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- fibroblast growth factor-23
WordNet
- the 6th letter of the Roman alphabet (同)f
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/03/02 02:14:26」(JST)
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Fibroblast growth factor 23 |
PDB rendering based on 2p39. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
2P39
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Identifiers |
Symbols |
FGF23; ADHR; HPDR2; HYPF; PHPTC |
External IDs |
OMIM: 605380 MGI: 1891427 HomoloGene: 10771 GeneCards: FGF23 Gene |
Gene Ontology |
Molecular function |
• type 1 fibroblast growth factor receptor binding
• growth factor activity
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Cellular component |
• extracellular region
• extracellular space
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Biological process |
• phosphate-containing compound metabolic process
• insulin receptor signaling pathway
• fibroblast growth factor receptor signaling pathway
• regulation of phosphate transport
• positive regulation of vitamin D 24-hydroxylase activity
• cell differentiation
• negative regulation of bone mineralization
• cellular phosphate ion homeostasis
• vitamin D catabolic process
• negative regulation of osteoblast differentiation
• positive regulation of transcription, DNA-dependent
• negative regulation of hormone secretion
• phosphate ion homeostasis
• positive regulation of ERK1 and ERK2 cascade
• positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
8074 |
64654 |
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Ensembl |
ENSG00000118972 |
ENSMUSG00000000182 |
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UniProt |
Q9GZV9 |
Q9EPC2 |
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RefSeq (mRNA) |
NM_020638 |
NM_022657 |
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RefSeq (protein) |
NP_065689 |
NP_073148 |
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Location (UCSC) |
Chr 12:
4.48 – 4.49 Mb |
Chr 6:
127.07 – 127.08 Mb |
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PubMed search |
[1] |
[2] |
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Fibroblast growth factor 23 or FGF23 is a protein that in humans is encoded by the FGF23 gene.[1] FGF23 is a member of the fibroblast growth factor (FGF) family which is responsible for phosphate metabolism.[2]
Contents
- 1 Function
- 2 Clinical significance
- 3 References
- 4 Further reading
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Function
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This section is empty. You can help by adding to it. (February 2013) |
Clinical significance
FGF23 is located on chromosome 12 and is composed of three exons. Mutations in FGF23 that render the protein resistant to proteolytic cleavage leads to increased activity of FGF23 and the renal phosphate loss found in the human disease autosomal dominant hypophosphatemic rickets. FGF23 is also overproduced by some types of tumors, such as the benign mesenchymal neoplasm Phosphaturic mesenchymal tumor causing tumor-induced osteomalacia, a paraneoplastic syndrome.[3] Loss of FGF23 activity is thought to lead to increased phosphate levels and the clinical syndrome of familial tumor calcinosis. This gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets.[4] Prior to discovery in 2000, it was hypothesized that a protein existed which performed the function of FGF23. This putative protein was known as phosphatonin.
References
- ^ Yamashita T, Yoshioka M, Itoh N (October 2000). "Identification of a novel fibroblast growth factor, FGF-23, preferentially expressed in the ventrolateral thalamic nucleus of the brain". Biochem. Biophys. Res. Commun. 277 (2): 494–8. doi:10.1006/bbrc.2000.3696. PMID 11032749.
- ^ Fukumoto S (2008). "Physiological regulation and disorders of phosphate metabolism--pivotal role of fibroblast growth factor 23". Intern. Med. 47 (5): 337–43. doi:10.2169/internalmedicine.47.0730. PMID 18310961.
- ^ Zadik Y, Nitzan DW (October 2011). "Tumor induced osteomalacia: A forgotten paraneoplastic syndrome?". Oral Oncol 48 (2): e9–10. doi:10.1016/j.oraloncology.2011.09.011. PMID 21985764.
- ^ "Entrez Gene: FGF23 fibroblast growth factor 23". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8074.
Further reading
- Kiela PR, Ghishan FK (January 2009). "Recent advances in the renal-skeletal-gut axis that controls phosphate homeostasis". Lab. Invest. 89 (1): 7–14. doi:10.1038/labinvest.2008.114. PMID 19029978.
- Silve C, Beck L (2003). "Is FGF23 the long sought after phosphaturic factor phosphatonin?". Nephrol. Dial. Transplant. 17 (6): 958–61. doi:10.1093/ndt/17.6.958. PMID 12032180.
- Quarles LD (2003). "FGF23, PHEX, and MEPE regulation of phosphate homeostasis and skeletal mineralization.". Am. J. Physiol. Endocrinol. Metab. 285 (1): E1–9. doi:10.1152/ajpendo.00016.2003. PMID 12791601.
