Wikipedia

PDGFA

PDGFA (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[34][35]

PDGFA
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген PDGFA[d][1]
Молекулярная функция collagen binding[d][2], гомодимеризация белка[d][3][4], platelet-derived growth factor receptor binding[d][5][6][7], связывание с белками плазмы[d][8][9], platelet-derived growth factor binding[d][10], protein heterodimerization activity[d][10], growth factor activity[d][11][11][12], phosphatidylinositol-4,5-bisphosphate 3-kinase activity[d][13], связывание похожих белков[d][14] һәм platelet-derived growth factor receptor binding[d][15][3][16][…]
Күзәнәк компоненты endoplasmic reticulum lumen[d][11], мембрана[d][11], Golgi membrane[d][11], внеклеточная область[d][11][11], Микроворсинка[d][11], поверхность клетки[d][17][3][18], platelet alpha granule lumen[d][11], внеклеточное пространство[d][19], Люмен аппарата Гольджи[d][11] һәм внеклеточное пространство[d][4][20]
Биологический процесс hair follicle development[d][11], embryonic lung development[d][11], positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway[d][21], negative chemotaxis[d][22], regulation of actin cytoskeleton organization[d][23], positive regulation of MAP kinase activity[d][24], regulation of branching involved in salivary gland morphogenesis by epithelial-mesenchymal signaling[d][11], positive regulation of cell migration[d][24][25], positive regulation of fibroblast proliferation[d][26][16], передача сигнала между клетками[d][27], platelet degranulation[d][11], extracellular matrix organization[d][11], regulation of DNA biosynthetic process[d][21][28], cell activation[d][23], MAPK cascade[d][11], negative regulation of platelet activation[d][17], multicellular organism development[d][11], positive regulation of mesenchymal cell proliferation[d][11], response to wounding[d][17], cell projection assembly[d][11], negative regulation of phosphatidylinositol biosynthetic process[d][17], Ангиогенез[d][11], positive regulation of protein autophosphorylation[d][29], positive regulation of ERK1 and ERK2 cascade[d][24], regulation of smooth muscle cell migration[d][22], морфогенез органа животных[d][11], positive regulation of phosphatidylinositol 3-kinase signaling[d][24], platelet-derived growth factor receptor signaling pathway[d][6][7][5], развитие лёгочной альвеолы[d][11], positive regulation of cell division[d][11], actin cytoskeleton organization[d][11], positive regulation of MAPK cascade[d][28], развитие кожи[d][11], regulation of glomerular mesangial cell proliferation[d][28], regulation of peptidyl-tyrosine phosphorylation[d][11], Заживление ран[d][23], phosphatidylinositol phosphate biosynthetic process[d][13], позитивная регуляция пролиферации клеток[d][30][6][31][…], regulation of signaling receptor activity[d][11], позитивная регуляция сигналов от протеинкиназы В[d][11][21], позитивная регуляция пролиферации клеток[d][32][26][10][…], positive regulation of phosphatidylinositol 3-kinase signaling[d][28][20], positive regulation of cell migration[d][28][33][20], positive regulation of protein autophosphorylation[d][12][20], positive regulation of MAP kinase activity[d][28][20], platelet-derived growth factor receptor signaling pathway[d][3][15][16][…] һәм positive regulation of ERK1 and ERK2 cascade[d][28][20]

