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Platelet-derived growth factor

January 01, 2023

"PDGF" redirects here. For the space hardware, see Power Data Grapple Fixture.

Platelet-derived growth factor (PDGF) is one among numerous growth factors that regulate cell growth and division. In particular, PDGF plays a significant role in 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 dimeric glycoprotein that can be composed of two A subunits (PDGF-AA), two B subunits (PDGF-BB), or one of each (PDGF-AB).

Platelet-derived growth factor (PDGF)
Platelet-derived growth factor BB monomer, Human
Identifiers
SymbolPDGF
PfamPF00341
InterProIPR000072
PROSITEPDOC00222
SCOP21pdg / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

PDGF[1][2] 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,[3] stored (in the alpha granules of platelets),[4] and released by platelets upon activation, it is also produced by other cells including smooth muscle cells, activated macrophages, and endothelial cells[5]

Recombinant PDGF is used in medicine to help heal chronic ulcers 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 isoforms of PDGF that activate cellular response through two different receptors. Known ligands include: PDGF-AA (PDGFA), -BB (PDGFB), -CC (PDGFC), and -DD (PDGFD), and -AB (a PDGFA and PDGFB heterodimer). The ligands interact with the two tyrosine kinase receptor monomers, PDGFRα (PDGFRA) and -Rβ (PDGFRB).[6] The PDGF family also includes a few other members of the family, including the VEGF sub-family.[7]

Mechanisms

The receptor for PDGF, PDGFR is classified as a receptor tyrosine kinase (RTK), a type of cell surface receptor. Two types of PDGFRs have been identified: alpha-type and beta-type PDGFRs.[8] 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.[9] PDGF binds to the PDGFR ligand binding pocket located within the second and third immunoglobulin domains.[10] Upon activation by PDGF, these receptors dimerise, and are "switched on" by auto-phosphorylation of several sites on their cytosolic domains, which serve to mediate binding of cofactors and subsequently activate signal transduction, for example, through the PI3K pathway or through reactive oxygen species (ROS)-mediated activation of the STAT3 pathway.[11] 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.[12] 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]

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.[13][14][15] Other growth factors in this family include vascular endothelial growth factors B and C (VEGF-B, VEGF-C)[16][17] which are active in angiogenesis and endothelial cell growth, and placenta growth factor (PlGF) which is also active in angiogenesis.[18]

PDGF plays a role in embryonic development, cell proliferation, cell migration, and angiogenesis.[19] Over-expression of PDGF has been linked to several diseases 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.[20]

PDGF is a required element in cellular division for fibroblasts, a type of connective tissue cell that is especially prevalent in wound healing.[20] In essence, the PDGFs allow a cell to skip the G1 checkpoints in order to divide.[21] 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.[22]

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,[23] 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.[23] 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.[23] 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.[24]

PDGF is also known to maintain proliferation of oligodendrocyte progenitor cells (OPCs).[25][26] It has also been shown that fibroblast growth factor (FGF) activates a signaling pathway that positively regulates the PDGF receptors in OPCs.[27]

History

PDGF was one of the first growth factors characterized,[28] and has led to an understanding of the mechanism of many growth factor signaling pathways.[citation needed]The first engineered dominant negative protein was designed to inhibit PDGF [29]

Medicine

Recombinant PDGF is used to help heal chronic ulcers and in orthopedic surgery and periodontics to stimulate bone regeneration and repair.[30] 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 antagonists to treat disease. Such antagonists include (but are not limited to) specific antibodies that target the molecule of interest, which act only in a neutralizing manner.[31]

The "c-Sis" oncogene is derived from PDGF.[26][32]

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.[33][34]

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, it new bone fully covered skull wounds in test animals and stimulated growth in human bone marrow stromal cells.[35][36]

The addition of PDGF at specific time‐points has been shown to stabilise vasculature in collagen‐glycosaminoglycan scaffolds.[37]

Family members

Human genes encoding proteins that belong to the platelet-derived growth factor family include:

