PDGFA

Mammalian protein found in Homo sapiens

PDGFA

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
3MJK

Identifiers

Aliases

PDGFA, PDGF-A, PDGF1, platelet derived growth factor subunit A

External IDs

OMIM: 173430 MGI: 97527 HomoloGene: 32055 GeneCards: PDGFA

Gene location (Human)

Chr.	Chromosome 7 (human)^[1]

Band	7p22.3	Start	497,258 bp^[1]
Band	7p22.3	End	520,296 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[2]

Band	5 G2\|5 77.65 cM	Start	138,961,769 bp^[2]
Band	5 G2\|5 77.65 cM	End	138,983,125 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

ascending aorta

right coronary artery

body of pancreas

popliteal artery

left coronary artery

optic nerve

body of stomach

middle temporal gyrus

olfactory bulb

left uterine tube

Top expressed in

calvaria

entorhinal cortex

iris

retinal pigment epithelium

tongue

internal carotid artery

ciliary body

external carotid artery

right lung lobe

corneal stroma

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	collagen binding protein homodimerization activity platelet-derived growth factor receptor binding protein binding platelet-derived growth factor binding protein heterodimerization activity growth factor activity phosphatidylinositol-4,5-bisphosphate 3-kinase activity identical protein binding
Cellular component	endoplasmic reticulum lumen membrane Golgi membrane extracellular region microvillus cell surface platelet alpha granule lumen extracellular space Golgi lumen
Biological process	hair follicle development embryonic lung development positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway negative chemotaxis regulation of actin cytoskeleton organization positive regulation of MAP kinase activity regulation of branching involved in salivary gland morphogenesis by epithelial-mesenchymal signaling positive regulation of cell migration positive regulation of fibroblast proliferation cell-cell signaling platelet degranulation extracellular matrix organization regulation of DNA biosynthetic process cell activation MAPK cascade negative regulation of platelet activation multicellular organism development positive regulation of mesenchymal cell proliferation response to wounding cell projection assembly negative regulation of phosphatidylinositol biosynthetic process angiogenesis positive regulation of protein autophosphorylation positive regulation of ERK1 and ERK2 cascade regulation of smooth muscle cell migration animal organ morphogenesis positive regulation of phosphatidylinositol 3-kinase signaling platelet-derived growth factor receptor signaling pathway lung alveolus development positive regulation of cell division actin cytoskeleton organization positive regulation of MAPK cascade skin development regulation of glomerular mesangial cell proliferation regulation of peptidyl-tyrosine phosphorylation wound healing phosphatidylinositol phosphate biosynthetic process positive regulation of cell population proliferation regulation of signaling receptor activity positive regulation of protein kinase B signaling
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


5154


18590

Ensembl


ENSG00000197461


ENSMUSG00000025856

UniProt


P04085


P20033

RefSeq (mRNA)

NM_002607 NM_033023 NM_001395363 NM_001395364 NM_001395365
NM_001395366


NM_008808 NM_001363271

RefSeq (protein)


NP_002598 NP_148983


NP_032834 NP_001350200

Location (UCSC)

Chr 7: 0.5 – 0.52 Mb

Chr 5: 138.96 – 138.98 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Platelet-derived growth factor subunit A is a protein that in humans is encoded by the PDGFA gene.^[5]^[6]

The protein encoded by this gene is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer or as a heterodimer with the platelet-derived growth factor beta polypeptide, where the dimers are connected by disulfide bonds. Studies using knockout mice have shown cellular defects in oligodendrocytes, alveolar smooth muscle cells, and Leydig cells in the testis; knockout mice die either as embryos or shortly after birth. Two splice variants have been identified for this gene.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000197461 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025856 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Stenman G, Rorsman F, Huebner K, Betsholtz C (Sep 1992). "The human platelet-derived growth factor alpha chain (PDGFA) gene maps to chromosome 7p22". Cytogenet Cell Genet. 60 (3–4): 206–7. doi:10.1159/000133337. PMID 1505216.
^ Matsui T, Heidaran M, Miki T, Popescu N, La Rochelle W, Kraus M, Pierce J, Aaronson S (Mar 1989). "Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes". Science. 243 (4892): 800–4. Bibcode:1989Sci...243..800M. doi:10.1126/science.2536956. PMID 2536956.
^ "Entrez Gene: PDGFA platelet-derived growth factor alpha polypeptide".