Искәрмәләр үзгәртү

  1. ↑ 1,0 1,1 UniProt
  2. ↑ R Somasundaram, D Schuppan Type I, II, III, IV, V, and VI collagens serve as extracellular ligands for the isoforms of platelet-derived growth factor (AA, BB, and AB) // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1996. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.271.43.26884 — PMID:8900172
  3. ↑ 3,0 3,1 3,2 3,3 Williams L. T., Escobedo J. A. A common PDGF receptor is activated by homodimeric A and B forms of PDGF // Science / H. Thorp — Northern America: AAAS, 1988. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.2836953 — PMID:2836953
  4. ↑ 4,0 4,1 C Betsholtz, B Westermark cDNA sequence and chromosomal localization of human platelet-derived growth factor A-chain and its expression in tumour cell lines // Nature / M. Skipper — NPG, Springer Science+Business Media, 1986. — ISSN 1476-4687; 0028-0836 — doi:10.1038/320695A0 — PMID:3754619
  5. ↑ 5,0 5,1 T Matsui, M Heidaran, T Miki et al. Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes // Science / H. Thorp — Northern America: AAAS, 1989. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.2536956 — PMID:2536956
  6. ↑ 6,0 6,1 6,2 Williams L. T., Escobedo J. A. A common PDGF receptor is activated by homodimeric A and B forms of PDGF // Science / H. Thorp — Northern America: AAAS, 1988. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.2836953 — PMID:2836953
  7. ↑ 7,0 7,1 Womer R. B., K Frick, Mitchell C. D. et al. PDGF induces c-myc mRNA expression in MG-63 human osteosarcoma cells but does not stimulate cell replication // J. Cell. Physio. — Wiley, 1987. — ISSN 0021-9541; 1097-4652 — doi:10.1002/JCP.1041320109 — PMID:2439522
  8. ↑ Chen T., Lin K., Chen C. et al. Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network // J. Proteome Res. / J. Yates — ACS, 2014. — ISSN 1535-3893; 1535-3907 — doi:10.1021/PR5002737 — PMID:25241761
  9. ↑ LJ F., AJ S., JE T. et al. Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to alpha and beta PDGF receptor // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1993. — 7 p. — ISSN 0021-9258; 1083-351X; 1067-8816 — PMID:7679113
  10. ↑ 10,0 10,1 10,2 B Westermark Platelet-derived growth factor: identification of constituent polypeptide chains // Biochem. Biophys. Res. Commun. — Academic Press, Elsevier BV, 1982. — ISSN 0006-291X; 1090-2104 — doi:10.1016/0006-291X(82)91941-6 — PMID:7073684
  11. ↑ 11,00 11,01 11,02 11,03 11,04 11,05 11,06 11,07 11,08 11,09 11,10 11,11 11,12 11,13 11,14 11,15 11,16 11,17 11,18 11,19 11,20 11,21 11,22 11,23 11,24 11,25 11,26 11,27 GOA
  12. ↑ 12,0 12,1 Hotta K. Adipocyte-derived plasma protein adiponectin acts as a platelet-derived growth factor-BB-binding protein and regulates growth factor-induced common postreceptor signal in vascular smooth muscle cell // Circulation — Lippincott Williams & Wilkins, 2002. — ISSN 0009-7322; 1524-4539 — doi:10.1161/01.CIR.0000018622.84402.FF — PMID:12070119
  13. ↑ 13,0 13,1 GOA
  14. ↑ Shim A. H., Liu H., Focia P. J. et al. Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2010. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1000806107 — PMID:20534510
  15. ↑ 15,0 15,1 T Matsui, M Heidaran, T Miki et al. Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes // Science / H. Thorp — Northern America: AAAS, 1989. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.2536956 — PMID:2536956
  16. ↑ 16,0 16,1 16,2 Womer R. B., K Frick, Mitchell C. D. et al. PDGF induces c-myc mRNA expression in MG-63 human osteosarcoma cells but does not stimulate cell replication // J. Cell. Physio. — Wiley, 1987. — ISSN 0021-9541; 1097-4652 — doi:10.1002/JCP.1041320109 — PMID:2439522
  17. ↑ 17,0 17,1 17,2 17,3 Bryckaert M. C., F Rendu, G Tobelem et al. Collagen-induced binding to human platelets of platelet-derived growth factor leading to inhibition of P43 and P20 phosphorylation // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1989. — ISSN 0021-9258; 1083-351X; 1067-8816 — PMID:2538439
  18. ↑ B Westermark Platelet-derived growth factor: purification and partial characterization // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1979. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.76.8.3722 — PMID:291037
  19. ↑ C Betsholtz, B Westermark cDNA sequence and chromosomal localization of human platelet-derived growth factor A-chain and its expression in tumour cell lines // Nature / M. Skipper — NPG, Springer Science+Business Media, 1986. — ISSN 1476-4687; 0028-0836 — doi:10.1038/320695A0 — PMID:3754619
