Editing Platelet-derived growth factor

{{Short description|Signaling glycoprotein regulating cell proliferation}}
{{Redirect|PDGF|the space hardware|Power Data Grapple Fixture}}
{{Infobox protein family
| Symbol = PDGF
| Name = Platelet-derived growth factor
| image = 1pdg.jpg
| width = 270
| caption = Platelet-derived growth factor BB monomer, Human
| Pfam= PF00341
| InterPro= IPR000072
| SMART=
| Prosite = PDOC00222
| SCOP = 1pdg
| TCDB =
| OPM family=
| OPM protein=
}}

'''Platelet-derived growth factor''' ('''PDGF''') is one among numerous [[growth factor]]s that regulate [[cell (biology)|cell]] growth and [[cell division|division]]. In particular, PDGF plays a significant role in [[Angiogenesis|blood vessel formation]], the growth of blood vessels from already-existing blood vessel tissue, mitogenesis, i.e. proliferation, of mesenchymal cells such as fibroblasts, osteoblasts, tenocytes, vascular smooth muscle cells and mesenchymal stem cells as well as [[chemotaxis]], the directed migration, of mesenchymal cells. Platelet-derived growth factor is a [[protein dimer|dimeric]] [[glycoprotein]] that can be composed of two A subunits (PDGF-AA), two B subunits (PDGF-BB), or one of each (PDGF-AB).

PDGF<ref name="PUB00000590">{{cite journal |vauthors=Hannink M, Donoghue DJ | title = Structure and function of platelet-derived growth factor (PDGF) and related proteins | journal = Biochim. Biophys. Acta | volume = 989 | issue = 1 | pages = 1–10 | year = 1989 | pmid = 2546599 | doi = 10.1016/0304-419x(89)90031-0 }}</ref><ref name="PUB00001228">{{cite journal | author = Heldin CH | title = Structural and functional studies on platelet-derived growth factor | journal = EMBO J. | volume = 11 | issue = 12 | pages = 4251–4259 | year = 1992 | pmid = 1425569 | pmc = 556997 | doi = 10.1002/j.1460-2075.1992.tb05523.x }}</ref> is a potent [[mitogen]] for cells of [[mesenchymal]] origin, including [[fibroblasts]],  [[smooth muscle cells]] and [[glial cells]]. In both mouse and human, the PDGF signalling network consists of five ligands, PDGF-AA through -DD (including -AB), and two receptors, PDGFRalpha and PDGFRbeta. All PDGFs function as secreted, disulphide-linked homodimers, but only PDGFA and B can form functional heterodimers.

Though PDGF is synthesized,<ref>{{cite web|last=Minarcik|first=John|title=Global Path Course: Video|url=http://www.gopathdx.com/?action-model-name-lectures-itemid-69|access-date=2011-06-27|archive-url=https://web.archive.org/web/20180929134650/http://www.gopathdx.com/?action-model-name-lectures-itemid-69|archive-date=2018-09-29|url-status=dead}}</ref> stored (in the alpha granules of [[platelets]]),<ref>{{cite web|title=The Basic Biology of Platelet Growth Factors|date = September 2004|url=http://www.perfusion.com/cgi-bin/absolutenm/templates/articledisplay.asp?articleid=1678&|access-date=2014-05-08}}</ref> and released by platelets upon activation, it is also produced by other cells including smooth muscle cells, activated macrophages, and endothelial cells<ref>{{cite book|last=Kumar|first=Vinay|title=Robbins and Coltran Pathologic Basis of Disease|year=2010|publisher=Elsevier|location=China|isbn=978-1-4160-3121-5|pages=88–89}}</ref>

[[Recombinant DNA|Recombinant]] PDGF is used in medicine to help heal [[Ulcer (dermatology)|chronic ulcers]], to heal ocular surface diseases and in orthopedic surgery and periodontics as an alternative to bone autograft to stimulate bone regeneration and repair.

