|
|
Gene Symbol |
FGA |
|
Aliases |
Fib2 |
|
Entrez Gene ID |
|
|
Gene Name |
Fibrinogen alpha chain |
|
Chromosomal Location |
4q31.3 |
|
HGNC ID |
|
|
Summary |
This gene encodes the alpha subunit of the coagulation factor fibrinogen, which is a component of the blood clot. Following vascular injury, the encoded preproprotein is proteolytically processed by thrombin during the conversion of fibrinogen to fibrin. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia, afibrinogenemia and renal amyloidosis. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that undergoes proteolytic processing. [provided by RefSeq, Jan 2016]
|
|
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:0065003 |
Biological process |
Protein-containing complex assembly |
IMP |
18676163 |
GO:0070374 |
Biological process |
Positive regulation of ERK1 and ERK2 cascade |
IDA |
10903502, 19193866 |
GO:0070527 |
Biological process |
Platelet aggregation |
HMP |
23382103 |
GO:0070527 |
Biological process |
Platelet aggregation |
IDA |
6281794 |
GO:0072377 |
Biological process |
Blood coagulation, common pathway |
IMP |
12706644 |
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 |
8910396, 16846481, 18676163 |
GO:0005615 |
Cellular component |
Extracellular space |
IDA |
6777381 |
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, 28344315, 28675934 |
GO:0070062 |
Cellular component |
Extracellular exosome |
HDA |
19056867, 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:0005198 |
Molecular function |
Structural molecule activity |
IMP |
10891444 |
GO:0005201 |
Molecular function |
Extracellular matrix structural constituent |
HDA |
28344315 |
GO:0005201 |
Molecular function |
Extracellular matrix structural constituent |
RCA |
25037231, 28675934 |
GO:0005515 |
Molecular function |
Protein binding |
IPI |
10954706, 12706644, 15174051, 22582013, 25241761, 26091039 |
GO:0050839 |
Molecular function |
Cell adhesion molecule binding |
IDA |
9182580 |
|
Protein Information |
|
Protein Name |
Fibrinogen alpha chain, fibrinogen, A alpha polypeptide |
|
Function |
Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) 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 via an ITGB3-dependent pathway. 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 immune response via both innate and T-cell mediated pathways. |
|
|
|
|
|
UniProt |
|
|
PDB |
1BBR, 1DM4, 1FPH, 1FZA, 1FZB, 1FZC, 1FZD, 1FZE, 1FZF, 1FZG, 1LT9, 1LTJ, 1N86, 1N8E, 1RE3, 1RE4, 1RF0, 1RF1, 1YCP, 2A45, 2FFD, 2H43, 2HLO, 2HOD, 2HPC, 2OYH, 2OYI, 2Q9I, 2XNX, 2XNY, 2Z4E, 3AT0, 3BVH, 3E1I, 3GHG, 3H32, 3HUS, 4F27, 5CFA |
|
|
|
Interactions |
| |
STRING |
MINT |
IntAct |
ENSP00000400341 |
Q9Y261 |
Q9Y261 |
|
| |
View interactions
|
|
| |
Associated Diseases
Disease group | Disease Name | References |
Blood Disorders |
Dysfibrinogenemia |
1912564, 6667926, 6191801, 3618591, 3590111, 3667568, 11460527, 4052020, 11435303, 7298640, 8140431, 2738154, 3345340, 16846481, 4082078, 3726812, 8473507, 14615374 |
Thrombophilia |
|
Cardiovascular Diseases |
Pulmonary thromboembolism |
|
Pulmonary Embolism |
|
Deep Vein Thrombosis |
|
Congenital, Hereditary, and Neonatal Diseases and Abnormalities |
Fibrinogen Deficiency |
|
Afibrinogenemia |
|
Dysfibrinogenemia |
|
Digestive System Diseases |
Liver Diseases |
|
Hepatitis |
|
Cholestasis |
|
Endocrine System Diseases |
PCOS |
|
Musculoskeletal Diseases |
Osteoporosis |
|
Neoplasms |
Mouth Neoplasms |
|
Nervous System Diseases |
Stroke |
|
Nutritional and Metabolic Diseases |
Amyloidosis |
|
|
References |
|
|
Gupta Sajal, Ghulmiyyah Jana, Sharma Rakesh, Halabi Jacques, Agarwal Ashok |
Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA. |
Biomed Res Int. 2014;2014:916212. doi: 10.1155/2014/916212. Epub 2014 May 12. |
Abstract
Endometriosis, PCOS, and unexplained infertility are currently the most common diseases rendering large numbers of women infertile worldwide. Oxidative stress, due to its deleterious effects on proteins and nucleic acids, is postulated to be the one of the important mechanistic pathways in differential expression of proteins and in these diseases. The emerging field of proteomics has allowed identification of proteins involved in cell cycle, as antioxidants, extracellular matrix (ECM), cytoskeleton, and their linkage to oxidative stress in female infertility related diseases. The aim of this paper is to assess the association of oxidative stress and protein expression in the reproductive microenvironments such as endometrial fluid, peritoneal fluid, and follicular fluid, as well as reproductive tissues and serum. The review also highlights the literature that proposes the use of the fertility related proteins as potential biomarkers for noninvasive and early diagnosis of the aforementioned diseases rather than utilizing the more invasive methods used currently. The review will highlight the power of proteomic profiles identified in infertility related disease conditions and their linkage with underlying oxidative stress. The power of proteomics will be reviewed with regard to eliciting molecular mechanisms for early detection and management of these infertility related conditions. |