Nath K, Gogi R, Khan AA, Hameed S (1978). "Vascular hamartoma and vascular tumours of orbit". Indian Journal of Ophthalmology. 25 (1): 18–23. PMID 612586.
Ishibashi T, Bottaro DP, Chan A, et al. (1993). "Expression cloning of a human dual-specificity phosphatase". Proc. Natl. Acad. Sci. U.S.A. 89 (24): 12170–4. doi:10.1073/pnas.89.24.12170. PMC 50720. PMID 1281549.
Raines EW, Lane TF, Iruela-Arispe ML, et al. (1992). "The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors". Proc. Natl. Acad. Sci. U.S.A. 89 (4): 1281–5. Bibcode:1992PNAS...89.1281R. doi:10.1073/pnas.89.4.1281. PMC 48433. PMID 1311092.
Andersson M, Ostman A, Bäckström G, et al. (1992). "Assignment of interchain disulfide bonds in platelet-derived growth factor (PDGF) and evidence for agonist activity of monomeric PDGF". J. Biol. Chem. 267 (16): 11260–6. doi:10.1016/S0021-9258(19)49905-5. PMID 1317862.
Rorsman F, Leveen P, Betsholtz C (1993). "Platelet-derived growth factor (PDGF) A-chain mRNA heterogeneity generated by the use of alternative promoters and alternative polyadenylation sites". Growth Factors. 7 (3): 241–51. doi:10.3109/08977199209046928. PMID 1360804.
Wang Z, Lin XH, Qiu QQ, Deuel TF (1992). "Modulation of transcription of the platelet-derived growth factor A-chain gene by a promoter region sensitive to S1 nuclease". J. Biol. Chem. 267 (24): 17022–31. doi:10.1016/S0021-9258(18)41887-X. PMID 1512241.
Bonthron D, Collins T, Grzeschik KH, et al. (1992). "Platelet-derived growth factor A chain: confirmation of localization of PDGFA to chromosome 7p22 and description of an unusual minisatellite". Genomics. 13 (2): 257–63. doi:10.1016/0888-7543(92)90240-S. PMID 1612586.
Takimoto Y, Wang ZY, Kobler K, Deuel TF (1991). "Promoter region of the human platelet-derived growth factor A-chain gene". Proc. Natl. Acad. Sci. U.S.A. 88 (5): 1686–90. Bibcode:1991PNAS...88.1686T. doi:10.1073/pnas.88.5.1686. PMC 51089. PMID 1848007.
Fabisiak JP, Evans JN, Absher M, et al. (1991). "Expression of platelet-derived growth factor A-chain (PDGF-A) mRNA in lung tissue and cells. Complex regulation during remodeling". Chest. 99 (3 Suppl): 52S–54S. doi:10.1378/chest.99.3_Supplement.52S. PMID 1997274.
Mendoza AE, Young R, Orkin SH, Collins T (1990). "Increased platelet-derived growth factor A-chain expression in human uterine smooth muscle cells during the physiologic hypertrophy of pregnancy". Proc. Natl. Acad. Sci. U.S.A. 87 (6): 2177–81. Bibcode:1990PNAS...87.2177M. doi:10.1073/pnas.87.6.2177. PMC 53649. PMID 2315311.
