FGF1

This article is about fibroblast growth factor-1. For the internal ribosome entry site, see FGF-1 internal ribosome entry site (IRES).

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

Genetically Related Diseases

hypertrophic cardiomyopathy^[1]

Gene ontology
Molecular function	• S100 protein binding • Hsp70 protein binding • protein binding • growth factor activity • receptor binding • 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
Cellular component	• cytoplasm • cytosol • proteinaceous extracellular matrix • nucleoplasm • extracellular space • extracellular region • cell cortex • nucleolus • nucleus
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 • positive regulation of ERK1 and ERK2 cascade • regulation of endothelial cell chemotaxis to fibroblast growth factor • positive regulation of cholesterol biosynthetic process • cell proliferation • positive regulation of cell division • phosphatidylinositol-mediated signaling • positive regulation of transcription from RNA polymerase II promoter • signal transduction • positive regulation of GTPase activity • 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 • regulation of phosphatidylinositol 3-kinase signaling • 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
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


2246


14164

Ensembl


ENSG00000113578


ENSMUSG00000036585

UniProt


P05230


P61148

RefSeq (mRNA)

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_010197

RefSeq (protein)

NP_000791.1 NP_001138364.1 NP_001138406.1 NP_001138407.1 NP_001244134.1
NP_001244136.1 NP_001244137.1 NP_001244138.1 NP_001244139.1 NP_149127.1 NP_149128.1


NP_034327.1

Location (UCSC)

Chr 5: 142.59 – 142.7 Mb

Chr 18: 38.84 – 38.93 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Heparin-binding growth factor 1 is a protein that in humans is encoded by the FGF1 gene.^[4]^[5]

Function

The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. 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.^[6]

In mice with diet-induced diabetes, the equivalent of type 2 diabetes in humans, a single injection of the protein FGF1 is enough to restore blood sugar levels to a healthy range for > 2 days.^[7]

Interactions

FGF1 has been shown to interact with:

References

↑ "Diseases that are genetically associated with FGF1 view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Dionne CA, Crumley G, Bellot F, Kaplow JM, Searfoss G, Ruta M, Burgess WH, Jaye M, Schlessinger J (Sep 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 (Aug 1986). "Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization". Science. 233 (4763): 541–5. doi:10.1126/science.3523756. PMID 3523756.
↑ "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 (Sep 2014). "Endocrinization of FGF1 produces a neomorphic and potent insulin sensitizer". Nature. 513 (7518): 436–9. doi:10.1038/nature13540. PMID 25043058. Lay summary – Salk Institute.
1 2 3 Skjerpen CS, Nilsen T, Wesche J, Olsnes S (Aug 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 (Nov 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 (Sep 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.
1 2 3 Santos-Ocampo S, Colvin JS, Chellaiah A, Ornitz DM (Jan 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 (Jan 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 (Oct 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 (Dec 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 (Oct 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.
↑ Mouta Carreira C, LaVallee TM, Tarantini F, Jackson A, Lathrop JT, Hampton B, Burgess WH, Maciag T (Aug 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 (Jul 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.