See also

References

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  2. ^ Heldin CH (1992). "Structural and functional studies on platelet-derived growth factor". EMBO J. 11 (12): 4251–4259. doi:10.1002/j.1460-2075.1992.tb05523.x. PMC 556997. PMID 1425569.
  3. ^ Minarcik, John. . Archived from the original on 2018-09-29. Retrieved 2011-06-27.
  4. ^ "The Basic Biology of Platelet Growth Factors". September 2004. Retrieved 2014-05-08.
  5. ^ Kumar, Vinay (2010). Robbins and Coltran Pathologic Basis of Disease. China: Elsevier. pp. 88–89. ISBN 978-1-4160-3121-5.
  6. ^ Fredriksson, Linda; Li, Hong; Eriksson, Ulf (August 2004). "The PDGF family: four gene products form five dimeric isoforms". Cytokine & Growth Factor Reviews. 15 (4): 197–204. doi:10.1016/j.cytogfr.2004.03.007. PMID 15207811.
  7. ^ Tischer, Edmund; Gospodarowicz, Denis; Mitchell, Richard; Silva, Maria; Schilling, James; Lau, Kenneth; Crisp, Tracey; Fiddes, John C.; Abraham, Judith A. (December 1989). "Vascular endothelial growth factor: A new member of the platelet-derived growth factor gene family". Biochemical and Biophysical Research Communications. 165 (3): 1198–1206. doi:10.1016/0006-291X(89)92729-0. PMID 2610687.
  8. ^ Matsui T, Heidaran M, Miki T, Popescu N, La Rochelle W, Kraus M, Pierce J, Aaronson S (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.
  9. ^ Heidaran MA, Pierce JH, Yu JC, Lombardi D, Artrip JE, Fleming TP, Thomason A, Aaronson SA (25 October 1991). "Role of alpha beta receptor heterodimer formation in beta platelet-derived growth factor (PDGF) receptor activation by PDGF-AB". J. Biol. Chem. 266 (30): 20232–7. doi:10.1016/S0021-9258(18)54914-0. PMID 1657917.
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  16. ^ Olofsson B, Pajusola K, Kaipainen A, von Euler G, Joukov V, Saksela O, Orpana A, Pettersson RF, Alitalo K, Eriksson U (1996). "Vascular endothelial growth factor B, a novel growth factor for endothelial cells". Proc. Natl. Acad. Sci. U.S.A. 93 (6): 2567–2581. Bibcode:1996PNAS...93.2576O. doi:10.1073/pnas.93.6.2576. PMC 39839. PMID 8637916.
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  19. ^ . Archived from the original on 2006-11-13. Retrieved 2007-11-17.
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  21. ^ Song G, Ouyang G, Bao S (2005). "The activation of Akt/PKB signaling pathway and cell survival". J. Cell. Mol. Med. 9 (1): 59–71. doi:10.1111/j.1582-4934.2005.tb00337.x. PMC 6741304. PMID 15784165.
  22. ^ Pierce GF, Mustoe TA, Altrock BW, Deuel TF, Thomason A (April 1991). "Role of platelet-derived growth factor in wound healing". J. Cell. Biochem. 45 (4): 319–26. doi:10.1002/jcb.240450403. PMID 2045423. S2CID 8539542.
  23. ^ a b c Kratchmarova I, Blagoev B, Haack-Sorensen M, Kassem M, Mann M (June 2005). "Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation". Science. 308 (5727): 1472–7. Bibcode:2005Sci...308.1472K. doi:10.1126/science.1107627. PMID 15933201. S2CID 10690497.