Claesson-Welsh L, Eriksson A, Westermark B, Heldin CH (1989). "cDNA cloning and expression of the human A-type platelet-derived growth factor (PDGF) receptor establishes structural similarity to the B-type PDGF receptor". Proc. Natl. Acad. Sci. U.S.A. 86 (13): 4917–21. Bibcode:1989PNAS...86.4917C. doi:10.1073/pnas.86.13.4917. PMC 297526. PMID 2544881.
Rorsman F, Bywater M, Knott TJ, et al. (1988). "Structural characterization of the human platelet-derived growth factor A-chain cDNA and gene: alternative exon usage predicts two different precursor proteins". Mol. Cell. Biol. 8 (2): 571–7. doi:10.1128/MCB.8.2.571. PMC 363182. PMID 2832727.
Beckmann MP, Betsholtz C, Heldin CH, et al. (1988). "Comparison of biological properties and transforming potential of human PDGF-A and PDGF-B chains". Science. 241 (4871): 1346–9. Bibcode:1988Sci...241.1346B. doi:10.1126/science.2842868. PMID 2842868.
Bonthron DT, Morton CC, Orkin SH, Collins T (1988). "Platelet-derived growth factor A chain: gene structure, chromosomal location, and basis for alternative mRNA splicing". Proc. Natl. Acad. Sci. U.S.A. 85 (5): 1492–6. Bibcode:1988PNAS...85.1492B. doi:10.1073/pnas.85.5.1492. PMC 279797. PMID 3422746.
Tong BD, Auer DE, Jaye M, et al. (1987). "cDNA clones reveal differences between human glial and endothelial cell platelet-derived growth factor A-chains". Nature. 328 (6131): 619–21. doi:10.1038/328619a0. PMID 3614363. S2CID 4362771.
Collins T, Bonthron DT, Orkin SH (1987). "Alternative RNA splicing affects function of encoded platelet-derived growth factor A chain". Nature. 328 (6131): 621–4. doi:10.1038/328621a0. PMID 3614364. S2CID 4268696.
Hoppe J, Schumacher L, Eichner W, Weich HA (1987). "The long 3'-untranslated regions of the PDGF-A and -B mRNAs are only distantly related". FEBS Lett. 223 (2): 243–6. doi:10.1016/0014-5793(87)80297-1. PMID 3666150. S2CID 46032767.
Betsholtz C, Johnsson A, Heldin CH, et al. (1986). "cDNA sequence and chromosomal localization of human platelet-derived growth factor A-chain and its expression in tumour cell lines". Nature. 320 (6064): 695–9. Bibcode:1986Natur.320..695B. doi:10.1038/320695a0. PMID 3754619. S2CID 4281536.
Takimoto Y, Li WY, Wang ZY, et al. (1993). "Nucleotide sequence of the 5' region of the human platelet-derived growth factor A-chain gene". Hiroshima J. Med. Sci. 42 (1): 47–52. PMID 8486521.

