同: FGF-1

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2019/06/20 17:25:55」(JST)

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FGF1, also known as acidic fibroblast growth factor (aFGF), is a growth factor and signaling protein encoded by the FGF1 gene.^[5]^[6] It is synthesized as a 155 amino acid polypeptide, whose mature form is a non-glycosylated 17-18 kDa protein. Fibroblast growth factor protein was first purified in 1975, but soon afterwards others using different conditions isolated acidic FGF, Heparin-binding growth factor-1, and Endothelial cell growth factor-1.^[7] Gene sequencing revealed that this group was actually the same growth factor and that FGF1 was a member of a family of FGF proteins.

FGF-1 has no definitive signal sequence and thus is not secreted through classical pathways, but it does appear to form a disulfide linked dimer inside cells that associate with a complex of proteins at the cell membrane (including S100A13 and Syt1) which then help flip it through the membrane to the exterior of the cell.^[8]^[9] Once in the reducing conditions of the surrounding tissue, the dimer dissociates into monomeric FGF1 that can enter systemic circulation or be sequestered in tissues binding to heparan sulfate proteoglycans of the extracellular matrix. FGF1 can then bind to and exert its effects via specific fibroblast growth factor receptor (FGFR) proteins which themselves constitute a family of closely related molecules.^[10]

In addition to its extracellular activity, FGF1 can also function intracellularly. The protein has a nuclear localization sequence (NLS) but the route that FGF1 takes to get to the nucleus is unclear and it appears that some sort of cell surface receptor binding is necessary, followed by its internalization and translocation to the nucleus whereupon it can interact with nuclear isoforms of FGFRs.^[10] This is different from FGF2 which also can activate nuclear FGFRs but has splicing variants of the protein that never leave the cell and go directly to the nucleus.

Function

FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described.^[11]

FGF1 is multifunctional with many reported effects. For one example, in mice with diet-induced diabetes that is an experimental equivalent of type 2 diabetes in humans, a single injection of the FGF1 protein is enough to restore blood sugar levels to a healthy range for > 2 days.^[12]

Interactions

FGF1 has been shown to interact with:

