Wikipedia

SERPINE1

SERPINE1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[34][35]

SERPINE1
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген SERPINE1[d][1]
Молекулярная функция peptidase inhibitor activity[d][2], protease binding[d][3][4][5][…], связывание с белками плазмы[d][6][7][8], signaling receptor binding[d][9], serine-type endopeptidase inhibitor activity[d][10][10][11][…], serine-type endopeptidase inhibitor activity[d][10][10][12][…] һәм serine-type endopeptidase inhibitor activity[d][2][13][14][…]
Күзәнәк компоненты внеклеточный матрикс[d][15][16], күзәнәк мембраны[d][2], экзосома[d][17], platelet alpha granule lumen[d][2], внеклеточная область[d][2][2][18], внеклеточное пространство[d][10][19][12], внеклеточное пространство[d][2][13][20][…] һәм collagen-containing extracellular matrix[d][21][22][23]
Биологический процесс negative regulation of endothelial cell apoptotic process[d][20], positive regulation of receptor-mediated endocytosis[d][9], negative regulation of peptidase activity[d][2], negative regulation of fibrinolysis[d][5], positive regulation of inflammatory response[d][24], negative regulation of plasminogen activation[d][20][25][14], фибринолиз[d][2], negative regulation of smooth muscle cell-matrix adhesion[d][26], negative regulation of blood coagulation[d][13], negative regulation of vascular wound healing[d][18], regulation of signaling receptor activity[d][26], negative regulation of smooth muscle cell migration[d][26], positive regulation of monocyte chemotaxis[d][27], platelet degranulation[d][2], extracellular matrix organization[d][2], positive regulation of angiogenesis[d][20], negative regulation of cell migration[d][28], positive regulation of blood coagulation[d][29], defense response to Gram-negative bacterium[d][24], negative regulation of extrinsic apoptotic signaling pathway via death domain receptors[d][20], Циркадный ритм[d][2], Ангиогенез[d][30], positive regulation of interleukin-8 production[d][27], negative regulation of wound healing[d][26], cellular response to lipopolysaccharide[d][27], negative regulation of cell adhesion mediated by integrin[d][26], negative regulation of endopeptidase activity[d][12], положительная регуляция транскрипции РНК полимеразой II промотор[d][2], positive regulation of leukotriene production involved in inflammatory response[d][27], replicative senescence[d][31], dentinogenesis[d][32], positive regulation of odontoblast differentiation[d][32] һәм negative regulation of endopeptidase activity[d][13][33]
Изображение Gene Atlas