== Types and classification ==

There are five different [[isoform]]s of PDGF that activate cellular response through two different [[receptor (biochemistry)|receptors]]. Known [[ligand]]s include: PDGF-AA (''[[PDGFA]]''), -BB (''[[PDGFB]]''), -CC (''[[PDGFC]]''), and -DD (''[[PDGFD]]''), and -AB (a ''[[PDGFA]]'' and ''[[PDGFB]]'' [[Protein dimer|heterodimer]]'')''. The ligands interact with the two [[Receptor tyrosine kinase|tyrosine kinase receptor]] monomers, PDGFRα (''[[PDGFRA]]'') and -Rβ (''[[PDGFRB]]'').<ref>{{Cite journal|last1=Fredriksson|first1=Linda|last2=Li|first2=Hong|last3=Eriksson|first3=Ulf|date=August 2004|title=The PDGF family: four gene products form five dimeric isoforms|journal=Cytokine & Growth Factor Reviews|volume=15|issue=4|pages=197–204|doi=10.1016/j.cytogfr.2004.03.007|pmid=15207811}}</ref> The PDGF family also includes a few other members of the family, including the [[VEGF sub-family]].<ref>{{Cite journal|last1=Tischer|first1=Edmund|last2=Gospodarowicz|first2=Denis|last3=Mitchell|first3=Richard|last4=Silva|first4=Maria|last5=Schilling|first5=James|last6=Lau|first6=Kenneth|last7=Crisp|first7=Tracey|last8=Fiddes|first8=John C.|last9=Abraham|first9=Judith A.|date=December 1989|title=Vascular endothelial growth factor: A new member of the platelet-derived growth factor gene family|journal=Biochemical and Biophysical Research Communications|volume=165|issue=3|pages=1198–1206|doi=10.1016/0006-291X(89)92729-0|pmid=2610687}}</ref>

