EDN1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[23][24]

EDN1
Молекулярная модель
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген EDN1[d][1]
Молекулярная функция hormone activity[d][2][3], signaling receptor binding[d][4], cytokine activity[d][5], endothelin B receptor binding[d][6][4][3], связывание с белками плазмы[d][7] һәм endothelin A receptor binding[d][4][3]
Күзәнәк компоненты Цитоплазма[8], Тельца Вайбеля — Паладе[d][4], basal part of cell[d][4], внеклеточная область[d][4][4][4], rough endoplasmic reticulum lumen[d][4], внеклеточное пространство[d][4][9][10][…] һәм transport vesicle[d][4]
Биологический процесс skeletal system development[d][4], response to amino acid[d][4], positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway[d][4], positive regulation of MAP kinase activity[d][3][11], regulation of sensory perception of pain[d][4], вазоконстрикция[d][4][4][2][…], body fluid secretion[d][4], positive regulation of sarcomere organization[d][11], positive regulation of cardiac muscle hypertrophy[d][11], cell surface receptor signaling pathway[d][6], multicellular organism aging[d][4], artery smooth muscle contraction[d][12][4][13], cellular response to interferon-gamma[d][4], positive regulation of chemokine-mediated signaling pathway[d][14], phosphatidylinositol 3-kinase signaling[d][15], response to leptin[d][4], positive regulation of mitotic nuclear division[d][3], cellular response to hypoxia[d][4], response to muscle stretch[d][4], cellular response to calcium ion[d][4], cellular response to transforming growth factor beta stimulus[d][4], positive regulation of renal sodium excretion[d][4], blood vessel morphogenesis[d][4], negative regulation of blood coagulation[d][9], response to nicotine[d][4], in utero embryonic development[d][4], neutrophil chemotaxis[d][16], развитие сердца[d][4], positive regulation of prostaglandin secretion[d][4], vein smooth muscle contraction[d][17], cartilage development[d][4], rhythmic excitation[d][4], protein kinase C-activating G protein-coupled receptor signaling pathway[d][4], cellular response to glucocorticoid stimulus[d][4], branching involved in blood vessel morphogenesis[d][4], negative regulation of hormone secretion[d][4], positive regulation of smooth muscle contraction[d][4], negative regulation of nitric-oxide synthase biosynthetic process[d][9], positive regulation of prostaglandin-endoperoxide synthase activity[d][18], positive regulation of urine volume[d][4], positive regulation of JUN kinase activity[d][11], leukocyte activation[d][9], membrane depolarization[d][4], negative regulation of transcription by RNA polymerase II[d][5], ответ на озон[d][4], respiratory gaseous exchange by respiratory system[d][4], positive regulation of heart rate[d][2], regulation of blood pressure[d][4], response to lipopolysaccharide[d][4], response to prostaglandin F[d][4], regulation of vasoconstriction[d][4], cellular response to interleukin-1[d][4], response to salt[d][4], positive regulation of cell size[d][11], middle ear morphogenesis[d][4], ноцицепция[d][4], prostaglandin biosynthetic process[d][18], dorsal/ventral pattern formation[d][4], phospholipase D-activating G protein-coupled receptor signaling pathway[d][4], positive regulation of odontogenesis[d][4], regulation of pH[d][4], positive regulation of smooth muscle cell proliferation[d][19], protein kinase C deactivation[d][9], histamine secretion[d][4], maternal process involved in parturition[d][4], intracellular signal transduction[d][4], response to hypoxia[d][4], neural crest cell development[d][4], regulation of systemic arterial blood pressure by endothelin[d][2], nitric oxide transport[d][9], positive regulation of cell migration[d][16], response to testosterone[d][4], positive regulation of cytosolic calcium ion concentration[d][4][20], epithelial fluid transport[d][4], positive regulation of nitric