Yu YL, Kha H, Golden JA, Migchielsen AA, Goetzl EJ, Turck CW (Apr 1992). "An acidic fibroblast growth factor protein generated by alternate splicing acts like an antagonist". The Journal of Experimental Medicine. 175 (4): 1073–80. doi:10.1084/jem.175.4.1073. PMC 2119192. PMID 1372643.
Chiu IM, Wang WP, Lehtoma K (May 1990). "Alternative splicing generates two forms of mRNA coding for human heparin-binding growth factor 1". Oncogene. 5 (5): 755–62. PMID 1693186.
Zhu X, Komiya H, Chirino A, Faham S, Fox GM, Arakawa T, Hsu BT, Rees DC (Jan 1991). "Three-dimensional structures of acidic and basic fibroblast growth factors". Science. 251 (4989): 90–3. doi:10.1126/science.1702556. PMID 1702556.
Wang WP, Quick D, Balcerzak SP, Needleman SW, Chiu IM (Sep 1991). "Cloning and sequence analysis of the human acidic fibroblast growth factor gene and its preservation in leukemia patients". Oncogene. 6 (9): 1521–9. PMID 1717925.
Wu DQ, Kan MK, Sato GH, Okamoto T, Sato JD (Sep 1991). "Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors". The Journal of Biological Chemistry. 266 (25): 16778–85. PMID 1885605.
Crumley G, Dionne CA, Jaye M (Aug 1990). "The gene for human acidic fibroblast growth factor encodes two upstream exons alternatively spliced to the first coding exon". Biochemical and Biophysical Research Communications. 171 (1): 7–13. doi:10.1016/0006-291X(90)91348-V. PMID 2393407.
Harper JW, Strydom DJ, Lobb RR (Jul 1986). "Human class 1 heparin-binding growth factor: structure and homology to bovine acidic brain fibroblast growth factor". Biochemistry. 25 (14): 4097–103. doi:10.1021/bi00362a017. PMID 2427112.
Winkles JA, Friesel R, Burgess WH, Howk R, Mehlman T, Weinstein R, Maciag T (Oct 1987). "Human vascular smooth muscle cells both express and respond to heparin-binding growth factor I (endothelial cell growth factor)". Proceedings of the National Academy of Sciences of the United States of America. 84 (20): 7124–8. doi:10.1073/pnas.84.20.7124. PMC 299242. PMID 2444975.
Wang WP, Lehtoma K, Varban ML, Krishnan I, Chiu IM (Jun 1989). "Cloning of the gene coding for human class 1 heparin-binding growth factor and its expression in fetal tissues". Molecular and Cellular Biology. 9 (6): 2387–95. PMC 362312. PMID 2474753.
Mergia A, Tischer E, Graves D, Tumolo A, Miller J, Gospodarowicz D, Abraham JA, Shipley GD, Fiddes JC (Nov 1989). "Structural analysis of the gene for human acidic fibroblast growth factor". Biochemical and Biophysical Research Communications. 164 (3): 1121–9. doi:10.1016/0006-291X(89)91785-3. PMID 2590193.
Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA (Jul 1986). "The complete amino acid sequence of human brain-derived acidic fibroblast growth factor". Biochemical and Biophysical Research Communications. 138 (2): 611–7. doi:10.1016/S0006-291X(86)80540-X. PMID 3527167.
Gautschi P, Fràter-Schröder M, Böhlen P (Aug 1986). "Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors". FEBS Letters. 204 (2): 203–7. doi:10.1016/0014-5793(86)80812-2. PMID 3732516.
Gautschi-Sova P, Müller T, Böhlen P (Nov 1986). "Amino acid sequence of human acidic fibroblast growth factor". Biochemical and Biophysical Research Communications. 140 (3): 874–80. doi:10.1016/0006-291X(86)90716-3. PMID 3778488.
Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA (Mar 1986). "Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities". Biochemical and Biophysical Research Communications. 135 (2): 541–8. doi:10.1016/0006-291X(86)90028-8. PMID 3964259.
Zhao XM, Yeoh TK, Hiebert M, Frist WH, Miller GG (Nov 1993). "The expression of acidic fibroblast growth factor (heparin-binding growth factor-1) and cytokine genes in human cardiac allografts and T cells". Transplantation. 56 (5): 1177–82. doi:10.1097/00007890-199311000-00025. PMID 7504343.
Pineda-Lucena A, Jiménez MA, Nieto JL, Santoro J, Rico M, Giménez-Gallego G (Sep 1994). "1H-NMR assignment and solution structure of human acidic fibroblast growth factor activated by inositol hexasulfate". Journal of Molecular Biology. 242 (1): 81–98. doi:10.1006/jmbi.1994.1558. PMID 7521397.
Chotani MA, Payson RA, Winkles JA, Chiu IM (Feb 1995). "Human fibroblast growth factor 1 gene expression in vascular smooth muscle cells is modulated via an alternate promoter in response to serum and phorbol ester". Nucleic Acids Research. 23 (3): 434–41. doi:10.1093/nar/23.3.434. PMC 306694. PMID 7533902.
Opalenik SR, Shin JT, Wehby JN, Mahesh VK, Thompson JA (Jul 1995). "The HIV-1 TAT protein induces the expression and extracellular appearance of acidic fibroblast growth factor". The Journal of Biological Chemistry. 270 (29): 17457–67. doi:10.1074/jbc.270.29.17457. PMID 7542239.
Myers RL, Payson RA, Chotani MA, Deaven LL, Chiu IM (Feb 1993). "Gene structure and differential expression of acidic fibroblast growth factor mRNA: identification and distribution of four different transcripts". Oncogene. 8 (2): 341–9. PMID 7678925.