== Mechanisms ==

The [[Receptor (biochemistry)|receptor]] for PDGF, '''PDGFR''' is classified as a [[receptor tyrosine kinase]] (RTK), a type of [[plasma membrane|cell surface]] receptor.  Two types of PDGFRs have been identified: alpha-type and beta-type PDGFRs.<ref>{{cite journal |vauthors=Matsui T, Heidaran M, Miki T, Popescu N, La Rochelle W, Kraus M, Pierce J, Aaronson S | title = Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes | journal = Science | volume = 243 | issue = 4892 | pages = 800–804 | year = 1989 | pmid = 2536956 | doi = 10.1126/science.2536956 | bibcode = 1989Sci...243..800M | url = https://zenodo.org/record/1231010 }}</ref> The alpha type binds to PDGF-AA, PDGF-BB and PDGF-AB, whereas the beta type PDGFR binds with high affinity to PDGF-BB and PDGF-AB.<ref>{{cite journal | vauthors = Heidaran MA, Pierce JH, Yu JC, Lombardi D, Artrip JE, Fleming TP, Thomason A, Aaronson SA | title = Role of alpha beta receptor heterodimer formation in beta platelet-derived growth factor (PDGF) receptor activation by PDGF-AB | journal = J. Biol. Chem. | volume = 266 | issue = 30 | pages = 20232–7 | date = 25 October 1991 | doi = 10.1016/S0021-9258(18)54914-0 | pmid = 1657917 | doi-access = free }}</ref>
PDGF binds to the PDGFR ligand binding pocket located within the second and third immunoglobulin domains.<ref>{{cite journal | vauthors = Heidaran MA, Pierce JH, Jensen RA, Matsui T, Aaronson SA | title = Chimeric alpha- and beta-platelet-derived growth factor (PDGF) receptors define three immunoglobulin-like domains of the alpha-PDGF receptor that determine PDGF-AA binding specificity | journal = J. Biol. Chem. | volume = 265 | issue = 31 | pages = 18741–18744 | date = 5 November 1990 | doi = 10.1016/S0021-9258(17)30572-0 | pmid = 2172231 | doi-access = free }}</ref> Upon activation by PDGF, these receptors dimerise, and are "switched on" by auto-[[phosphorylation]] of several sites on their [[cytosol]]ic domains, which serve to mediate binding of cofactors and subsequently activate [[signal transduction]], for example, through the [[Phosphoinositide 3-kinase|PI3K]] pathway or through [[reactive oxygen species (ROS)]]-mediated activation of the [[STAT3]] pathway.<ref name="pmid24165129">{{cite journal |vauthors=Blazevic T, Schwaiberger AV, Schreiner CE, Schachner D, Schaible AM, Grojer CS, Atanasov AG, Werz O, Dirsch VM, Heiss EH | title = 12/15-Lipoxygenase Contributes to Platelet-derived Growth Factor-induced Activation of Signal Transducer and Activator of Transcription 3 | journal = J. Biol. Chem. | volume = 288 | issue = 49 | pages = 35592–35603 | date = December 2013 | pmid = 24165129 | pmc = 3853304 | doi = 10.1074/jbc.M113.489013 | doi-access = free }}</ref> Downstream effects of this include regulation of [[gene expression]] and the [[cell cycle]].
The role of PI3K has been investigated by several laboratories. Accumulating data suggests that, while this molecule is, in general, part of growth signaling complex, it plays a more profound role in controlling cell migration.<ref>{{cite journal |vauthors=Yu JC, Li W, Wang LM, Uren A, Pierce JH, Heidaran MA | title = Differential requirement of a motif within the carboxyl-terminal domain of alpha-platelet-derived growth factor (alpha PDGF) receptor for PDGF focus forming activity chemotaxis, or growth | journal = J. Biol. Chem. | volume = 270 | issue = 13 | pages = 7033–7036 | year = 1995 | pmid = 7706238 | doi = 10.1074/jbc.270.13.7033 | doi-access = free }}</ref>
The different ligand isoforms have variable affinities for the receptor isoforms, and the receptor isoforms may variably form hetero- or homo- dimers.  This leads to specificity of downstream signaling.  It has been shown that the [[sis oncogene]] is derived from the PDGF B-chain [[gene]]. PDGF-BB is the highest-affinity ligand for the PDGFR-beta; PDGFR-beta is a key marker of hepatic stellate cell activation in the process of [[fibrogenesis]].{{Citation needed|date=April 2007}}