CSNK2A2^[13]
CSNK2B^[13]
CSNK2A1^[13]
FIBP^[14]
FGFR1^[15]^[16]
FGFR2^[16]^[17]^[18]
FGFR3^[16]^[19]
FGFR4^[20]^[21]
HSPA9^[22] and
S100A13^[9]^[23]^[24]
Synaptotagmin 1 (SYT1) ^[9]^[23]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000113578 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000036585 - Ensembl, May 2017
^ "Human PubMed Reference:".
^ "Mouse PubMed Reference:".
^ Dionne CA, Crumley G, Bellot F, Kaplow JM, Searfoss G, Ruta M, Burgess WH, Jaye M, Schlessinger J (September 1990). "Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors". The EMBO Journal. 9 (9): 2685–92. PMC 551973. PMID 1697263.
^ Jaye M, Howk R, Burgess W, Ricca GA, Chiu IM, Ravera MW, O'Brien SJ, Modi WS, Maciag T, Drohan WN (August 1986). "Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization". Science. 233 (4763): 541–5. doi:10.1126/science.3523756. PMID 3523756.
^ Burgess WH, Maciag T (1989). "The heparin-binding (fibroblast) growth factor family of proteins". Annual Review of Biochemistry. 58: 575–606. doi:10.1146/annurev.bi.58.070189.003043. PMID 2549857.
^ Tarantini F, Gamble S, Jackson A, Maciag T (December 1995). "The cysteine residue responsible for the release of fibroblast growth factor-1 residues in a domain independent of the domain for phosphatidylserine binding". The Journal of Biological Chemistry. 270 (49): 29039–42. doi:10.1074/jbc.270.49.29039. PMID 7493920.
^ ^a ^b ^c Prudovsky I, Bagala C, Tarantini F, Mandinova A, Soldi R, Bellum S, Maciag T (July 2002). "The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export". The Journal of Cell Biology. 158 (2): 201–8. doi:10.1083/jcb.200203084. PMC 2173119. PMID 12135982.
^ ^a ^b Coleman SJ, Bruce C, Chioni AM, Kocher HM, Grose RP (August 2014). "The ins and outs of fibroblast growth factor receptor signalling". Clinical Science. 127 (4): 217–31. doi:10.1042/CS20140100. PMID 24780002.
^ "Entrez Gene: FGF1 fibroblast growth factor 1 (acidic)".
^ Suh JM, Jonker JW, Ahmadian M, Goetz R, Lackey D, Osborn O, Huang Z, Liu W, Yoshihara E, van Dijk TH, Havinga R, Fan W, Yin YQ, Yu RT, Liddle C, Atkins AR, Olefsky JM, Mohammadi M, Downes M, Evans RM (September 2014). "Endocrinization of FGF1 produces a neomorphic and potent insulin sensitizer". Nature. 513 (7518): 436–9. doi:10.1038/nature13540. PMC 4184286. PMID 25043058. Lay summary – Salk Institute.
^ ^a ^b ^c Skjerpen CS, Nilsen T, Wesche J, Olsnes S (August 2002). "Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity". The EMBO Journal. 21 (15): 4058–69. doi:10.1093/emboj/cdf402. PMC 126148. PMID 12145206.
^ Kolpakova E, Wiedłocha A, Stenmark H, Klingenberg O, Falnes PO, Olsnes S (November 1998). "Cloning of an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor". The Biochemical Journal. 336 (1): 213–22. doi:10.1042/bj3360213. PMC 1219860. PMID 9806903.
^ Schlessinger J, Plotnikov AN, Ibrahimi OA, Eliseenkova AV, Yeh BK, Yayon A, Linhardt RJ, Mohammadi M (September 2000). "Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization". Molecular Cell. 6 (3): 743–50. doi:10.1016/s1097-2765(00)00073-3. PMID 11030354.
^ ^a ^b ^c Santos-Ocampo S, Colvin JS, Chellaiah A, Ornitz DM (January 1996). "Expression and biological activity of mouse fibroblast growth factor-9". The Journal of Biological Chemistry. 271 (3): 1726–31. doi:10.1074/jbc.271.3.1726. PMID 8576175.
^ Stauber DJ, DiGabriele AD, Hendrickson WA (January 2000). "Structural interactions of fibroblast growth factor receptor with its ligands". Proceedings of the National Academy of Sciences of the United States of America. 97 (1): 49–54. doi:10.1073/pnas.97.1.49. PMC 26614. PMID 10618369.
^ Pellegrini L, Burke DF, von Delft F, Mulloy B, Blundell TL (October 2000). "Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin". Nature. 407 (6807): 1029–34. doi:10.1038/35039551. PMID 11069186.
^ Chellaiah A, Yuan W, Chellaiah M, Ornitz DM (December 1999). "Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity". The Journal of Biological Chemistry. 274 (49): 34785–94. doi:10.1074/jbc.274.49.34785. PMID 10574949.
^ Loo BB, Darwish KK, Vainikka SS, Saarikettu JJ, Vihko PP, Hermonen JJ, Goldman AA, Alitalo KK, Jalkanen MM (May 2000). "Production and characterization of the extracellular domain of recombinant human fibroblast growth factor receptor 4". The International Journal of Biochemistry & Cell Biology. 32 (5): 489–97. doi:10.1016/S1357-2725(99)00145-4. PMID 10736564.
^ Kan M, Wu X, Wang F, McKeehan WL (May 1999). "Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase". The Journal of Biological Chemistry. 274 (22): 15947–52. doi:10.1074/jbc.274.22.15947. PMID 10336501.
^ Mizukoshi E, Suzuki M, Loupatov A, Uruno T, Hayashi H, Misono T, Kaul SC, Wadhwa R, Imamura T (October 1999). "Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin". The Biochemical Journal. 343 (2): 461–6. doi:10.1042/0264-6021:3430461. PMC 1220575. PMID 10510314.
^ ^a ^b Mouta Carreira C, LaVallee TM, Tarantini F, Jackson A, Lathrop JT, Hampton B, Burgess WH, Maciag T (August 1998). "S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro". The Journal of Biological Chemistry. 273 (35): 22224–31. doi:10.1074/jbc.273.35.22224. PMID 9712836.
^ Landriscina M, Bagalá C, Mandinova A, Soldi R, Micucci I, Bellum S, Prudovsky I, Maciag T (July 2001). "Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress". The Journal of Biological Chemistry. 276 (27): 25549–57. doi:10.1074/jbc.M102925200. PMID 11432880.