PDB gallery

1afc: STRUCTURAL STUDIES OF THE BINDING OF THE ANTI-ULCER DRUG SUCROSE OCTASULFATE TO ACIDIC FIBROBLAST GROWTH FACTOR

1axm: HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR

1bar: THREE-DIMENSIONAL STRUCTURES OF ACIDIC AND BASIC FIBROBLAST GROWTH FACTORS

1djs: LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1

1dzc: HIGH RESOLUTION STRUCTURE OF ACIDIC FIBROBLAST GROWTH FACTOR. MUTANT FGF-4-ALA-(23-154), 24 NMR STRUCTURES

1dzd: HIGH RESOLUTION STRUCTURE OF ACIDIC FIBROBLAST GROWTH FACTOR (27-154), 24 NMR STRUCTURES

1e0o: CRYSTAL STRUCTURE OF A TERNARY FGF1-FGFR2-HEPARIN COMPLEX

1evt: CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)

1hkn: A COMPLEX BETWEEN ACIDIC FIBROBLAST GROWTH FACTOR AND 5-AMINO-2-NAPHTHALENESULFONATE

1jqz: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag.

1jt3: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Histidine Tag AND LEU 73 REPLACED BY VAL (L73V)

1jt4: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND VAL 109 REPLACED BY LEU (V109L)

1jt5: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 73 REPLACED BY VAL AND VAL 109 REPLACED BY LEU (L73V/V109L)

1jt7: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 44 REPLACED BY PHE AND LEU 73 REPLACED BY VAL AND VAL 109 REPLACED BY LEU (L44F/L73V/V109L)

1jtc: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 44 REPLACED BY PHE (L44F)

1jy0: Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag and Cys 117 replaced with Val (C117V).

1k5u: Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with His93 replaced by Gly (H93G).

1k5v: Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with Asn106 replaced by Gly (N106G).

1m16: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag and Leu 44 Replaced with Phe (L44F), Leu 73 Replaced with Val (L73V), Val 109 Replaced with Leu (V109L) and Cys 117 Replaced with Val (C117V).

1nzk: Crystal Structure of a Multiple Mutant (L44F, L73V, V109L, L111I, C117V) of Human Acidic Fibroblast Growth Factor

1p63: Human Acidic Fibroblast Growth Factor. 140 Amino Acid Form with Amino Terminal His Tag and Leu111 Replaced with Ile (L111I)

1pzz: Crystal structure of FGF-1, V51N mutant

1q03: Crystal structure of FGF-1, S50G/V51G mutant

1q04: Crystal structure of FGF-1, S50E/V51N

1rg8: Human Acidic Fibroblast Growth Factor (haFGF-1) at 1.10 angstrom resolution (140 amino acid form)

1rml: NMR STUDY OF ACID FIBROBLAST GROWTH FACTOR BOUND TO 1,3,6-NAPHTHALENE TRISULPHONATE, 26 STRUCTURES

1ry7: Crystal Structure of the 3 Ig form of FGFR3c in complex with FGF1

1yto: Crystal Structure of Gly19 deletion Mutant of Human Acidic Fibroblast Growth Factor

1z2v: Crystal Structure of Glu60 deletion Mutant of Human Acidic Fibroblast Growth Factor