== Function ==
PDGFs are mitogenic during early developmental stages, driving the proliferation of undifferentiated [[mesenchyme]] and some [[progenitor]] populations. During later maturation stages, PDGF signalling has been implicated in tissue remodelling and cellular differentiation, and in inductive events involved in patterning and morphogenesis. In addition to driving mesenchymal proliferation, PDGFs have been shown to direct the migration, differentiation and function of a variety of specialised mesenchymal and migratory cell types, both during development and in the adult animal.<ref>{{cite journal|last1=Ataliotis|first1=P|last2=Symes|first2=K|last3=Chou|first3=MM|last4=Ho|first4=L|last5=Mercola|first5=M|title=PDGF signalling is required for gastrulation of Xenopus laevis.|journal=Development|date=September 1995|volume=121|issue=9|pages=3099–3110|doi=10.1242/dev.121.9.3099|pmid=7555734}}</ref><ref>{{cite journal|last1=Symes|first1=K|last2=Mercola|first2=M|title=Embryonic mesoderm cells spread in response to platelet-derived growth factor and signaling by phosphatidylinositol 3-kinase.|journal=Proceedings of the National Academy of Sciences of the United States of America|date=3 September 1996|volume=93|issue=18|pages=9641–4|pmid=8790383|doi=10.1073/pnas.93.18.9641|pmc=38481|bibcode=1996PNAS...93.9641S|doi-access=free}}</ref><ref name="PUB00014075">{{cite journal |vauthors=Hoch RV, Soriano P | title = Roles of PDGF in animal development | journal = Development | volume = 130 | issue = 20 | pages = 4769–4784 | year = 2003 | pmid = 12952899 | doi = 10.1242/dev.00721 | s2cid = 24124211 | doi-access =  }}</ref> Other growth factors in this family include vascular endothelial growth factors B and C (VEGF-B, VEGF-C)<ref name="PUB00004886">{{cite journal |vauthors=Olofsson B, Pajusola K, Kaipainen A, von Euler G, Joukov V, Saksela O, Orpana A, Pettersson RF, Alitalo K, Eriksson U | title = Vascular endothelial growth factor B, a novel growth factor for endothelial cells | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 6 | pages = 2567–2581 | year = 1996 | pmid = 8637916 | pmc = 39839 | doi = 10.1073/pnas.93.6.2576 | bibcode = 1996PNAS...93.2576O | doi-access = free }}</ref><ref name="PUB00001288">{{cite journal |vauthors=Joukov V, Pajusola K, Kaipainen A, Chilov D, Lahtinen I, Kukk E, Saksela O, Kalkkinen N, Alitalo K | title = A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases | journal = EMBO J. | volume = 15 | issue = 2 | pages = 290–298 | year = 1996 | pmid = 8617204 | pmc = 449944 | doi = 10.1002/j.1460-2075.1996.tb00359.x }}</ref> which are active in angiogenesis and endothelial cell growth, and placenta growth factor (PlGF) which is also active in angiogenesis.<ref name="PUB00004494">{{cite journal |vauthors=Maglione D, Guerriero V, Viglietto G, Ferraro MG, Aprelikova O, Alitalo K, Del Vecchio S, Lei KJ, Chou JY, Persico MG | title = Two alternative mRNAs coding for the angiogenic factor, placenta growth factor (PlGF), are transcribed from a single gene of chromosome 14 | journal = Oncogene | volume = 8 | issue = 4 | pages = 925–931 | year = 1993 | pmid = 7681160 }}</ref>

PDGF plays a role in [[embryo]]nic development, cell proliferation, cell migration, and [[angiogenesis]].<ref>{{cite web |url=http://www.multi-targetedtherapy.com/pdgfSignaling.asp |title=PDGF Pathways |access-date=2007-11-17 |url-status=dead |archive-url=https://web.archive.org/web/20061113131941/http://www.multi-targetedtherapy.com/pdgfSignaling.asp |archive-date=2006-11-13 }}</ref> Over-expression of PDGF has been linked to several [[disease]]s such as [[atherosclerosis]], fibrotic disorders and malignancies.  Synthesis occurs due to external stimuli such as thrombin, low oxygen tension, or other cytokines and growth factors.<ref name="pmid16970222">{{cite journal |vauthors=Alvarez RH, Kantarjian HM, Cortes JE | title = Biology of platelet-derived growth factor and its involvement in disease | journal = Mayo Clin. Proc. | volume = 81 | issue = 9 | pages = 1241–1257 | date = September 2006 | pmid = 16970222 | doi = 10.4065/81.9.1241 }}</ref>

PDGF is a required element in cellular division for [[fibroblasts]], a type of connective tissue cell that is especially prevalent in wound healing.<ref name="pmid16970222"/> In essence, the PDGFs allow a cell to skip the [[cell cycle|G1 checkpoints]] in order to divide.<ref name="pmid15784165">{{cite journal |vauthors=Song G, Ouyang G, Bao S | title = The activation of Akt/PKB signaling pathway and cell survival | journal = J. Cell. Mol. Med. | volume = 9 | issue = 1 | pages = 59–71 | year = 2005 | pmid = 15784165 | doi = 10.1111/j.1582-4934.2005.tb00337.x | pmc = 6741304 }}</ref> It has been shown that in monocytes-macrophages and fibroblasts, exogenously administered PDGF stimulates chemotaxis, proliferation, and gene expression and significantly augmented the influx of inflammatory cells and fibroblasts, accelerating extracellular matrix and collagen formation and thus reducing the time for the healing process to occur.<ref name="pmid2045423">{{cite journal |vauthors=Pierce GF, Mustoe TA, Altrock BW, Deuel TF, Thomason A | title = Role of platelet-derived growth factor in wound healing | journal = J. Cell. Biochem. | volume = 45 | issue = 4 | pages = 319–326 | date = April 1991 | pmid = 2045423 | doi = 10.1002/jcb.240450403 | s2cid = 8539542 }}</ref>