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  26. ^ a b Proto-Oncogene+Proteins+c-sis at the US National Library of Medicine Medical Subject Headings (MeSH)
  27. ^ McKinnon RD, Matsui T, Dubois-Dalcq M, Aaronson SA (November 1990). "FGF modulates the PDGF-driven pathway of oligodendrocyte development". Neuron. 5 (5): 603–14. doi:10.1016/0896-6273(90)90215-2. PMID 2171589. S2CID 23026544.
  28. ^ Paul D, Lipton A, Klinger I (1971). "Serum factor requirements of normal and simian virus 40-transformed 3T3 mouse fibroplasts". Proc Natl Acad Sci U S A. 68 (3): 645–52. Bibcode:1971PNAS...68..645P. doi:10.1073/pnas.68.3.645. PMC 389008. PMID 5276775.
  29. ^ Mercola, M; Deininger, P L; Shamah, S M; Porter, J; Wang, C Y; Stiles, C D (1 December 1990). "Dominant-negative mutants of a platelet-derived growth factor gene". Genes & Development. 4 (12b): 2333–2341. doi:10.1101/gad.4.12b.2333. PMID 2279701.
  30. ^ Friedlaender GE, Lin S, Solchaga LA, Snel LB, Lynch SE (2013). "The role of recombinant human platelet-derived growth factor-BB (rhPDGF-BB) in orthopaedic bone repair and regeneration". Current Pharmaceutical Design. 19 (19): 3384–90. doi:10.2174/1381612811319190005. PMID 23432673. 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
  31. ^ Shulman T, Sauer FG, Jackman RM, Chang CN, Landolfi NF (July 1997). "An antibody reactive with domain 4 of the platelet-derived growth factor beta receptor allows BB binding while inhibiting proliferation by impairing receptor dimerization". J. Biol. Chem. 272 (28): 17400–4. doi:10.1074/jbc.272.28.17400. PMID 9211881.
  32. ^ McClintock JT, Chan IJ, Thaker SR, Katial A, Taub FE, Aotaki-Keen AE, Hjelmeland LM (1992). "Detection of c-sis proto-oncogene transcripts by direct enzyme-labeled cDNA probes and in situ hybridization". In Vitro Cell Dev Biol. 28A (2): 102–8. doi:10.1007/BF02631013. PMID 1537750. S2CID 9958016.
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  35. ^ Elangovan, S.; d'Mello, S. R.; Hong, L.; Ross, R. D.; Allamargot, C.; Dawson, D. V.; Stanford, C. M.; Johnson, G. K.; Sumner, D. R.; Salem, A. K. (2013-11-12). "Bio patch can regrow bone for dental implants and craniofacial defects". Biomaterials. KurzweilAI. 35 (2): 737–47. doi:10.1016/j.biomaterials.2013.10.021. PMC 3855224. PMID 24161167. Retrieved 2013-12-28.
  36. ^ Elangovan S, D'Mello SR, Hong L, Ross RD, Allamargot C, Dawson DV, Stanford CM, Johnson GK, Sumner DR, Salem AK (2014). "The enhancement of bone regeneration by gene activated matrix encoding for platelet derived growth factor". Biomaterials. 35 (2): 737–747. doi:10.1016/j.biomaterials.2013.10.021. PMC 3855224. PMID 24161167.
  37. ^ Amaral, Ronaldo Jose Farias Correa; Cavanagh, Brenton; O'Brien, Fergal Joseph; Kearney, Cathal John (16 December 2018). "Platelet‐derived growth factor stabilises vascularisation in collagen‐glycosaminoglycan scaffolds". Journal of Tissue Engineering and Regenerative Medicine. 13 (2): 261–273. doi:10.1002/term.2789. PMID 30554484. S2CID 58767660.