oxide biosynthetic process[d][21], передача сигнала между клетками[d][8], cellular response to tumor necrosis factor[d][4], response to activity[d][4], response to dexamethasone[d][4], superoxide anion generation[d][4], positive regulation of endothelial cell migration[d][21], cellular response to peptide hormone stimulus[d][4], cellular response to fatty acid[d][4], peptide hormone secretion[d][3], cellular response to mineralocorticoid stimulus[d][4], позитивная регуляция пролиферации клеток[d][4][15][20], inositol phosphate-mediated signaling[d][20], positive regulation of hormone secretion[d][3], negative regulation of smooth muscle cell apoptotic process[d][4], calcium-mediated signaling[d][3][20], response to transforming growth factor beta[d][4], положительная регуляция транскрипции РНК полимеразой II промотор[d][4][22], positive regulation of DNA-binding transcription factor activity[d][22], positive regulation of cell growth involved in cardiac muscle cell development[d][22][22], positive regulation of neutrophil chemotaxis[d][4], regulation of signaling receptor activity[d][4], G protein-coupled receptor signaling pathway[d][4][15], adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway[d][4], regulation of glucose transmembrane transport[d][4], negative regulation of gene expression[d][4], positive regulation of NIK/NF-kappaB signaling[d][4] һәм positive regulation of vascular associated smooth muscle cell proliferation[d][4]

Искәрмәләр үзгәртү

  1. 1,0 1,1 UniProt
  2. 2,0 2,1 2,2 2,3 A Inoue, M Yanagisawa, S Kimura et al. The human endothelin family: three structurally and pharmacologically distinct isopeptides predicted by three separate genes // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 1989. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.86.8.2863PMID:2649896
  3. 3,0 3,1 3,2 3,3 3,4 3,5 3,6 3,7 M Maggi, T Barni, G Fantoni et al. Expression and biological effects of endothelin-1 in human gonadotropin-releasing hormone-secreting neurons // J. Clin. Endocrinol. Metab. / R. Paul RobertsonEndocrine Society, 2000. — ISSN 0021-972X; 1945-7197; 0096-7173; 0368-1610doi:10.1210/JC.85.4.1658PMID:10770212
  4. 4,00 4,01 4,02 4,03 4,04 4,05 4,06 4,07 4,08 4,09 4,10 4,11 4,12 4,13 4,14 4,15 4,16 4,17 4,18 4,19 4,20 4,21 4,22 4,23 4,24 4,25 4,26 4,27 4,28 4,29 4,30 4,31 4,32 4,33 4,34 4,35 4,36 4,37 4,38 4,39 4,40 4,41 4,42 4,43 4,44 4,45 4,46 4,47 4,48 4,49 4,50 4,51 4,52 4,53 4,54 4,55 4,56 4,57 4,58 4,59 4,60 4,61 4,62 4,63 4,64 4,65 4,66 4,67 4,68 4,69 4,70 4,71 4,72 4,73 4,74 4,75 4,76 4,77 4,78 4,79 4,80 4,81 GOA
  5. 5,0 5,1 Patterson C., Bode C. Krüppel-like factor 15 regulates BMPER in endothelial cells // Cardiovascular ResearchOUP, 2010. — ISSN 0008-6363; 1755-3245doi:10.1093/CVR/CVP314PMID:19767294
  6. 6,0 6,1 A. Sakamoto, M. Yanagisawa, T. Sakurai et al. Cloning and functional expression of human cDNA for the ETB endothelin receptor // Biochem. Biophys. Res. Commun.Academic Press, Elsevier BV, 1991. — ISSN 0006-291X; 1090-2104doi:10.1016/0006-291X(91)90158-4PMID:1713452
  7. Smet F. D., Bock K. D., Georgiadou M. et al. Inhibition of tumor angiogenesis and growth by a small-molecule multi-FGF receptor blocker with allosteric properties // Cancer CellCell Press, Elsevier BV, 2013. — ISSN 1535-6108; 1878-3686doi:10.1016/J.CCR.2013.02.019PMID:23597562
  8. 8,0 8,1 Yandle T. G., Lewis L. K., Nicholls M. G. Effects of endothelin-1 on release of adrenomedullin and C-type natriuretic peptide from individual human vascular endothelial cells // Journal of EndocrinologyBioscientifica, 2002. — ISSN 0022-0795; 1479-6805doi:10.1677/JOE.0.1750225PMID:12379507
  9. 9,0 9,1 9,2 9,3 9,4 9,5 Ramzy D., Rao V., Tumiati L. C. et al. Elevated endothelin-1 levels impair nitric oxide homeostasis through a PKC-dependent pathway // CirculationLippincott Williams & Wilkins, 2006. — ISSN 0009-7322; 1524-4539doi:10.1161/CIRCULATIONAHA.105.001503PMID:16820593