In terms of osteogenic differentiation of mesenchymal stem cells, comparing PDGF to epidermal growth factor (EGF), which is also implicated in stimulating cell growth, proliferation, and differentiation,<ref name="Kratchmarova, I 2005" /> MSCs were shown to have stronger osteogenic differentiation into bone-forming cells when stimulated by epidermal growth factor (EGF) versus PDGF.  However, comparing the signaling pathways between them reveals that the PI3K pathway is exclusively activated by PDGF, with EGF having no effect. Chemically inhibiting the PI3K pathway in PDGF-stimulated cells negates the differential effect between the two growth factors, and actually gives PDGF an edge in osteogenic differentiation.<ref name="Kratchmarova, I 2005">{{cite journal |vauthors=Kratchmarova I, Blagoev B, Haack-Sorensen M, Kassem M, Mann M | title = Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation | journal = Science | volume = 308 | issue = 5727 | pages = 1472–1477 | date = June 2005 | pmid = 15933201 | doi = 10.1126/science.1107627 | bibcode = 2005Sci...308.1472K | s2cid = 10690497 }}</ref> [[Wortmannin]] is a PI3K-specific inhibitor, and treatment of cells with Wortmannin in combination with PDGF resulted in enhanced osteoblast differentiation compared to just PDGF alone, as well as compared to EGF.<ref name="Kratchmarova, I 2005"/> These results indicate that the addition of Wortmannin can significantly increase the response of cells into an osteogenic lineage in the presence of PDGF, and thus might reduce the need for higher concentrations of PDGF or other growth factors, making PDGF a more viable growth factor for osteogenic differentiation than other, more expensive growth factors currently used in the field such as BMP2.<ref>Hayashi, A. The New Standard of Care for Nonunions?.  AAOS Now. 2009.</ref>

PDGF is also known to maintain proliferation of [[oligodendrocyte progenitor cell]]s (OPCs).<ref>{{cite journal |vauthors=[[Ben Barres|Barres BA]], Hart IK, Coles HS, Burne JF, Voyvodic JT, Richardson WD, Raff MC | title = Cell Death and Control of Cell Survival in the Oligodendrocyte Lineage | journal = Cell | volume = 70 | issue = 1 | pages = 31–46 | year = 1992 | pmid = 1623522 | doi = 10.1016/0092-8674(92)90531-G | s2cid = 11529297 }}</ref><ref name="ReferenceA">{{MeshName|Proto-Oncogene+Proteins+c-sis}}</ref> It has also been shown that fibroblast growth factor (FGF) activates a signaling pathway that positively regulates the PDGF receptors in OPCs.<ref name="pmid2171589">{{cite journal |vauthors=McKinnon RD, Matsui T, Dubois-Dalcq M, Aaronson SA | title = FGF modulates the PDGF-driven pathway of oligodendrocyte development | journal = Neuron | volume = 5 | issue = 5 | pages = 603–614 | date = November 1990 | pmid = 2171589 | doi = 10.1016/0896-6273(90)90215-2 | s2cid = 23026544 }}</ref>

