PDGFB

PDGFB
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1PDG, 3MJG, 4HQU, 4HQX, 4QCI
Identifiers
Aliases	PDGFB, IBGC5, PDGF-2, PDGF2, SIS, SSV, c-sis, platelet derived growth factor subunit B
External IDs	OMIM: 190040; MGI: 97528; HomoloGene: 74303; GeneCards: PDGFB; OMA:PDGFB - orthologs
Gene location (Human) Chr. Chromosome 22 (human)[1] Band 22q13.1 Start 39,223,359 bp[1] End 39,244,982 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15 E1|15 37.85 cM Start 79,995,874 bp[2] End 80,014,977 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in olfactory bulb apex of heart pancreatic ductal cell right lung vena cava subcutaneous adipose tissue triceps brachii muscle left ventricle upper lobe of left lung right lobe of thyroid gland Top expressed in triceps brachii muscle left lung right lung digastric muscle left lung lobe vastus lateralis muscle sternocleidomastoid muscle ankle temporal muscle right ventricle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein homodimerization activity protein heterodimerization activity chemoattractant activity platelet-derived growth factor receptor binding platelet-derived growth factor binding superoxide-generating NADPH oxidase activator activity growth factor activity identical protein binding collagen binding protein binding phosphatidylinositol-4,5-bisphosphate 3-kinase activity Cellular component platelet alpha granule lumen cytoplasm extracellular region Golgi membrane basolateral plasma membrane cell surface endoplasmic reticulum lumen membrane extracellular matrix extracellular space Golgi lumen collagen-containing extracellular matrix Biological process activation of protein kinase B activity positive regulation of DNA biosynthetic process positive regulation of chemotaxis cellular response to growth factor stimulus positive regulation of protein tyrosine kinase activity peptidyl-tyrosine phosphorylation positive regulation of cell division heart development positive regulation of glomerular filtration positive regulation of mitotic nuclear division positive regulation of MAP kinase activity positive regulation of metanephric mesenchymal cell migration positive regulation of hyaluronan biosynthetic process MAPK cascade protein phosphorylation positive regulation of glomerular mesangial cell proliferation cellular response to mycophenolic acid positive regulation of fibroblast proliferation activation of protein kinase activity multicellular organism development positive regulation of protein autophosphorylation positive regulation of reactive oxygen species metabolic process reactive oxygen species metabolic process negative regulation of transcription, DNA-templated protein kinase C signaling metanephric glomerular mesangial cell development negative regulation of phosphatidylinositol biosynthetic process response to wounding positive regulation of phosphatidylinositol 3-kinase activity cell chemotaxis positive regulation of ERK1 and ERK2 cascade platelet degranulation positive regulation of cell population proliferation positive regulation of DNA replication positive regulation of gene expression embryonic placenta development paracrine signaling monocyte chemotaxis positive regulation of endothelial cell proliferation positive regulation of phosphatidylinositol 3-kinase signaling positive regulation of calcium ion import positive regulation of transcription, DNA-templated peptidyl-serine phosphorylation positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway positive regulation of blood vessel endothelial cell migration hemopoiesis positive regulation of cell migration positive regulation of peptidyl-tyrosine phosphorylation extracellular matrix organization negative regulation of protein binding positive regulation of MAPK cascade positive regulation of cyclin-dependent protein serine/threonine kinase activity negative regulation of platelet activation phosphatidylinositol phosphate biosynthetic process positive regulation of vascular associated smooth muscle cell migration positive chemotaxis negative regulation of vascular associated smooth muscle cell differentiation interleukin-18-mediated signaling pathway positive regulation of pri-miRNA transcription by RNA polymerase II negative regulation of pri-miRNA transcription by RNA polymerase II negative regulation of gene expression positive regulation of smooth muscle cell migration positive regulation of smooth muscle cell proliferation positive regulation of vascular associated smooth muscle cell dedifferentiation platelet-derived growth factor receptor signaling pathway positive regulation of vascular associated smooth muscle cell proliferation negative regulation of platelet-derived growth factor receptor-beta signaling pathway regulation of signaling receptor activity positive regulation of protein kinase B signaling Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5155 18591 Ensembl ENSG00000100311 ENSMUSG00000000489 UniProt P01127 P31240 RefSeq (mRNA) NM_033016 NM_002608 NM_011057 RefSeq (protein) NP_002599 NP_148937 NP_035187 Location (UCSC) Chr 22: 39.22 – 39.24 Mb Chr 15: 80 – 80.01 Mb PubMed search [3] [4]
Wikidata
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Platelet-derived growth factor subunit B is a protein that in humans is encoded by the PDGFB gene.^[5][6]

Function

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 (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha (PDGFA) polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds.

Clinical significance

Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 17, at sites where the PDGFB and COL1A1 genes are respectively located or, alternatively, an abnormal small supernumerary ring chromosome merge these two genes to form a COL1A-PDGFB fusion gene. This fusion gene greatly overproduces PDGFB and is considered responsible for causing the development and/or progression of three closely related fibroblastic and myofibroblastic tumors of the skin: giant cell fibroblastoma, dermatofibrosarcoma protuberans, and dermatofibrosarcoma protuberans, sarcomatous.^[7]

Two splice variants have been identified for the PDGFB gene.^[8]

See also

• Platelet-derived growth factor

References

1. GRCh38: Ensembl release 89: ENSG00000100311 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000000489 – 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. Ratner L, Josephs SF, Jarrett R, Reitz MS, Wong-Staal F (Sep 1985). "Nucleotide sequence of transforming human c-sis cDNA clones with homology to platelet-derived growth factor". Nucleic Acids Res. 13 (14): 5007–18. doi:10.1093/nar/13.14.5007. PMC 321845. PMID 2991848.
6. Clements JM, Bawden LJ, Bloxidge RE, Catlin G, Cook AL, Craig S, Drummond AH, Edwards RM, Fallon A, Green DR (Jan 1992). "Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor binding and activation". EMBO J. 10 (13): 4113–20. doi:10.1002/j.1460-2075.1991.tb04988.x. PMC 453161. PMID 1661670.
7. Baranov E, Hornick JL (March 2020). "Soft Tissue Special Issue: Fibroblastic and Myofibroblastic Neoplasms of the Head and Neck". Head and Neck Pathology. 14 (1): 43–58. doi:10.1007/s12105-019-01104-3. PMC 7021862. PMID 31950474.
8. "Entrez Gene: PDGFB platelet-derived growth factor beta polypeptide (simian sarcoma viral (v-sis) oncogene homolog)".

Further reading

• Kurup S, Abramsson A, Li JP, Lindahl U, Kjellen L, Betsholtz C, Gerhardt H, Spillmann D (2006). "Heparan sulphate requirement in platelet-derived growth factor B-mediated pericyte recruitment". Biochem. Soc. Trans. 34 (Pt 3): 454–5. doi:10.1042/BST0340454. PMID 16709185.