  10. P Dimoulios, G Kolios, G Notas et al. Ursodeoxycholic acid reduces increased circulating endothelin 2 in primary biliary cirrhosis // Alimentary Pharmacology & TherapeuticsWiley-Blackwell, 2005. — ISSN 0269-2813; 1365-2036; 0953-0673doi:10.1111/J.1365-2036.2005.02307.XPMID:15691296
  11. 11,0 11,1 11,2 11,3 11,4 Koga A., Oka N., Kikuchi T. et al. Adenovirus-mediated overexpression of caveolin-3 inhibits rat cardiomyocyte hypertrophy // Hypertension / A. DominiczakLippincott Williams & Wilkins, 2003. — ISSN 0194-911X; 1524-4563doi:10.1161/01.HYP.0000082926.08268.5DPMID:12847114
  12. Armour C. L. Functional and autoradiographic studies of endothelin-1 and endothelin-2 in human bronchi, pulmonary arteries, and airway parasympathetic ganglia, Functional and Autoradiographic Studies of Endothelin-1 and Endothelin-2 in Human Bronchi, Pulmonary Arteries, and Airway Parasympathetic Ganglia // Journal of Cardiovascular PharmacologyLippincott Williams & Wilkins, 1991. — ISSN 0160-2446; 1533-4023doi:10.1097/00005344-199100177-00059PMID:1725334
  13. G Bogoni, A Rizzi, G Calo et al. Characterization of endothelin receptors in the human umbilical artery and vein // Br. J. Pharmacol.Wiley-Blackwell, 1996. — ISSN 0007-1188; 1476-5381doi:10.1111/J.1476-5381.1996.TB16078.XPMID:8982507
  14. Wilson J. L., Burchell J., Grimshaw M. J. Endothelins induce CCR7 expression by breast tumor cells via endothelin receptor A and hypoxia-inducible factor-1 // Cancer Res. / G. C. PrendergastAmerican Association for Cancer Research, 2006. — ISSN 0008-5472; 1538-7445doi:10.1158/0008-5472.CAN-06-1222PMID:17178876
  15. 15,0 15,1 15,2 G Burnstock Mechanisms of endothelin 1-stimulated proliferation in colorectal cancer cell lines // British Journal of SurgeryWiley, 2007. — ISSN 0007-1323; 1365-2168doi:10.1002/BJS.5536PMID:17078114
  16. 16,0 16,1 Elferink J. G., B M De Koster The involvement of protein kinase G in stimulation of neutrophil migration by endothelins // Eur. J. Pharmacol.Elsevier BV, 1998. — ISSN 0014-2999; 1879-0712; 0922-4106doi:10.1016/S0014-2999(98)00265-9PMID:9696419
  17. Maguire J. J. Endothelin converting enzyme (ECE) activity in human vascular smooth muscle // Br. J. Pharmacol.Wiley-Blackwell, 1997. — ISSN 0007-1188; 1476-5381doi:10.1038/SJ.BJP.0701564PMID:9422810
  18. 18,0 18,1 Leis H. J., D Zach, E Huber et al. Prostaglandin endoperoxide synthase-2 contributes to the endothelin/sarafotoxin-induced prostaglandin E2 synthesis in mouse osteoblastic cells (MC3T3-E1): evidence for a protein tyrosine kinase-signaling pathway and involvement of protein kinase C // Endocrinology / T. K. WoodruffLos Angeles, Calif: Endocrine Society, OUP, 1998. — ISSN 0013-7227; 1945-7170doi:10.1210/EN.139.3.1268PMID:9492062
  19. Lüscher T. F. Endothelin-1 potentiates human smooth muscle cell growth to PDGF: effects of ETA and ETB receptor blockade // CirculationLippincott Williams & Wilkins, 1999. — ISSN 0009-7322; 1524-4539doi:10.1161/01.CIR.100.1.5PMID:10393673
  20. 20,0 20,1 20,2 20,3 Y Yada, K Higuchi, G Imokawa Effects of endothelins on signal transduction and proliferation in human melanocytes // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1991. — ISSN 0021-9258; 1083-351X; 1067-8816PMID:1917960
  21. 21,0 21,1 I Giaever Permissive role of nitric oxide in endothelin-induced migration of endothelial cells // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1997. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.272.3.1747PMID:8999856
  22. 22,0 22,1 22,2 22,3 Song D. W., Ryu J. Y., Kim J. O. et al. The miR-19a/b family positively regulates cardiomyocyte hypertrophy by targeting atrogin-1 and MuRF-1 // Biochem. J.London [etc.]: Portland Press, 2014. — ISSN 0264-6021; 1470-8728doi:10.1042/BJ20130833PMID:24117217
  23. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  24. 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.)