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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; OMA:PDGFA - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7p22.3 Start 497,258 bp End 520,296 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5 G2|5 77.65 cM Start 138,961,769 bp End 138,983,125 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in buccal mucosa cell ascending aorta Descending thoracic aorta right coronary artery body of pancreas popliteal artery tibial arteries left coronary artery optic nerve C1 segment Top expressed in Ileal epithelium choroid plexus of fourth ventricle calvaria choroidal fissure entorhinal cortex tunica media of zone of aorta iris retinal pigment epithelium perirhinal cortex CA3 field 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
Wikidata
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Platelet-derived growth factor subunit A is a protein that in humans is encoded by the PDGFA gene.

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.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000197461 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000025856 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "Entrez Gene: PDGFA platelet-derived growth factor alpha polypeptide".

Further reading

• 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.

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