- Fukagawa M, Nii-Kono T, Kazama JJ (2005). "Role of fibroblast growth factor 23 in health and in chronic kidney disease.". Curr. Opin. Nephrol. Hypertens. 14 (4): 325–9. doi:10.1097/01.mnh.0000172717.49476.80. PMID 15930999.
- Imel EA, Econs MJ (2006). "Fibroblast growth factor 23: roles in health and disease.". J. Am. Soc. Nephrol. 16 (9): 2565–75. doi:10.1681/ASN.2005050573. PMID 16033853.
- Liu S, Quarles LD (2007). "How fibroblast growth factor 23 works.". J. Am. Soc. Nephrol. 18 (6): 1637–47. doi:10.1681/ASN.2007010068. PMID 17494882.
- Econs, Michael J.; Strom, Tim M.; White, Kenneth E.; Evans, Wayne E.; O'Riordan, Jeffery L.H.; Speer, Marcy C.; Lorenz-Depiereux, Bettina; Grabowski, Monika et al. (2000). "Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23.". Nat. Genet. 26 (3): 345–8. doi:10.1038/81664. PMID 11062477.
- White KE, Jonsson KB, Carn G, et al. (2001). "The autosomal dominant hypophosphatemic rickets (ADHR) gene is a secreted polypeptide overexpressed by tumors that cause phosphate wasting.". J. Clin. Endocrinol. Metab. 86 (2): 497–500. doi:10.1210/jc.86.2.497. PMID 11157998.
- Shimada T, Mizutani S, Muto T, et al. (2001). "Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia.". Proc. Natl. Acad. Sci. U.S.A. 98 (11): 6500–5. doi:10.1073/pnas.101545198. PMC 33497. PMID 11344269. //www.ncbi.nlm.nih.gov/pmc/articles/PMC33497/.
- Bowe AE, Finnegan R, Jan de Beur SM, et al. (2001). "FGF-23 inhibits renal tubular phosphate transport and is a PHEX substrate.". Biochem. Biophys. Res. Commun. 284 (4): 977–81. doi:10.1006/bbrc.2001.5084. PMID 11409890.
- White KE, Carn G, Lorenz-Depiereux B, et al. (2002). "Autosomal-dominant hypophosphatemic rickets (ADHR) mutations stabilize FGF-23.". Kidney Int. 60 (6): 2079–86. doi:10.1046/j.1523-1755.2001.00064.x. PMID 11737582.
- Kruse K, Woelfel D, Strom TM, Storm TM (2002). "Loss of renal phosphate wasting in a child with autosomal dominant hypophosphatemic rickets caused by a FGF23 mutation.". Horm. Res. 55 (6): 305–8. doi:10.1159/000050018. PMID 11805436.
- Yamashita T, Konishi M, Miyake A, et al. (2002). "Fibroblast growth factor (FGF)-23 inhibits renal phosphate reabsorption by activation of the mitogen-activated protein kinase pathway.". J. Biol. Chem. 277 (31): 28265–70. doi:10.1074/jbc.M202527200. PMID 12032146.
- Saito H, Kusano K, Kinosaki M, et al. (2003). "Human fibroblast growth factor-23 mutants suppress Na+-dependent phosphate co-transport activity and 1alpha,25-dihydroxyvitamin D3 production.". J. Biol. Chem. 278 (4): 2206–11. doi:10.1074/jbc.M207872200. PMID 12419819.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.ncbi.nlm.nih.gov/pmc/articles/PMC139241/.
- Bai XY, Miao D, Goltzman D, Karaplis AC (2003). "The autosomal dominant hypophosphatemic rickets R176Q mutation in fibroblast growth factor 23 resists proteolytic cleavage and enhances in vivo biological potency.". J. Biol. Chem. 278 (11): 9843–9. doi:10.1074/jbc.M210490200. PMID 12519781.
- Larsson T, Zahradnik R, Lavigne J, et al. (2003). "Immunohistochemical detection of FGF-23 protein in tumors that cause oncogenic osteomalacia.". Eur. J. Endocrinol. 148 (2): 269–76. doi:10.1530/eje.0.1480269. PMID 12590648.