|
|
Ma Xiang, Fan Lu, Meng Yan, Hou Zheng, Mao Yun-Dong, Wang Wei, Ding Wei, Liu Jia-Yin |
Laboratory of Reproductive Medicine, Nanjing Medical University, and The Center of Clinical Reproductive Medicine, The First Affiliated Hospital of Nanjing Medical University, People's Republic of China. |
Mol Hum Reprod. 2007 Aug;13(8):527-35. doi: 10.1093/molehr/gam036. Epub 2007 Jun |
Abstract
Polycystic ovary syndrome (PCOS) is the most common cause of anovulatory infertility, affecting 5-10% of females of reproductive age. Currently, little is known about the changes in whole proteins between PCOS and normal ovaries. In the present study, a proteomic approach comprised two-dimensional gel electrophoresis (2DE) analysis and mass spectroscopy was used to identify proteins and examine expression patterns in three PCOS and normal ovaries. One hundred and ten protein spots were separated and showed different intensities between PCOS and normal ovaries. Sixty-nine proteins associated with cellular metabolism and physiological process were identified from 72 spots. Fifty-four proteins were up-regulated in PCOS ovaries and 15 other proteins were up-regulated in normal ovaries. These data demonstrate, for the first time, the complexity in the regulation of ovarian protein expression in human PCOS, and will provide important insight for a better understanding of the pathogenetic mechanisms underlying this clinical disorder. |
|
|
Ahn Ji Hyeon, Shin Myoung Chul, Park Joon Ha, Kim In Hye, Lee Jae-Chul, Yan Bing Chun, Hwang In Koo, Moon Seung Myung, Ahn Ji Yun, Ohk Taek Geun, Lee Tae Hun, Cho Jun Hwi, Shin Hyung-Cheul, Won Moo-Ho |
Department of Neurobiology, School of Medicine, Kangwon National University, Chuncheon, Gangwon 200701, Republic of Korea.| Department of Emergency Medicine, School of Medicine, Kangwon National University, Chuncheon, Gangwon 200701, Republic of Korea.| Department of Neurobiology, School of Medicine, Kangwon National University, Chuncheon, Gangwon 200701, Republic of Korea.| Department of Neurobiology, School of Medicine, Kangwon National University, Chuncheon, Gangwon 200701, Republic of Korea.| Department of Neurobiology, School of Medicine, Kangwon National University, Chuncheon, Gangwon 200701, Republic of Korea.| Institute of Integrative Traditional and Western Medicine, Medical College, Yangzhou University, Yangzhou, Jiangsu 225001, P.R. China.| Department of Anatomy and Cell Biology, College of Veterinary Medicine, Seoul National University, Seoul 151742, Republic of Korea.| Department of Neurosurgery, Dongtan Sacred Heart Hospital, College of Medicine, Hallym University, Hwaseong, Gyeonggi 445170, Republic of Korea.| Department of Emergency Medicine, School of Medicine, Kangwon National University, Chuncheon, Gangwon 200701, Republic of Korea.| Department of Emergency Medicine, School of Medicine, Kangwon National University, Chuncheon, Gangwon 200701, Republic of Korea.| Department of Emergency Medicine, Chuncheon Sacred Heart Hospital, College of Medicine, Hallym University, Chuncheon, Gangwon 200702, Republic of Korea.| Department of Emergency Medicine, School of Medicine, Kangwon National University, Chuncheon, Gangwon 200701, Republic of Korea.| Department of Physiology, College of Medicine, Hallym University, Chuncheon, Gangwon 200702, Republic of Korea.| Department of Neurobiology, School of Medicine, Kangwon National University, Chuncheon, Gangwon 200701, Republic of Korea. |
Mol Med Rep. 2015 Feb;11(2):1043-8. doi: 10.3892/mmr.2014.2800. Epub 2014 Oct 29. |
Abstract
Expression of cFos in the spinal cord following nociceptive stimulation is considered to be a neurotoxic biomarker. In the present study, the immunoreactivity of cFos in the spinal cord was compared between young adult (23 years in dogs and 6 months in mice) and aged (1012 years in dogs and 24 months in mice) Beagle dogs and C57BL/6J mice. In addition, changes to neuronal distribution and damage to the spinal cord were also investigated. There were no significant differences in neuronal loss or degeneration of the spinal neurons observed in either the aged dogs or mice. Weak cFos immunoreactivity was observed in the spinal neurons of the young adult animals; however, cFos immunoreactivity was markedly increased in the nuclei of spinal neurons in the aged dogs and mice, as compared with that of the young adults. In conclusion, cFos immunoreactivity was significantly increased without any accompanying neuronal loss in the aged spinal cord of mice and dogs, as compared with the spinal cords of the young adult animals. |
|
|
|
|
| © 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
|