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1. 難治性狭心症マネージメントのための血管新生療法therapeutic angiogenesis for management of refractory angina [show details]
…efficacy of intramyocardial FGF-1 (acidic FGF or aFGF) was evaluated in 20 patients with three vessel disease undergoing coronary artery bypass graft surgery (CABG); FGF-1 was injected at the site of the …
2. 頭蓋骨縫合早期癒合症候群craniosynostosis syndromes [show details]
3. インスリン様成長因子1の生理学physiology of insulin like growth factor 1 [show details]
4. びまん性神経膠腫の分子学的発症機序molecular pathogenesis of diffuse gliomas [show details]
5. 特発性肺線維症の病因pathogenesis of idiopathic pulmonary fibrosis [show details]

English Journal

Genetic Interaction of and is Associated with Memory Impairment and Hippocampal Atrophy in Alzheimer's Disease.

Chang YT, Kazui H, Ikeda M, Huang CW, Huang SH, Hsu SW, Chang WN, Chang CC.
Aging and disease. 2019 Jun;10(3)510-519.
The and fibroblast growth factor 1 () have both been associated with amyloid β accumulation and neurodegeneration. Investigation the effect of interactions on episodic memory (EM) deficits and hippocampus atrophy (HA) might elucidate the complex clinical-pathological relationship in Alzheimer's d
PMID 31164996

Tricalcium silicate cements: osteogenic and angiogenic responses of human bone marrow stem cells.

Ali MRW, Mustafa M, Bårdsen A, Bletsa A.
European journal of oral sciences. 2019 Jun;127(3)261-268.
Tricalcium silicate cements (TSCs) are used in endodontic procedures to promote wound healing and hard tissue formation. The aim of this study was to evaluate and compare the effect of commonly used TSCs [mineral trioxide aggregate (MTA), Biodentine, and TotalFill] on cellular metabolism and osteoge
PMID 30958908

miRNA-210-3p regulates trophoblast proliferation and invasiveness through fibroblast growth factor 1 in selective intrauterine growth restriction.

Li L, Huang X, He Z, Xiong Y, Fang Q.
Journal of cellular and molecular medicine. 2019 Jun;23(6)4422-4433.
Selective intrauterine growth restriction (sIUGR), which affects approximately 10%-15% of monochorionic (MC) twin pregnancies, is highly associated with intrauterine foetal death and neurological impairment in both twins. Data suggest that unequal sharing of the single placenta is the main contribut
PMID 30993882

Japanese Journal

レクチンとしての繊維芽細胞増殖因子 (第1土曜特集レクチン医学最前線) -- (レクチンの新たな視点)

浅田眞弘
医学のあゆみ 269(9), 738-742, 2019-06-01
NAID 40021898273

Epac1 deficiency inhibits basic fibroblast growth factor-mediated vascular smooth muscle cell migration

Kato Yuko,Yokoyama Utako,Fujita Takayuki,Umemura Masanari,Kubota Tetsuo,Ishikawa Yoshihiro
The journal of physiological sciences 69(2), 175-184, 2019-03
NAID 40021818894

インプラント体埋入部に近接する骨欠損への炭酸含有アパタイト　－bFGF複合体の応用

向井景祐,金山圭一,森永啓嗣,竹内浩子,木村洋子,長谷川徹,北後光信,佐藤匠,清水雄太,伊神裕高,渋谷俊昭
岐阜歯科学会雑誌 = The Journal of Gifu Dental Society 45(3), 165-173, 2019-02
… In the study described here, the authors investigated the efficacy of a complex in which carbonate-containing apatite (CA) was used as a carrier and basic fibroblast growth factor (bFGF) was added in the augmentation of bone surrounding implants. … Remnant CA granules were observed, but obvious bone augmentation was seen in the fibroblast growth factor (FGF) + CA group. …
NAID 120006606096