Искәрмәләр үзгәртү

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,00 2,01 2,02 2,03 2,04 2,05 2,06 2,07 2,08 2,09 2,10 2,11 2,12 GOA
  3. ↑ Korkmaz B. Discriminating between the activities of human neutrophil elastase and proteinase 3 using serpin-derived fluorogenic substrates // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2002. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M202918200 — PMID:12114510
  4. ↑ Bugge T. H. Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity // Biochem. J. — London [etc.]: Portland Press, 2005. — ISSN 0264-6021; 1470-8728 — doi:10.1042/BJ20050299 — PMID:15853774
  5. ↑ 5,0 5,1 Wagner O. F., Vries C. d., C Hohmann et al. Interaction between plasminogen activator inhibitor type 1 (PAI-1) bound to fibrin and either tissue-type plasminogen activator (t-PA) or urokinase-type plasminogen activator (u-PA). Binding of t-PA/PAI-1 complexes to fibrin mediated by both the finger and the kringle-2 domain of t-PA // J. Clin. Invest. / R. S. Ahima — American Society for Clinical Investigation, 1989. — ISSN 0021-9738; 1558-8238 — doi:10.1172/JCI114211 — PMID:2503541
  6. ↑ Yao H., He G., Chen C. et al. PAI1: a novel PP1-interacting protein that mediates human plasma's anti-apoptotic effect in endothelial cells // J Cell Mol Med, or JCMM — Wiley-Blackwell, Wiley, 2017. — ISSN 1582-1838; 1582-4934; 1453-1321 — doi:10.1111/JCMM.13127 — PMID:28296156
  7. ↑ Dricot A., Barabási A., Tavernier J. et al. A proteome-scale map of the human interactome network // Cell — Cell Press, Elsevier BV, 2014. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2014.10.050 — PMID:25416956
  8. ↑ Boncela J., Cierniewski C. S. Binding of PAI-1 to endothelial cells stimulated by thymosin beta4 and modulation of their fibrinolytic potential // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2006. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M506303200 — PMID:16272158
  9. ↑ 9,0 9,1 S Stefansson, Lawrence D. A., Argraves W. S. Plasminogen activator inhibitor-1 and vitronectin promote the cellular clearance of thrombin by low density lipoprotein receptor-related proteins 1 and 2 // 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.271.14.8215 — PMID:8626514
  10. ↑ 10,0 10,1 10,2 10,3 10,4 GOA
  11. ↑ H Pannekoek, Meijer M. v., Schleef R. R. et al. Functional display of human plasminogen-activator inhibitor 1 (PAI-1) on phages: novel perspectives for structure-function analysis by error-prone DNA synthesis // Gene — Elsevier BV, 1993. — ISSN 0378-1119; 1879-0038 — doi:10.1016/0378-1119(93)90164-X — PMID:8508955
  12. ↑ 12,0 12,1 12,2 Ehrlich H. J., Gebbink R. K., J. Keijer et al. Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1990. — ISSN 0021-9258; 1083-351X; 1067-8816 — PMID:1695900
  13. ↑ 13,0 13,1 13,2 13,3 Ehrlich H. J., Gebbink R. K., J. Keijer et al. Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1990. — ISSN 0021-9258; 1083-351X; 1067-8816 — PMID:1695900
  14. ↑ 14,0 14,1 H Pannekoek, Meijer M. v., Schleef R. R. et al. Functional display of human plasminogen-activator inhibitor 1 (PAI-1) on phages: novel perspectives for structure-function analysis by error-prone DNA synthesis // Gene — Elsevier BV, 1993. — ISSN 0378-1119; 1879-0038 — doi:10.1016/0378-1119(93)90164-X — PMID:8508955
  15. ↑ J. Hagège, Peraldi M. N., E. Rondeau et al. Plasminogen activator inhibitor-1 deposition in the extracellular matrix of cultured human mesangial cells // Am. J. Pathol. — Elsevier BV, 1992. — ISSN 0002-9440; 1525-2191; 0097-3599 — PMID:1632457
  16. ↑ Zanivan S., Hernández-Fernaud J. R. SILAC-based proteomics of human primary endothelial cell morphogenesis unveils tumor angiogenic markers // Mol. Cell. Proteomics — American Society for Biochemistry and Molecular Biology, 2013. — ISSN 1535-9476; 1535-9484 — doi:10.1074/MCP.M113.031344 — PMID:23979707
  17. ↑ Atay S., Gercel-Taylor C., Kesimer M. et al. Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells // Exp. Cell. Res. — Academic Press, Elsevier BV, 2011. — ISSN 0014-4827; 1090-2422 — doi:10.1016/J.YEXCR.2011.01.014 — PMID:21276792
  18. ↑ 18,0 18,1 Carmeliet P., Moons L. Inhibitory role of plasminogen activator inhibitor-1 in arterial wound healing and neointima formation: a gene targeting and gene transfer study in mice // Circulation — Lippincott Williams & Wilkins, 1997. — ISSN 0009-7322; 1524-4539 — doi:10.1161/01.CIR.96.9.3180 — PMID:9386191