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(FHF3) FGF12(FHF1) FGF13(FHF2) FGF14(FHF4)
hormone-like: FGF15/19	FGF15 FGF19 FGF21 FGF23

EGF-like domain

TGFβ pathway

TGFβ
- TGFβ1
- TGFβ2
- TGFβ3

Insulin/IGF/
Relaxin family

Insulin and Insulin-like growth factor	IGF1 IGF2
Relaxin family peptide hormones	INSL3 INSL4 INSL5 INSL6 Relaxin 1 2 3

Platelet-derived

PDGFA
PDGFB
PDGFC
PDGFD

Vascular endothelial

Other

Growth factor receptor modulators

Angiopoietin

Agonists: Angiopoietin 1
Angiopoietin 4

Antagonists: Angiopoietin 2
Angiopoietin 3

Kinase inhibitors: Altiratinib
CE-245677
Rebastinib

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) Kinase inhibitors: Afatinib Agerafenib Brigatinib Canertinib Dacomitinib Erlotinib Gefitinib Grandinin Icotinib Lapatinib Neratinib Osimertinib Vandetanib WHI-P 154 Antibodies: Cetuximab Depatuxizumab Depatuxizumab mafodotin Futuximab Imgatuzumab Matuzumab Necitumumab Nimotuzumab Panitumumab Zalutumumab
ErbB2/HER2	Agonists: Unknown/none Antibodies: Ertumaxomab Pertuzumab Trastuzumab Trastuzumab deruxtecan Trastuzumab duocarmazine Trastuzumab emtansine Kinase inhibitors: Afatinib Lapatinib Mubritinib Neratinib Tucatinib
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 Selpercatinib Trafermin Velafermin
FGFR2	Agonists: Ersofermin FGF (1, 2 (bFGF), 3, 4, 5, 6, 7 (KGF), 8, 9, 10 (KGF2), 17, 18, 22) Palifermin Repifermin Selpercatinib Sprifermin Trafermin Antibodies: Aprutumab Aprutumab ixadotin Kinase inhibitors: Infigratinib
FGFR3	Agonists: Ersofermin FGF (1, 2 (bFGF), 4, 8, 9, 18, 23) Selpercatinib 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: Fosgonimeton
Hepatocyte growth factor

Potentiators: Dihexa (PNB-0408)

Kinase inhibitors: Altiratinib
AM7
AMG-458
Amuvatinib
BMS-777607
Cabozantinib
Capmatinib
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 Kinase inhibitors: BMS-754807 Linsitinib NVP-ADW742 NVP-AEW541 OSl-906 Antibodies: AVE-1642 Cixutumumab Dalotuzumab Figitumumab Ganitumab Robatumumab R1507 Teprotumumab Xentuzumab (against IGF-1 and IGF-2)
IGF-2	Agonists: Insulin-like growth factor-2 (somatomedin A) Antibodies: Dusigitumab Xentuzumab (against IGF-1 and IGF-2)
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 (p75^NTR)

Antagonists: ALE-0540
Dexamethasone
EVT-901 (SAR-127963)
Testosterone

Antibodies: Against NGF: ABT-110 (PG110)
ASP-6294
Fasinumab
Frunevetmab
Fulranumab
MEDI-578
Ranevetmab
Tanezumab

Aptamers: Against NGF: RBM-004

Decoy receptors: LEVI-04 (p75^NTR-Fc)

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 BNN-20 BNN-27 Cenegermin DHEA DHEA-S Gambogic amide NGF Tavilermide Antagonists: ALE-0540 Dexamethasone FX007 Testosterone Negative allosteric modulators: VM-902A Kinase inhibitors: Altiratinib AZD-6918 CE-245677 CH-7057288 DS-6051 Entrectinib GZ-389988 K252a Larotrectinib Lestaurtinib Milciclib ONO-4474 ONO-5390556 PLX-7486 Rebastinib SNA-120 (pegylated K252a)) Antibodies: Against TrkA: GBR-900; Against NGF: ABT-110 (PG110) ASP-6294 Fasinumab Frunevetmab Fulranumab MEDI-578 Ranevetmab Tanezumab Aptamers: Against NGF: RBM-004 Decoy receptors: ReN-1820 (TrkAd5)
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 BNN-20 Deoxygedunin Deprenyl Diosmetin DMAQ-B1 HIOC LM22A-4 N-Acetylserotonin NT-3 NT-4 Norwogonin (5,7,8-THF) R7 R13 TDP6 Antagonists: ANA-12 Cyclotraxin B Gossypetin (3,5,7,8,3',4'-HHF) Ligands: DHEA Kinase inhibitors: Altiratinib AZD-6918 CE-245677 CH-7057288 DS-6051 Entrectinib GZ-389988 K252a Larotrectinib Lestaurtinib ONO-4474 ONO-5390556 PLX-7486
TrkC	Agonists: BNN-20 DHEA NT-3 Kinase inhibitors: Altiratinib AZD-6918 CE-245677 CH-7057288 DS-6051 Entrectinib GZ-389988 K252a Larotrectinib Lestaurtinib ONO-4474 ONO-5390556 PLX-7486