「線維芽細胞増殖因子」

FGF1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4QO3, 1AXM, 1DJS, 1DZC, 1DZD, 1E0O, 1EVT, 1HKN, 1JQZ, 1JT3, 1JT4, 1JT5, 1JT7, 1JTC, 1JY0, 1K5U, 1K5V, 1M16, 1NZK, 1P63, 1PZZ, 1Q03, 1Q04, 1RG8, 1RML, 1RY7, 1YTO, 1Z2V, 1Z4S, 2AFG, 2AQZ, 2AXM, 2ERM, 2HW9, 2HWA, 2HWM, 2HZ9, 2K43, 2K4A, 2K8R, 2KI4, 2KI6, 2NTD, 2Q9X, 2RQ9, 3B9U, 3BA4, 3BA5, 3BA7, 3BAD, 3BAG, 3BAH, 3BAO, 3BAQ, 3BAU, 3BAV, 3BB2, 3CQA, 3CRG, 3CRH, 3CRI, 3CU1, 3FGM, 3FJ8, 3FJ9, 3FJA, 3FJB, 3FJC, 3FJD, 3FJE, 3FJF, 3FJH, 3FJI, 3FJJ, 3FJK, 3HOM, 3JUT, 3K1X, 3O3Q, 3OJ2, 3OJM, 3OJV, 3UD7, 3UD8, 3UD9, 3UDA, 4J23, 4Q91, 4Q9G, 4Q9P, 4QAL, 4QBC, 4QBV, 4QC4, 4XKI, 4YOL
Identifiers
Aliases	FGF1, AFGF, ECGF, ECGF-beta, ECGFA, ECGFB, FGF-1, FGF-alpha, FGFA, GLIO703, HBGF-1, HBGF1, fibroblast growth factor 1
External IDs	OMIM: 131220 MGI: 95515 HomoloGene: 625 GeneCards: FGF1
Gene location (Human)
Chr.	Chromosome 5 (human)
End	142,698,070 bp
Gene location (Mouse)
Chr.	Chromosome 18 (mouse)
End	38,929,472 bp
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• S100 protein binding; • protein binding; • growth factor activity; • protein tyrosine kinase activity; • Ras guanyl-nucleotide exchange factor activity; • phosphatidylinositol-4,5-bisphosphate 3-kinase activity; • fibroblast growth factor receptor binding; • integrin binding; • 1-phosphatidylinositol-3-kinase activity; • heparin binding; • Hsp70 protein binding;
Cellular component	• cytoplasm; • cytosol; • extracellular region; • cell cortex; • nucleolus; • cell nucleus; • extracellular space; • extracellular matrix;
Biological process	• cell differentiation; • cellular response to heat; • positive regulation of protein phosphorylation; • positive regulation of MAP kinase activity; • organ induction; • lung development; • positive regulation of epithelial cell proliferation; • anatomical structure morphogenesis; • positive regulation of intracellular signal transduction; • branch elongation involved in ureteric bud branching; • positive regulation of angiogenesis; • MAPK cascade; • multicellular organism development; • mesonephric epithelium development; • angiogenesis; • regulation of endothelial cell chemotaxis to fibroblast growth factor; • positive regulation of cholesterol biosynthetic process; • cell proliferation; • positive regulation of cell division; • positive regulation of transcription from RNA polymerase II promoter; • signal transduction; • phosphatidylinositol phosphorylation; • peptidyl-tyrosine phosphorylation; • positive regulation of sprouting angiogenesis; • activation of MAPK activity; • fibroblast growth factor receptor signaling pathway; • positive regulation of cell proliferation; • phosphatidylinositol-3-phosphate biosynthetic process; • regulation of endothelial tube morphogenesis; • positive regulation of cell migration; • positive regulation of endothelial cell migration; • activation of protein kinase B activity; • regulation of receptor activity; • positive regulation of protein kinase B signaling;
	Sources:Amigo / QuickGO
Orthologs
	2246
	14164
	ENSG00000113578
	ENSMUSG00000036585
	P05230
	P61148
NM_000800; NM_001144892; NM_001144934; NM_001144935; NM_001257205;
	NM_001257206; NM_001257207; NM_001257208; NM_001257209; NM_001257210; NM_001257211; NM_001257212; NM_033136; NM_033137; NM_001354955; NM_001354956; NM_001354957; NM_001354958; NM_001354959; NM_001354961; NM_001354963; NM_001354964; NM_001354951; NM_001354952; NM_001354953; NM_001354954; NM_001354962
	NM_010197
NP_000791; NP_001138364; NP_001138406; NP_001138407; NP_001244134;
	NP_001244135; NP_001244136; NP_001244137; NP_001244138; NP_001244139; NP_001244140; NP_001244141; NP_149127; NP_149128; NP_001341884; NP_001341885; NP_001341886; NP_001341887; NP_001341888; NP_001341890; NP_001341892; NP_001341893; NP_001341880; NP_001341881; NP_001341882; NP_001341883; NP_001341891
	NP_034327
	Wikidata
View/Edit Human	View/Edit Mouse

