Protein-coding gene in the species Homo sapiens
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 BExternal IDs OMIM : 190040 MGI : 97528 HomoloGene : 74303 GeneCards : PDGFB 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 patternBgee Human Mouse (ortholog)Top expressed in olfactory bulb 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 parotid 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
Wikidata View/Edit Human View/Edit Mouse
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
References
^ a b c GRCh38: Ensembl release 89: ENSG00000100311 – Ensembl , May 2017
^ a b c GRCm38: Ensembl release 89: ENSMUSG00000000489 – 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 .
^ 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.
^ 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.
^ 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.
^ "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.
Angiopoietin
Kinase inhibitors: Altiratinib
CE-245677
Rebastinib
CNTF EGF (ErbB)
FGF
FGFR1 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
FGFR3 FGFR4 Unsorted
HGF (c-Met) IGF
IGF-1
Kinase inhibitors: BMS-754807
Linsitinib
NVP-ADW742
NVP-AEW541
OSl-906
IGF-2
Antibodies: Dusigitumab
Xentuzumab (against IGF-1 and IGF-2)
Others
Cleavage products/derivatives with unknown target: Glypromate (GPE, (1-3)IGF-1)
Trofinetide
LNGF (p75NTR )
Aptamers: Against NGF: RBM-004
Decoy receptors: LEVI-04 (p75NTR-Fc)
PDGF RET (GFL)
SCF (c-Kit) TGFβ Trk
TrkA
Negative allosteric modulators: VM-902A
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
TrkC
VEGF 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)