2018836 |doi=  }}
*{{cite journal  |vauthors=Yoshida N, Wada H, Morita K |title=A new congenital abnormal fibrinogen Ise characterized by the replacement of B beta glycine-15 by cysteine. |journal=Blood |volume=77 |issue= 9 |pages= 1958–63 |year= 1991 |pmid= 2018836 |doi=  |display-authors=etal}}
*{{cite journal  | author=Chung DW, Harris JE, Davie EW |title=Nucleotide sequences of the three genes coding for human fibrinogen. |journal=Adv. Exp. Med. Biol. |volume=281 |issue=  |pages= 39-48 |year= 1991 |pmid= 2102623 |doi=  }}
*{{cite journal  |vauthors=Chung DW, Harris JE, Davie EW |title=Nucleotide sequences of the three genes coding for human fibrinogen. |journal=Adv. Exp. Med. Biol. |volume=281 |issue=  |pages= 39–48 |year= 1991 |pmid= 2102623 |doi=  10.1007/978-1-4615-3806-6_3 }}
*{{cite journal  | author=Danishefsky K, Hartwig R, Banerjee D, Redman C |title=Intracellular fate of fibrinogen B beta chain expressed in COS cells. |journal=Biochim. Biophys. Acta |volume=1048 |issue= 2-3 |pages= 202-8 |year= 1990 |pmid= 2322576 |doi=  }}
*{{cite journal  |vauthors=Danishefsky K, Hartwig R, Banerjee D, Redman C |title=Intracellular fate of fibrinogen B beta chain expressed in COS cells. |journal=Biochim. Biophys. Acta |volume=1048 |issue= 2–3 |pages= 202–8 |year= 1990 |pmid= 2322576 |doi=  10.1016/0167-4781(90)90057-9}}
*{{cite journal  | author=Berg K, Kierulf P |title=DNA polymorphisms at fibrinogen loci and plasma fibrinogen concentration. |journal=Clin. Genet. |volume=36 |issue= 4 |pages= 229-35 |year= 1989 |pmid= 2572363 |doi=  }}
*{{cite journal  |vauthors=Berg K, Kierulf P |title=DNA polymorphisms at fibrinogen loci and plasma fibrinogen concentration |journal=Clin. Genet. |volume=36 |issue= 4 |pages= 229–35 |year= 1989 |pmid= 2572363 |doi=10.1111/j.1399-0004.1989.tb03195.x }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=2244}}
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Revision as of 00:47, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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RefSeq (mRNA)

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View/Edit Human

Fibrinogen beta chain, also known as FGB, is a gene found in humans and most other vertebrates with a similar system of blood coagulation.

The protein encoded by this gene is the beta 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 afibrinogenemia, dysfibrinogenemia, hypodysfibrinogenemia and thrombotic tendency.[1]

Interactions

Fibrinogen beta chain has been shown to interact with Lipoprotein(a).[2]

See also

References

  1. ↑ "Entrez Gene: FGB fibrinogen beta chain".
  2. ↑ Klose, R; Fresser F; Kochl S; Parson W; Kapetanopoulos A; Fruchart-Najib J; Baier G; Utermann G (December 2000). "Mapping of a minimal apolipoprotein(a) interaction motif conserved in fibrin(ogen) beta - and gamma -chains". J. Biol. Chem. UNITED STATES. 275 (49): 38206–12. doi:10.1074/jbc.M003640200. ISSN 0021-9258. PMID 10980194.

Further reading



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