== History ==
PDGF was one of the first [[growth factor]]s characterized,<ref>{{cite journal |vauthors=Paul D, Lipton A, Klinger I | title = Serum factor requirements of normal and simian virus 40-transformed 3T3 mouse fibroplasts | journal = Proc Natl Acad Sci U S A | volume = 68 | issue = 3 | pages = 645–652 | year = 1971 | pmid = 5276775 | pmc = 389008 | doi = 10.1073/pnas.68.3.645 | bibcode = 1971PNAS...68..645P | doi-access = free }}</ref> and has led to an understanding of the mechanism of many growth factor [[biochemical signaling|signaling pathways]].{{Citation needed|date=April 2007}}The first engineered dominant negative protein was designed to inhibit PDGF <ref>{{cite journal|last1=Mercola|first1=M|last2=Deininger|first2=P L|last3=Shamah|first3=S M|last4=Porter|first4=J|last5=Wang|first5=C Y|last6=Stiles|first6=C D|title=Dominant-negative mutants of a platelet-derived growth factor gene.|journal=Genes & Development|date=1 December 1990|volume=4|issue=12b|pages=2333–2341|doi=10.1101/gad.4.12b.2333|pmid=2279701|doi-access=free}}</ref>

==Medicine==
[[Recombinant DNA|Recombinant]] PDGF is used to help heal [[Ulcer (dermatology)|chronic ulcers]] and in orthopedic surgery and periodontics to stimulate bone regeneration and repair.<ref name="pmid23432673">{{cite journal | vauthors = Friedlaender GE, Lin S, Solchaga LA, Snel LB, Lynch SE | title = The role of recombinant human platelet-derived growth factor-BB (rhPDGF-BB) in orthopaedic bone repair and regeneration | journal = Current Pharmaceutical Design | volume = 19 | issue = 19 | pages = 3384–3390 | date = 2013 | pmid = 23432673 | doi = 10.2174/1381612811319190005| quote = Demonstration of the safety and efficacy of rhPDGF-BB in the healing of chronic foot ulcers in diabetic patients and regeneration of alveolar (jaw) bone lost due to chronic infection from periodontal disease has resulted in two FDA-approved products based on this molecule }}</ref> PDGF may be beneficial when used by itself or especially in combination with other growth factors to stimulate soft and hard tissue healing (Lynch et al. 1987, 1989, 1991, 1995).

== Research ==

Like many other growth factors that have been linked to disease, PDGF and its receptors have provided a market for [[receptor antagonist]]s to treat disease. Such antagonists include (but are not limited to) specific [[antibody|antibodies]] that target the [[molecule]] of interest, which act only in a neutralizing manner.<ref name="pmid9211881">{{cite journal |vauthors=Shulman T, Sauer FG, Jackman RM, Chang CN, Landolfi NF | title = An antibody reactive with domain 4 of the platelet-derived growth factor beta receptor allows BB binding while inhibiting proliferation by impairing receptor dimerization | journal = J. Biol. Chem. | volume = 272 | issue = 28 | pages = 17400–17404 | date = July 1997 | pmid = 9211881 | doi = 10.1074/jbc.272.28.17400 | doi-access = free }}</ref>

The "c-Sis" [[oncogene]] is derived from PDGF.<ref name="ReferenceA"/><ref>{{cite journal |vauthors=McClintock JT, Chan IJ, Thaker SR, Katial A, Taub FE, Aotaki-Keen AE, Hjelmeland LM | title = Detection of c-sis proto-oncogene transcripts by direct enzyme-labeled cDNA probes and in situ hybridization | journal = In Vitro Cell Dev Biol | volume = 28A | issue = 2 | pages = 102–108 | year = 1992 | pmid = 1537750 | doi = 10.1007/BF02631013 | s2cid = 9958016 }}</ref>

Age related downregulation of the PDGF receptor on islet beta cells has been demonstrated to prevent islet beta cell proliferation in both animal and human cells and its re-expression triggered beta cell proliferation and corrected glucose regulation via insulin secretion.<ref>{{cite web|url=http://www.eurekalert.org/pub_releases/2011-10/jdrf-rmo101211.php |title=Researchers make older beta cells act young again |publisher=Eurekalert.org |date=2011-10-12 |access-date=2013-12-28}}</ref><ref>{{cite web |url=http://med.stanford.edu/ism/2011/october/kim.html |title=New Stanford molecular target for diabetes treatment discovered |publisher=Med.stanford.edu – Stanford University School of Medicine |date=2011-10-12 |access-date=2013-12-28 |url-status=dead |archive-url=https://web.archive.org/web/20131021184626/http://med.stanford.edu/ism/2011/october/kim.html |archive-date=2013-10-21 }}</ref>