  19. ↑ Bajou K., Noel A., Declerck Y. Plasminogen activator inhibitor-1 protects endothelial cells from FasL-mediated apoptosis // Cancer Cell — Cell Press, Elsevier BV, 2008. — ISSN 1535-6108; 1878-3686 — doi:10.1016/J.CCR.2008.08.012 — PMID:18835034
  20. ↑ 20,0 20,1 20,2 20,3 20,4 Bajou K., Noel A., Declerck Y. Plasminogen activator inhibitor-1 protects endothelial cells from FasL-mediated apoptosis // Cancer Cell — Cell Press, Elsevier BV, 2008. — ISSN 1535-6108; 1878-3686 — doi:10.1016/J.CCR.2008.08.012 — PMID:18835034
  21. ↑ J. Hagège, Peraldi M. N., E. Rondeau et al. Plasminogen activator inhibitor-1 deposition in the extracellular matrix of cultured human mesangial cells // Am. J. Pathol. — Elsevier BV, 1992. — ISSN 0002-9440; 1525-2191; 0097-3599 — PMID:1632457
  22. ↑ Zanivan S., Hernández-Fernaud J. R. SILAC-based proteomics of human primary endothelial cell morphogenesis unveils tumor angiogenic markers // Mol. Cell. Proteomics — American Society for Biochemistry and Molecular Biology, 2013. — ISSN 1535-9476; 1535-9484 — doi:10.1074/MCP.M113.031344 — PMID:23979707
  23. ↑ Naba A., Hynes R. O., Langer R. et al. Comprehensive proteomic characterization of stem cell-derived extracellular matrices. // Biomaterials — Elsevier BV, 2017. — 13 p. — ISSN 0142-9612; 1878-5905 — doi:10.1016/J.BIOMATERIALS.2017.03.008 — PMID:28327460
  24. ↑ 24,0 24,1 Florquin S., Tom van der Poll, Carmeliet P. et al. Plasminogen activator inhibitor type 1 is protective during severe Gram-negative pneumonia // Blood — American Society of Hematology, Elsevier BV, 2007. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2006-05-025197 — PMID:17032919
  25. ↑ Boulaftali Y., Adam F., Ollivier V. et al. Anticoagulant and antithrombotic properties of platelet protease nexin-1 // Blood — American Society of Hematology, Elsevier BV, 2009. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2009-04-217240 — PMID:19855083
  26. ↑ 26,0 26,1 26,2 26,3 26,4 Stefansson S., Lawrence D. A. The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin // Nature / M. Skipper — NPG, Springer Science+Business Media, 1996. — ISSN 1476-4687; 0028-0836 — doi:10.1038/383441A0 — PMID:8837777
  27. ↑ 27,0 27,1 27,2 27,3 Xu X., Wang H., Wang Z. et al. Plasminogen activator inhibitor-1 promotes inflammatory process induced by cigarette smoke extraction or lipopolysaccharides in alveolar epithelial cells // Experimental Lung Research — Informa, 2009. — ISSN 0190-2148; 1521-0499 — doi:10.3109/01902140902912519 — PMID:19916862
  28. ↑ Crandall D. L., Busler D. E., B McHendry-Rinde et al. Autocrine regulation of human preadipocyte migration by plasminogen activator inhibitor-1 // J. Clin. Endocrinol. Metab. / R. Paul Robertson — Endocrine Society, 2000. — ISSN 0021-972X; 1945-7197; 0096-7173; 0368-1610 — doi:10.1210/JCEM.85.7.6678 — PMID:10902815
  29. ↑ Fay W. P., Parker A. C., Condrey L. R. et al. Human plasminogen activator inhibitor-1 (PAI-1) deficiency: characterization of a large kindred with a null mutation in the PAI-1 gene // Blood — American Society of Hematology, Elsevier BV, 1997. — ISSN 0006-4971; 1528-0020 — PMID:9207454
  30. ↑ Aitkenhead M., Wang S., Nakatsu M. N. et al. Identification of endothelial cell genes expressed in an in vitro model of angiogenesis: induction of ESM-1, (beta)ig-h3, and NrCAM // Microvascular Research — Elsevier BV, 2002. — ISSN 0026-2862; 1095-9319 — doi:10.1006/MVRE.2001.2380 — PMID:11866539
  31. ↑ Bernards R. Plasminogen activator inhibitor-1 is a critical downstream target of p53 in the induction of replicative senescence // Nat. Cell Biol. — NPG, 2006. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB1448 — PMID:16862142
  32. ↑ 32,0 32,1 Jin B., Choung P. Recombinant Human Plasminogen Activator Inhibitor-1 Accelerates Odontoblastic Differentiation of Human Stem Cells from Apical Papilla. // Tissue Engineering Part A: Tissue Engineering — Mary Ann Liebert, Inc., 2016. — ISSN 1937-3341; 1937-335X — doi:10.1089/TEN.TEA.2015.0273 — PMID:27046084
  33. ↑ 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
  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.)


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