1z4s: Crystal Structure of Gly19 and Glu60 deletion mutant of Human Acidic Fibroblast Growth Factor

2afg: 2.0 ANGSTROM X-RAY STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH FACTOR

2aqz: Crystal structure of FGF-1, S17T/N18T/G19 deletion mutant

2axm: HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR

2erm: Solution structure of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue

2j3p: CRYSTAL STRUCTURE OF RAT FGF1 AT 1.4 A

Growth factors

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

EGF-like domain

TGFβ pathway

TGFβ
- TGFβ1
- TGFβ2
- TGFβ3

Insulin-like

IGF1
IGF2

Platelet-derived

Vascular endothelial

Other

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

Growth factor receptor modulators

Angiopoietin

Agonists: Angiopoietin 1
Angiopoietin 4

Antagonists: Angiopoietin 2
Angiopoietin 3

Antibodies: Evinacumab (against angiopoietin 3)
Nesvacumab (against angiopoietin 2)

CNTF

Agonists: Axokine
CNTF
Dapiclermin

EGF (ErbB)

EGF (ErbB1/HER1)	Agonists: Amphiregulin Betacellulin EGF (urogastrone) Epigen Epiregulin Heparin-binding EGF-like growth factor (HB-EGF) Murodermin Nepidermin Transforming growth factor alpha (TGFα) Antibodies: Cetuximab Depatuxizumab Depatuxizumab mafodotin Futuximab Imgatuzumab Matuzumab Necitumumab Nimotuzumab Panitumumab Zalutumumab Kinase inhibitors: Afatinib AG-490 Agerafenib Brigatinib Canertinib Dacomitinib Erlotinib Gefitinib Grandinin Icotinib Lapatinib Neratinib Osimertinib Vandetanib WHI-P 154

ErbB2/HER2	Agonists: Unknown/none Antibodies: Ertumaxomab Pertuzumab Trastuzumab Trastuzumab duocarmazine Trastuzumab emtansine Kinase inhibitors: Afatinib AG-490 Lapatinib Mubritinib Neratinib

ErbB3/HER3	Agonists: Neuregulins (heregulins) (1, 2, 6 (neuroglycan C)) Antibodies: Duligotumab Patritumab Seribantumab

ErbB4/HER4	Agonists: Betacellulin Epigen Heparin-binding EGF-like growth factor (HB-EGF) Neuregulins (heregulins) (1, 2, 3, 4, 5 (tomoregulin, TMEFF))

FGF

FGFR1	Agonists: Ersofermin FGF (1, 2 (bFGF), 3, 4, 5, 6, 8, 10 (KGF2), 20) Repifermin Trafermin Velafermin

FGFR2	Agonists: Ersofermin FGF (1, 2 (bFGF), 3, 4, 5, 6, 7 (KGF), 8, 9, 10 (KGF2), 17, 18, 22) Palifermin Repifermin Sprifermin Trafermin Antibodies: Aprutumab Aprutumab ixadotin

FGFR3	Agonists: Ersofermin FGF (1, 2 (bFGF), 4, 8, 9, 18, 23) Sprifermin Trafermin Antibodies: Burosumab (against FGF23)

FGFR4	Agonists: Ersofermin FGF (1, 2 (bFGF), 4, 6, 8, 9, 19) Trafermin

Unsorted	Agonists: FGF15/19

HGF (c-Met)

Agonists: Hepatocyte growth factor

Potentiators: Dihexa (PNB-0408)

Antibodies: Emibetuzumab
Ficlatuzumab
Flanvotumab
Onartuzumab
Rilotumumab
Telisotuzumab
Telisotuzumab vedotin

Kinase inhibitors: AM7 (drug)
AMG-458
Amuvatinib
BMS-777607
Cabozantinib
Crizotinib
Foretinib
Golvatinib
INCB28060
JNJ-38877605
K252a
MK-2461
PF-04217903
PF-2341066
PHA-665752
SU-11274
Tivantinib
Volitinib