- Campos M, Couture C, Hirata IY, et al. (2003). "Human recombinant endopeptidase PHEX has a strict S1' specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein.". Biochem. J. 373 (Pt 1): 271–9. doi:10.1042/BJ20030287. PMC 1223479. PMID 12678920. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1223479/.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
PDB gallery
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2p39: Crystal structure of human FGF23
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Growth factors
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Fibroblast |
FGF receptor ligands: FGF1/FGF2/FGF5 · FGF3/FGF4/FGF6 · KGF (FGF7/FGF10/FGF22) · FGF8/FGF17/FGF18 · FGF9/FGF16/FGF20
FGF homologous factors: FGF11 · FGF12 · FGF13 · FGF14
hormone-like: FGF19 · FGF21 · FGF23
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EGF-like domain |
TGF-α · EGF · HB-EGF
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TGFβ pathway |
TGF-β (TGF-β1, TGF-β2, TGF-β3)
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Insulin-like |
IGF-1 · IGF-2
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Platelet-derived |
PDGFA · PDGFB · PDGFC · PDGFD
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Vascular endothelial |
VEGF-A · VEGF-B · VEGF-C · VEGF-D · PGF
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Other |
Nerve · Hepatocyte
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B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
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UpToDate Contents
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English Journal
- Resistance to thyroid hormone due to mutations in the THRB gene impairs bone mass and affects calcium and phosphorus homeostasis.
- Cardoso LF1, de Paula FJ1, Maciel LM2.
- Bone.Bone.2014 Oct;67:222-7. doi: 10.1016/j.bone.2014.07.017. Epub 2014 Jul 23.
- CONTEXT: Resistance to thyroid hormone (RTH) is an inherited syndrome of reduced tissue responsiveness to thyroid hormone, which is usually due to mutations in the thyroid hormone receptor β gene (THRB). Few studies have been conducted to investigate bone and mineral metabolism in RTH.OBJECTIVE: Th
- PMID 25063548
- Impact of hemodialysis, left ventricular mass and FGF-23 on myocardial mechanics in end-stage renal disease: a three-dimensional speckle tracking study.
- Kovács A1, Tapolyai M, Celeng C, Gara E, Faludi M, Berta K, Apor A, Nagy A, Tislér A, Merkely B.
- The international journal of cardiovascular imaging.Int J Cardiovasc Imaging.2014 Oct;30(7):1331-7. doi: 10.1007/s10554-014-0480-2. Epub 2014 Jul 8.
- Left ventricular (LV) hypertrophy and one of its inducers, the fibroblast growth factor-23 (FGF-23) were found to be associated with unfavourable outcome in end-stage renal disease (ESRD) patients. We sought to investigate the influence of hemodialysis (HD), increased LV mass and FGF-23 on LV mechan
- PMID 25001896
- Eldecalcitol replaces endogenous calcitriol but does not fully compensate for its action in vivo.
- Saito H1, Harada S2.
- The Journal of steroid biochemistry and molecular biology.J Steroid Biochem Mol Biol.2014 Oct;144PA:189-196. doi: 10.1016/j.jsbmb.2013.11.013. Epub 2013 Nov 26.
- Calcitriol (1α,25-dihydroxyvitamin D3, 1α,25(OH)2D3) is an essential hormone that works in cooperation with parathyroid hormone (PTH) and fibroblast growth factor-23 (FGF-23) to regulate calcium and phosphorus homeostasis. Previous in vivo studies in rats have shown that eldecalcitol, a vitamin D
- PMID 24291401
Japanese Journal
- 骨血管相関におけるリン代謝の重要性 (第15回日本骨粗鬆症学会 シンポジウム1 骨粗鬆症と動脈硬化の接点)
- 今西 康雄,与田 真貴,三木 隆己 [他]
- オステオポローシスジャパン : 日本骨粗鬆症学会雑誌 22(1), 15-18, 2014
- NAID 40019986923
- これからのカルシウム・リン代謝マーカー : 25OHD,FGF-23 (AYUMI 骨代謝マーカーUpdate : 研究と臨床)
- 新着論文 要約と解説 2型糖尿病患者は経口リン摂取に対するFGF23の反応が障害される : 動脈硬化の推定機序
- 中原 健裕,倉林 正彦
- O.li.v.e. : osteo lipid vascular & endocrinology : 骨代謝と生活習慣病の連関 3(3), 165-168, 2013-08
- NAID 40019794777
Related Links
- 線維芽細胞増殖因子(Fibroblast growth factor: FGF). 23はFGF15に対する相同性 によりクローニングさ. れた液性因子であり,FGF19やFGF21と共にFGF19サ. ブ ファミリーに属している. FGF23 遺伝子は251個の. アミノ酸からなる蛋白をコードして いる.
- FGF23はおもに骨組織の骨芽細胞系の細胞により産生される.リン過剰になるとその 産生は亢進する.腎不全による高リン血症において,著しく血中濃度が上昇する.また, 1,25(OH)2DもFGF23産生を刺激する.FGF23は腎臓に作用し,近位尿細管で ...
Related Pictures
★リンクテーブル★
[★]
線維芽細胞増殖因子 fibroblast growth factor
[★]
フェニルアラニン phenylalanine
[★]
- 関
- See Fibroblast growth factors