External links

January 01, 2023
platelet, derived, growth, factor, pdgf, redirects, here, space, hardware, power, data, grapple, fixture, pdgf, among, numerous, growth, factors, that, regulate, cell, growth, division, particular, pdgf, plays, significant, role, blood, vessel, formation, grow. PDGF redirects here For the space hardware see Power Data Grapple Fixture Platelet derived growth factor PDGF is one among numerous growth factors that regulate cell growth and division In particular PDGF plays a significant role in 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 dimeric glycoprotein that can be composed of two A subunits PDGF AA two B subunits PDGF BB or one of each PDGF AB Platelet derived growth factor PDGF Platelet derived growth factor BB monomer HumanIdentifiersSymbolPDGFPfamPF00341InterProIPR000072PROSITEPDOC00222SCOP21pdg SCOPe SUPFAMAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryPDGF 1 2 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 3 stored in the alpha granules of platelets 4 and released by platelets upon activation it is also produced by other cells including smooth muscle cells activated macrophages and endothelial cells 5 Recombinant PDGF is used in medicine to help heal chronic ulcers and in orthopedic surgery and periodontics as an alternative to bone autograft to stimulate bone regeneration and repair Contents 1 Types and classification 2 Mechanisms 3 Function 4 History 5 Medicine 6 Research 7 Family members 8 See also 9 References 10 External linksTypes and classification EditThere are five different isoforms of PDGF that activate cellular response through two different receptors Known ligands include PDGF AA PDGFA BB PDGFB CC PDGFC and DD PDGFD and AB a PDGFA and PDGFB heterodimer The ligands interact with the two tyrosine kinase receptor monomers PDGFRa PDGFRA and Rb PDGFRB 6 The PDGF family also includes a few other members of the family including the VEGF sub family 7 Mechanisms EditThe receptor for PDGF PDGFR is classified as a receptor tyrosine kinase RTK a type of cell surface receptor Two types of PDGFRs have been identified alpha type and beta type PDGFRs 8 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 9 PDGF binds to the PDGFR ligand binding pocket located within the second and third immunoglobulin domains 10 Upon activation by PDGF these receptors dimerise and are switched on by auto phosphorylation of several sites on their cytosolic domains which serve to mediate binding of cofactors and subsequently activate signal transduction for example through the PI3K pathway or through reactive oxygen species ROS mediated activation of the STAT3 pathway 11 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 12 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 Function EditPDGFs 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 13 14 15 Other growth factors in this family include vascular endothelial growth factors B and C VEGF B VEGF C 16 17 which are active in angiogenesis and endothelial cell growth and placenta growth factor PlGF which is also active in angiogenesis 18 PDGF plays a role in embryonic development cell proliferation cell migration and angiogenesis 19 Over expression of PDGF has been linked to several diseases 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 20 PDGF is a required element in cellular division for fibroblasts a type of connective tissue cell that is especially prevalent in wound healing 20 In essence the PDGFs allow a cell to skip the G1 checkpoints in order to divide 21 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 22 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 23 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 23 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 23 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 24 PDGF is also known to maintain proliferation of oligodendrocyte progenitor cells OPCs 25 26 It has also been shown that fibroblast growth factor FGF activates a signaling pathway that positively regulates the PDGF receptors in OPCs 27 History EditPDGF was one of the first growth factors characterized 28 and has led to an understanding of the mechanism of many growth factor signaling pathways citation needed The first engineered dominant negative protein was designed to inhibit PDGF 29 Medicine EditRecombinant PDGF is used to help heal chronic ulcers and in orthopedic surgery and periodontics to stimulate bone regeneration and repair 30 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 EditLike many other growth factors that have been linked to disease PDGF and its receptors have provided a market for receptor antagonists to treat