|
|
Gene Symbol |
FGB |
|
Aliases |
HEL-S-78p |
|
Entrez Gene ID |
|
|
Gene Name |
Fibrinogen beta chain |
|
Chromosomal Location |
4q31.3 |
|
HGNC ID |
|
|
Summary |
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. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2014]
|
|
RefSeq DNA |
|
|
RefSeq mRNA |
|
|
e!Ensembl
|
Gene Ontology (GO)
GO ID |
Ontology |
Function |
Evidence |
Reference |
GO:0007160 |
Biological process |
Cell-matrix adhesion |
IDA |
10903502 |
GO:0031639 |
Biological process |
Plasminogen activation |
IDA |
16846481 |
GO:0034116 |
Biological process |
Positive regulation of heterotypic cell-cell adhesion |
IDA |
8100742 |
GO:0034622 |
Biological process |
Cellular protein-containing complex assembly |
IDA |
8910396 |
GO:0042730 |
Biological process |
Fibrinolysis |
IDA |
16846481 |
GO:0043152 |
Biological process |
Induction of bacterial agglutination |
IDA |
24367264 |
GO:0045907 |
Biological process |
Positive regulation of vasoconstriction |
IDA |
15739255 |
GO:0045921 |
Biological process |
Positive regulation of exocytosis |
IDA |
19193866 |
GO:0050714 |
Biological process |
Positive regulation of protein secretion |
IDA |
19193866 |
GO:0051258 |
Biological process |
Protein polymerization |
IDA |
12706644 |
GO:0051592 |
Biological process |
Response to calcium ion |
IDA |
6777381 |
GO:0070374 |
Biological process |
Positive regulation of ERK1 and ERK2 cascade |
IDA |
10903502, 19193866 |
GO:0070527 |
Biological process |
Platelet aggregation |
IDA |
6281794 |
GO:0072378 |
Biological process |
Blood coagulation, fibrin clot formation |
IDA |
16846481 |
GO:0090277 |
Biological process |
Positive regulation of peptide hormone secretion |
IDA |
19193866 |
GO:1900026 |
Biological process |
Positive regulation of substrate adhesion-dependent cell spreading |
NAS |
24041635 |
GO:1902042 |
Biological process |
Negative regulation of extrinsic apoptotic signaling pathway via death domain receptors |
IDA |
10903502 |
GO:2000352 |
Biological process |
Negative regulation of endothelial cell apoptotic process |
IDA |
10903502 |
GO:0005576 |
Cellular component |
Extracellular region |
NAS |
14718574 |
GO:0005577 |
Cellular component |
Fibrinogen complex |
IDA |
6688356, 8910396, 16846481, 18676163 |
GO:0005615 |
Cellular component |
Extracellular space |
HDA |
16502470 |
GO:0005615 |
Cellular component |
Extracellular space |
IDA |
6777381, 19996109 |
GO:0009897 |
Cellular component |
External side of plasma membrane |
IDA |
6777381 |
GO:0009986 |
Cellular component |
Cell surface |
IDA |
6777381 |
GO:0031091 |
Cellular component |
Platelet alpha granule |
IDA |
6777381 |
GO:0062023 |
Cellular component |
Collagen-containing extracellular matrix |
HDA |
25037231, 28327460, 28344315, 28675934 |
GO:0070062 |
Cellular component |
Extracellular exosome |
HDA |
23533145 |
GO:0072562 |
Cellular component |
Blood microparticle |
HDA |
22516433 |
GO:1903561 |
Cellular component |
Extracellular vesicle |
HDA |
24769233 |
GO:0005102 |
Molecular function |
Signaling receptor binding |
IDA |
10903502 |
GO:0005198 |
Molecular function |
Structural molecule activity |
IDA |
8910396 |
GO:0005201 |
Molecular function |
Extracellular matrix structural constituent |
HDA |
28344315 |
GO:0005201 |
Molecular function |
Extracellular matrix structural constituent |
RCA |
25037231, 28327460, 28675934 |
GO:0005515 |
Molecular function |
Protein binding |
IPI |
12706644, 20162731 |
GO:0050839 |
Molecular function |
Cell adhesion molecule binding |
IDA |
9182580 |
GO:0051087 |
Molecular function |
Chaperone binding |
IPI |
19996109 |
|
Protein Information |
|
Protein Name |
Fibrinogen beta chain, beta-fibrinogen, epididymis secretory sperm binding protein Li 78p, fibrinogen, B beta polypeptide |
|
Function |
Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways. |
|
|
|
|
|
UniProt |
|
|
PDB |