A non-viral PDGF "bio patch" can regenerate missing or damaged bone by delivering DNA in a nano-sized particle directly into cells via genes. Repairing bone fractures, fixing craniofacial defects and improving dental implants are among potential uses. The patch employs a collagen platform seeded with particles containing the genes needed for producing bone. In experiments, new bone fully covered skull wounds in test animals and stimulated growth in human bone marrow [[stromal cell]]s.<ref>{{cite journal|url=http://www.kurzweilai.net/bio-patch-can-regrow-bone-for-dental-implants-and-craniofacial-defects |title=Bio patch can regrow bone for dental implants and craniofacial defects |journal=Biomaterials |volume=35 |issue=2 |pages=737–747 |doi=10.1016/j.biomaterials.2013.10.021 |pmid=24161167 |pmc=3855224 |publisher=KurzweilAI |date=2013-11-12 |access-date=2013-12-28|last1=Elangovan |first1=S. |last2=d'Mello |first2=S. R. |last3=Hong |first3=L. |last4=Ross |first4=R. D. |last5=Allamargot |first5=C. |last6=Dawson |first6=D. V. |last7=Stanford |first7=C. M. |last8=Johnson |first8=G. K. |last9=Sumner |first9=D. R. |last10=Salem |first10=A. K. }}</ref><ref>{{cite journal |vauthors=Elangovan S, D'Mello SR, Hong L, Ross RD, Allamargot C, Dawson DV, Stanford CM, Johnson GK, Sumner DR, Salem AK | title = The enhancement of bone regeneration by gene activated matrix encoding for platelet derived growth factor | journal = Biomaterials | volume = 35 | issue = 2 | pages = 737–747 | year = 2014 | pmid = 24161167 | pmc = 3855224 | doi = 10.1016/j.biomaterials.2013.10.021 }}</ref>

The addition of PDGF at specific time‐points has been shown to stabilise vasculature in collagen‐[[glycosaminoglycan]] scaffolds.<ref>{{cite journal |last1=Amaral |first1=Ronaldo Jose Farias Correa |last2=Cavanagh |first2=Brenton |last3=O'Brien |first3=Fergal Joseph |last4=Kearney |first4=Cathal John |title=Platelet-derived growth factor stabilises vascularisation in collagen-glycosaminoglycan scaffolds |journal=Journal of Tissue Engineering and Regenerative Medicine |volume=13 |issue=2 |pages=261–273 |date=16 December 2018 |doi=10.1002/term.2789|pmid=30554484 |s2cid=58767660 |url=https://figshare.com/articles/journal_contribution/10765319 |doi-access=free |url-access=subscription }}</ref>

== Family members ==

Human genes encoding proteins that belong to the platelet-derived growth factor family include:
* [[PDGFA]]; [[PDGFB]]; [[PDGFC]]; [[PDGFD]]
* [[Placental growth factor|PGF]]
* [[Vascular endothelial growth factor|VEGF]]; [[Vascular endothelial growth factor B|VEGFB]]; [[Vascular endothelial growth factor C|VEGFC]]; [[Vascular endothelial growth factor D|VEGFD]]

== See also ==
* [[Platelet-activating factor]]
* [[Platelet-derived growth factor receptor]]
* [[atheroma]] platelet involvement in smooth muscle proliferation
* [[Withaferin A]] potent inhibitor of angiogenesis

== References ==
{{Reflist|35em}}

== External links ==
* {{MeshName|platelet-derived+growth+factor}}

{{Signaling proteins}}
{{Oncogenes}}
{{Growth factor receptor modulators}}

{{DEFAULTSORT:Platelet-Derived Growth Factor}}
[[Category:Growth factors]]
[[Category:Protein domains]]