disease Such antagonists include but are not limited to specific antibodies that target the molecule of interest which act only in a neutralizing manner 31 The c Sis oncogene is derived from PDGF 26 32 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 33 34 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 it new bone fully covered skull wounds in test animals and stimulated growth in human bone marrow stromal cells 35 36 The addition of PDGF at specific time points has been shown to stabilise vasculature in collagen glycosaminoglycan scaffolds 37 Family members EditHuman genes encoding proteins that belong to the platelet derived growth factor family include PDGFA PDGFB PDGFC PDGFD PGF VEGF VEGFB VEGFC VEGFDSee also EditPlatelet activating factor Platelet derived growth factor receptor atheroma platelet involvement in smooth muscle proliferation Withaferin A potent inhibitor of angiogenesisReferences Edit Hannink M Donoghue DJ 1989 Structure and function of platelet derived growth factor PDGF and related proteins Biochim Biophys Acta 989 1 1 10 doi 10 1016 0304 419x 89 90031 0 PMID 2546599 Heldin CH 1992 Structural and functional studies on platelet derived growth factor EMBO J 11 12 4251 4259 doi 10 1002 j 1460 2075 1992 tb05523 x PMC 556997 PMID 1425569 Minarcik John Global Path Course Video Archived from the original on 2018 09 29 Retrieved 2011 06 27 The Basic Biology of Platelet Growth Factors September 2004 Retrieved 2014 05 08 Kumar Vinay 2010 Robbins and Coltran Pathologic Basis of Disease China Elsevier pp 88 89 ISBN 978 1 4160 3121 5 Fredriksson Linda Li Hong Eriksson Ulf August 2004 The PDGF family four gene products form five dimeric isoforms Cytokine amp Growth Factor Reviews 15 4 197 204 doi 10 1016 j cytogfr 2004 03 007 PMID 15207811 Tischer Edmund Gospodarowicz Denis Mitchell Richard Silva Maria Schilling James Lau Kenneth Crisp Tracey Fiddes John C Abraham Judith A December 1989 Vascular endothelial growth factor A new member of the platelet derived growth factor gene family Biochemical and Biophysical Research Communications 165 3 1198 1206 doi 10 1016 0006 291X 89 92729 0 PMID 2610687 Matsui T Heidaran M Miki T Popescu N La Rochelle W Kraus M Pierce J Aaronson S 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 Heidaran MA Pierce JH Yu JC Lombardi D Artrip JE Fleming TP Thomason A Aaronson SA 25 October 1991 Role of alpha beta receptor heterodimer formation in beta platelet derived growth factor PDGF receptor activation by PDGF AB J Biol Chem 266 30 20232 7 doi 10 1016 S0021 9258 18 54914 0 PMID 1657917 Heidaran MA Pierce JH Jensen RA Matsui T Aaronson SA 5 November 1990 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 J Biol Chem 265 31 18741 4 doi 10 1016 S0021 9258 17 30572 0 PMID 2172231 Blazevic T Schwaiberger AV Schreiner CE Schachner D Schaible AM Grojer CS Atanasov AG Werz O Dirsch VM Heiss EH December 2013 12 15 Lipoxygenase Contributes to Platelet derived Growth Factor induced Activation of Signal Transducer and Activator of Transcription 3 J Biol Chem 288 49 35592 603 doi 10 1074 jbc M113 489013 PMC 3853304 PMID 24165129 Yu JC Li W Wang LM Uren A Pierce JH Heidaran MA 1995 Differential requirement of a motif within the carboxyl terminal domain of alpha platelet derived growth factor alpha PDGF receptor for PDGF 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stanford edu 2011 10 12 Archived from the original on 2013 10 21 Retrieved 2013 12 28 Elangovan S d Mello S R Hong L Ross R D Allamargot C Dawson D V Stanford C M Johnson G K Sumner D R Salem A K 2013 11 12 Bio patch can regrow bone for dental implants and craniofacial defects Biomaterials KurzweilAI 35 2 737 47 doi 10 1016 j biomaterials 2013 10 021 PMC 3855224 PMID 24161167 Retrieved 2013 12 28 Elangovan S D Mello SR Hong L Ross RD Allamargot C Dawson DV Stanford CM Johnson GK Sumner DR Salem AK 2014 The enhancement of bone regeneration by gene activated matrix encoding for platelet derived growth factor Biomaterials 35 2 737 747 doi 10 1016 j biomaterials 2013 10 021 PMC 3855224 PMID 24161167 Amaral Ronaldo Jose Farias Correa Cavanagh Brenton O Brien Fergal Joseph Kearney Cathal John 16 December 2018 Platelet derived growth factor stabilises vascularisation in collagen glycosaminoglycan scaffolds Journal of Tissue Engineering and Regenerative Medicine 13 2 261 273 doi 10 1002 term 2789 PMID 30554484 S2CID 58767660 External links Editplatelet derived growth factor at the US National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Platelet derived growth factor amp oldid 1129986515, wikipedia, wiki, book, books, library,

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