IGF

IGF-1	Agonists: des(1-3)IGF-1 Insulin-like growth factor-1 (somatomedin C) IGF-1 LR3 Insulin-like growth factor-2 (somatomedin A) Insulin Mecasermin Mecasermin rinfabate Antagonists: BMS-754807 Antibodies: AVE1642 Cixutumumab Dalotuzumab Figitumumab Ganitumab Robatumumab R1507 Teprotumumab Kinase inhibitors: Linsitinib NVP-ADW742 NVP-AEW541 OSl-906

IGF-2	Agonists: Insulin-like growth factor-2 (somatomedin A) Antibodies: Dusigitumab

Others	Binding proteins: IGFBP (1, 2, 3, 4, 5, 6, 7) Cleavage products/derivatives with unknown target: Glypromate (GPE, (1-3)IGF-1) Trofinetide

LNGF

Agonists: BDNF
Cenegermin
NGF
NT-3
NT-4

Antagonists: SAR127963

Antibodies: Against NGF: Fasinumab
Fulranumab
Ranevetmab
Tanezumab

PDGF

Agonists: Becaplermin
Platelet-derived growth factor (A, B, C, D)

RET (GFL)

GFRα1	Agonists: Glial cell line-derived neurotrophic factor (GDNF) Liatermin Kinase inhibitors: Vandetanib

GFRα2	Agonists: Neurturin (NRTN) Kinase inhibitors: Vandetanib

GFRα3	Agonists: Artemin (ARTN) Kinase inhibitors: Vandetanib

GFRα4	Agonists: Persephin (PSPN) Kinase inhibitors: Vandetanib

Unsorted	Kinase inhibitors: Agerafenib

SCF (c-Kit)

Agonists: Ancestim
Stem cell factor

TGFβ

See here instead.

Trk

TrkA	Agonists: Amitriptyline Cenegermin Gambogic amide NGF Tavilermide Antagonists: FX007 Kinase inhibitors: Entrectinib K252a Lestaurtinib LOXO-101 Antibodies: Against NGF: Fasinumab Fulranumab Ranevetmab Tanezumab

TrkB	Agonists: 3,7-DHF 3,7,8,2'-THF 4'-DMA-7,8-DHF 7,3'-DHF 7,8-DHF 7,8,2'-THF 7,8,3'-THF Amitriptyline BDNF Deoxygedunin Diosmetin HIOC LM22A-4 N-Acetylserotonin NT-3 NT-4 Norwogonin (5,7,8-THF) R7 TDP6 Antagonists: ANA-12 Cyclotraxin B Gossypetin (3,5,7,8,3',4'-HHF) Kinase inhibitors: Entrectinib K252a Lestaurtinib LOXO-101

TrkC	Agonists: NT-3 Kinase inhibitors: Entrectinib K252a Lestaurtinib LOXO-101

VEGF

Agonists: Placental growth factor (PGF)
Telbermin
VEGF (A, B, C, D (FIGF))

Allosteric modulators: Cyclotraxin B

Decoy receptors: Aflibercept

Others

Additional growth factors: Adrenomedullin
Colony-stimulating factors (see here instead)
Connective tissue growth factor (CTGF)
Ephrins (A1, A2, A3, A4, A5, B1, B2, B3)
Erythropoietin (see here instead)
Glucose-6-phosphate isomerase (GPI; PGI, PHI, AMF)
Glia maturation factor (GMF)
Hepatoma-derived growth factor (HDGF)
Interleukins/T-cell growth factors (see here instead)
Leukemia inhibitory factor (LIF)
Macrophage-stimulating protein (MSP; HLP, HGFLP)
Midkine (NEGF2)
Migration-stimulating factor (MSF; PRG4)
Oncomodulin
Pituitary adenylate cyclase-activating peptide (PACAP)
Pleiotrophin
Renalase
Thrombopoietin (see here instead)
Wnt signaling proteins

Additional growth factor receptor modulators: Cerebrolysin (neurotrophin mixture)

See also: Peptide receptor modulators
Cytokine receptor modulators

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FGF1

Function

Interactions

See also

References

Further reading