  20. ↑ 20,0 20,1 20,2 20,3 20,4 20,5 Livstone M. S., Thomas P. D., Lewis S. E. et al. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium // Brief. Bioinform. — OUP, 2011. — ISSN 1467-5463; 1477-4054 — doi:10.1093/BIB/BBR042 — PMID:21873635
  21. ↑ 21,0 21,1 21,2 Wagner B., Gorin Y. PDGF receptor-{beta} modulates metanephric mesenchyme chemotaxis induced by PDGF AA // American journal of physiology: Renal Physiology — 2008. — ISSN 1931-857X; 1522-1466; 0363-6127 — doi:10.1152/AJPRENAL.90368.2008 — PMID:19019919
  22. ↑ 22,0 22,1 Clunn G. F., Refson J. S., Lymn J. S. et al. Platelet-derived growth factor beta-receptors can both promote and inhibit chemotaxis in human vascular smooth muscle cells // Arteriosclerosis, Thrombosis, and Vascular Biology — Lippincott Williams & Wilkins, 1997. — ISSN 1079-5642; 1524-4636 — doi:10.1161/01.ATV.17.11.2622 — PMID:9409235
  23. ↑ 23,0 23,1 23,2 B Westermark Mechanism of action and in vivo role of platelet-derived growth factor // Physiological Reviews / D. Brown — USA: American Physiological Society, 1999. — 680 p. — ISSN 0031-9333; 1522-1210 — doi:10.1152/PHYSREV.1999.79.4.1283 — PMID:10508235
  24. ↑ 24,0 24,1 24,2 24,3 Ricono J. M., Arar M., Choudhury G. G. et al. Effect of platelet-derived growth factor isoforms in rat metanephric mesenchymal cells // American journal of physiology: Renal Physiology — 2002. — ISSN 1931-857X; 1522-1466; 0363-6127 — doi:10.1152/AJPRENAL.0323.2000 — PMID:11788434
  25. ↑ Ball S. G., Shuttleworth C. A., Kielty C. M. Vascular endothelial growth factor can signal through platelet-derived growth factor receptors // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2007. — 12 p. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200608093 — PMID:17470632
  26. ↑ 26,0 26,1 H Boström, M Hellström, C Betsholtz PDGF-C is a new protease-activated ligand for the PDGF alpha-receptor // Nat. Cell Biol. — NPG, 2000. — ISSN 1465-7392; 1476-4679 — doi:10.1038/35010579 — PMID:10806482
  27. ↑ C Betsholtz, B Westermark Comparison of biological properties and transforming potential of human PDGF-A and PDGF-B chains // Science / H. Thorp — Northern America: AAAS, 1988. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.2842868 — PMID:2842868
  28. ↑ 28,0 28,1 28,2 28,3 28,4 28,5 28,6 Ricono J. M., Arar M., Choudhury G. G. et al. Effect of platelet-derived growth factor isoforms in rat metanephric mesenchymal cells // American journal of physiology: Renal Physiology — 2002. — ISSN 1931-857X; 1522-1466; 0363-6127 — doi:10.1152/AJPRENAL.0323.2000 — PMID:11788434
  29. ↑ Hotta K. Adipocyte-derived plasma protein adiponectin acts as a platelet-derived growth factor-BB-binding protein and regulates growth factor-induced common postreceptor signal in vascular smooth muscle cell // Circulation — Lippincott Williams & Wilkins, 2002. — ISSN 0009-7322; 1524-4539 — doi:10.1161/01.CIR.0000018622.84402.FF — PMID:12070119
  30. ↑ Alitalo K., Tammela T., Homman-Ludiye J. et al. VEGF-C is a trophic factor for neural progenitors in the vertebrate embryonic brain // Nat. Neurosci. — NPG, 2006. — ISSN 1097-6256; 1546-1726 — doi:10.1038/NN1646 — PMID:16462734
  31. ↑ H Boström, M Hellström, C Betsholtz PDGF-C is a new protease-activated ligand for the PDGF alpha-receptor // Nat. Cell Biol. — NPG, 2000. — ISSN 1465-7392; 1476-4679 — doi:10.1038/35010579 — PMID:10806482
  32. ↑ Alitalo K., Tammela T., Homman-Ludiye J. et al. VEGF-C is a trophic factor for neural progenitors in the vertebrate embryonic brain // Nat. Neurosci. — NPG, 2006. — ISSN 1097-6256; 1546-1726 — doi:10.1038/NN1646 — PMID:16462734
  33. ↑ Ball S. G., Shuttleworth C. A., Kielty C. M. Vascular endothelial growth factor can signal through platelet-derived growth factor receptors // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2007. — 12 p. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200608093 — PMID:17470632
  34. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  35. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар үзгәртү

  • Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
  • Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)


Бу — аксым турында мәкалә төпчеге.
Сез мәкаләне үзгәртеп һәм мәгълүмат өстәп,   Википедия проектына ярдәм итә аласыз.
Чыганак — https://tt.wikipedia.org/w/index.php?title=PDGFA&oldid=4133069