6BIJ, 6BIL, 6ATZ, 1FZA, 1FZB, 1FZC, 1FZE, 1FZF, 1FZG, 1LT9, 1LTJ, 1N86, 1N8E, 1RE3, 1RE4, 1RF0, 1RF1, 2A45, 2FFD, 2H43, 2HLO, 2HOD, 2HPC, 2OYH, 2OYI, 2Q9I, 2XNX, 2XNY, 2Z4E, 3BVH, 3E1I, 3GHG, 3H32, 3HUS |
|
|
|
Interactions |
| |
STRING |
MINT |
IntAct |
ENSP00000368880 |
Q12778 |
Q12778 |
|
| |
View interactions
|
|
| |
Associated Diseases
Disease group | Disease Name | References |
Blood Disorders |
Dysfibrinogenemia |
|
Congenital, Hereditary, and Neonatal Diseases and Abnormalities |
Fibrinogen Deficiency |
|
Dysfibrinogenemia |
|
Endocrine System Diseases |
PCOS |
|
Musculoskeletal Diseases |
Osteoporosis |
|
Nervous System Diseases |
Parkinson Disease |
|
Reproductive disorders |
Preeclampsia |
|
|
References |
|
|
Khan Gulafshana Hafeez, Galazis Nicolas, Docheva Nikolina, Layfield Robert, Atiomo William |
Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK gulafshanahafeez@hotmail.com.| Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK.| Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK.| School of Life Sciences, University of Nottingham, Nottingham, UK.| Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK. |
Hum Reprod. 2015 Jan;30(1):133-48. doi: 10.1093/humrep/deu268. Epub 2014 Oct 28. |
Abstract
STUDY QUESTION: Do any proteomic biomarkers previously identified for pre-eclampsia (PE) overlap with those identified in women with polycystic ovary syndrome (PCOS). SUMMARY ANSWER: Five previously identified proteomic biomarkers were found to be common in women with PE and PCOS when compared with controls. WHAT IS KNOWN ALREADY: Various studies have indicated an association between PCOS and PE; however, the pathophysiological mechanisms supporting this association are not known. STUDY DESIGN, SIZE, DURATION: A systematic review and update of our PCOS proteomic biomarker database was performed, along with a parallel review of PE biomarkers. The study included papers from 1980 to December 2013. PARTICIPANTS/MATERIALS, SETTING, METHODS: In all the studies analysed, there were a total of 1423 patients and controls. The number of proteomic biomarkers that were catalogued for PE was 192. MAIN RESULTS AND THE ROLE OF CHANCE: Five proteomic biomarkers were shown to be differentially expressed in women with PE and PCOS when compared with controls: transferrin, fibrinogen alpha, beta and gamma chain variants, kininogen-1, annexin 2 and peroxiredoxin 2. In PE, the biomarkers were identified in serum, plasma and placenta and in PCOS, the biomarkers were identified in serum, follicular fluid, and ovarian and omental biopsies. LIMITATIONS, REASONS FOR CAUTION: The techniques employed to detect proteomics have limited ability in identifying proteins that are of low abundance, some of which may have a diagnostic potential. The sample sizes and number of biomarkers identified from these studies do not exclude the risk of false positives, a limitation of all biomarker studies. The biomarkers common to PE and PCOS were identified from proteomic analyses of different tissues. WIDER IMPLICATIONS OF THE FINDINGS: This data amalgamation of the proteomic studies in PE and in PCOS, for the first time, discovered a panel of five biomarkers for PE which are common to women with PCOS, including transferrin, fibrinogen alpha, beta and gamma chain variants, kininogen-1, annexin 2 and peroxiredoxin 2. If validated, these biomarkers could provide a useful framework for the knowledge infrastructure in this area. To accomplish this goal, a well co-ordinated multidisciplinary collaboration of clinicians, basic scientists and mathematicians is vital. STUDY FUNDING/COMPETING INTERESTS: No financial support was obtained for this project. There are no conflicts of interest. |
|
|
|
|
| © 2019, Biomedical Informatics Centre, NIRRH |
National Institute for Research in Reproductive Health, Jehangir Merwanji Street, Parel, Mumbai-400 012
Tel: 91-22-24192104, Fax No: 91-22-24139412
|