　　[★]

英: fibroblast growth factor, FGF
同: 線維芽細胞成長因子, ヘパリン結合性増殖因子 heparin-binding growth factor HBGF
関: bFGF、FGFファミリー

種類

fibroblast growth factor 1 FGF-1 acidic FGF
fibroblast growth factor 2 FGF-2 basic FGF
fibroblast growth factor 3 FGF-3
fibroblast growth factor 7 FGF-7 Keratinocyte growth factor

「fibroblast growth factor-1」

　　[★]

線維芽細胞増殖因子1、線維芽細胞増殖因子-1、線維芽細胞成長因子1、線維芽細胞成長因子-1

関: acidic fibroblast growth factor、FGF-1、FGF1

「fibroblast growth factor-10」

　　[★]

線維芽細胞増殖因子-10

「grow」

　　[★]

v.

(過去: grew-過去分詞: grown)

成長する、生育する、伸びる

関: extend、growth、outgrow、outgrowth、stretch

「fact」

　　[★]

n.

事実、現状、実際、実態

関: actual、actually、in fact、in practice、indeed、practically

「factor」

　　[★]

n.

因子、要因、要素、ファクター

関: element、elementary、factorial、parameter

「fibroblast」

　　[★] 線維芽細胞

同: fibroblasts, scleroderma phenotype

「growth」

　　[★]

n.

成長

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000113578 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000036585 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid1697263-5] Dionne CA, Crumley G, Bellot F, Kaplow JM, Searfoss G, Ruta M, Burgess WH, Jaye M, Schlessinger J (September 1990). "Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors". The EMBO Journal. 9 (9): 2685–92. PMC 551973. PMID 1697263.

[pmid3523756-6] Jaye M, Howk R, Burgess W, Ricca GA, Chiu IM, Ravera MW, O'Brien SJ, Modi WS, Maciag T, Drohan WN (August 1986). "Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization". Science. 233 (4763): 541–5. doi:10.1126/science.3523756. PMID 3523756.

[7] Burgess WH, Maciag T (1989). "The heparin-binding (fibroblast) growth factor family of proteins". Annual Review of Biochemistry. 58: 575–606. doi:10.1146/annurev.bi.58.070189.003043. PMID 2549857.

[8] Tarantini F, Gamble S, Jackson A, Maciag T (December 1995). "The cysteine residue responsible for the release of fibroblast growth factor-1 residues in a domain independent of the domain for phosphatidylserine binding". The Journal of Biological Chemistry. 270 (49): 29039–42. doi:10.1074/jbc.270.49.29039. PMID 7493920.

[Prudovsky&Maciag-9] Prudovsky I, Bagala C, Tarantini F, Mandinova A, Soldi R, Bellum S, Maciag T (July 2002). "The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export". The Journal of Cell Biology. 158 (2): 201–8. doi:10.1083/jcb.200203084. PMC 2173119. PMID 12135982.

[pmid_24780002-10] Coleman SJ, Bruce C, Chioni AM, Kocher HM, Grose RP (August 2014). "The ins and outs of fibroblast growth factor receptor signalling". Clinical Science. 127 (4): 217–31. doi:10.1042/CS20140100. PMID 24780002.

[11] "Entrez Gene: FGF1 fibroblast growth factor 1 (acidic)".

[12] Suh JM, Jonker JW, Ahmadian M, Goetz R, Lackey D, Osborn O, Huang Z, Liu W, Yoshihara E, van Dijk TH, Havinga R, Fan W, Yin YQ, Yu RT, Liddle C, Atkins AR, Olefsky JM, Mohammadi M, Downes M, Evans RM (September 2014). "Endocrinization of FGF1 produces a neomorphic and potent insulin sensitizer". Nature. 513 (7518): 436–9. doi:10.1038/nature13540. PMC 4184286. PMID 25043058. Lay summary – Salk Institute.

[pmid12145206-13] Skjerpen CS, Nilsen T, Wesche J, Olsnes S (August 2002). "Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity". The EMBO Journal. 21 (15): 4058–69. doi:10.1093/emboj/cdf402. PMC 126148. PMID 12145206.

[pmid9806903-14] Kolpakova E, Wiedłocha A, Stenmark H, Klingenberg O, Falnes PO, Olsnes S (November 1998). "Cloning of an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor". The Biochemical Journal. 336 (1): 213–22. doi:10.1042/bj3360213. PMC 1219860. PMID 9806903.

[pmid11030354-15] Schlessinger J, Plotnikov AN, Ibrahimi OA, Eliseenkova AV, Yeh BK, Yayon A, Linhardt RJ, Mohammadi M (September 2000). "Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization". Molecular Cell. 6 (3): 743–50. doi:10.1016/s1097-2765(00)00073-3. PMID 11030354.

[pmid8576175-16] Santos-Ocampo S, Colvin JS, Chellaiah A, Ornitz DM (January 1996). "Expression and biological activity of mouse fibroblast growth factor-9". The Journal of Biological Chemistry. 271 (3): 1726–31. doi:10.1074/jbc.271.3.1726. PMID 8576175.

[pmid10618369-17] Stauber DJ, DiGabriele AD, Hendrickson WA (January 2000). "Structural interactions of fibroblast growth factor receptor with its ligands". Proceedings of the National Academy of Sciences of the United States of America. 97 (1): 49–54. doi:10.1073/pnas.97.1.49. PMC 26614. PMID 10618369.

[pmid11069186-18] Pellegrini L, Burke DF, von Delft F, Mulloy B, Blundell TL (October 2000). "Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin". Nature. 407 (6807): 1029–34. doi:10.1038/35039551. PMID 11069186.

[pmid10574949-19] Chellaiah A, Yuan W, Chellaiah M, Ornitz DM (December 1999). "Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity". The Journal of Biological Chemistry. 274 (49): 34785–94. doi:10.1074/jbc.274.49.34785. PMID 10574949.

[pmid10736564-20] Loo BB, Darwish KK, Vainikka SS, Saarikettu JJ, Vihko PP, Hermonen JJ, Goldman AA, Alitalo KK, Jalkanen MM (May 2000). "Production and characterization of the extracellular domain of recombinant human fibroblast growth factor receptor 4". The International Journal of Biochemistry & Cell Biology. 32 (5): 489–97. doi:10.1016/S1357-2725(99)00145-4. PMID 10736564.

[pmid10336501-21] Kan M, Wu X, Wang F, McKeehan WL (May 1999). "Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase". The Journal of Biological Chemistry. 274 (22): 15947–52. doi:10.1074/jbc.274.22.15947. PMID 10336501.

[pmid10510314-22] Mizukoshi E, Suzuki M, Loupatov A, Uruno T, Hayashi H, Misono T, Kaul SC, Wadhwa R, Imamura T (October 1999). "Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin". The Biochemical Journal. 343 (2): 461–6. doi:10.1042/0264-6021:3430461. PMC 1220575. PMID 10510314.

[pmid9712836-23] Mouta Carreira C, LaVallee TM, Tarantini F, Jackson A, Lathrop JT, Hampton B, Burgess WH, Maciag T (August 1998). "S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro". The Journal of Biological Chemistry. 273 (35): 22224–31. doi:10.1074/jbc.273.35.22224. PMID 9712836.

[pmid11432880-24] Landriscina M, Bagalá C, Mandinova A, Soldi R, Micucci I, Bellum S, Prudovsky I, Maciag T (July 2001). "Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress". The Journal of Biological Chemistry. 276 (27): 25549–57. doi:10.1074/jbc.M102925200. PMID 11432880.

v t e Intercellular signaling peptides and proteins / ligands
Growth factors	Epidermal growth factor Fibroblast growth factor Nerve growth factor Platelet-derived growth factor Transforming growth factor beta superfamily Vascular endothelial growth factor
Ephrin	EFNA1 EFNA2 EFNA3 EFNA4 EFNA5 EFNB1 EFNB2 EFNB3
Other	Adipokine Agouti signaling protein Agouti-related protein Angiogenic protein CCN intercellular signaling protein Cysteine-rich protein 61 Connective tissue growth factor Nephroblastoma overexpressed protein Cytokine Endothelin EDN1 EDN2 EDN3 Hedgehog protein Interferon Kinin Parathyroid hormone-related protein Semaphorin Somatomedin Tolloid-like metalloproteinase Tumor necrosis factor Wnt protein
see also extracellular ligand disorders

リンク元	「線維芽細胞増殖因子」
拡張検索	「fibroblast growth factor-1」「fibroblast growth factor-10」
関連記事	「grow」「fact」「factor」「fibroblast」「growth」

匿名

検索

案内

案内

fibroblast growth factor 1