von Dr. Diana Sandulache
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| [1.] Dsa/Fragment 022 02 - Diskussion Zuletzt bearbeitet: 2016-08-20 19:07:12 WiseWoman | Busjahn et al 2002, Dsa, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop |
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| Untersuchte Arbeit: Seite: 22, Zeilen: 2-14 |
Quelle: Busjahn et al 2002 Seite(n): 256, Zeilen: l.col: 1ff |
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| The serum- and glucocorticoid-regulated kinase (SGK) was originally cloned from rat mammary tumor cells as a glucocorticoid responsive gene. The human isoform was subsequently cloned as a cell volume–sensitive gene upregulated by both hypertonic and isotonic cell shrinkage (Waldegger S. et al., (1997) Proc Natl Acad Sci; Waldegger S. et al., (2000) Cell Physiol Biochem).
Because of the discovery of the 2 isoforms SGK2 and SGK3 (Kobayashi T. et al., (1999) Biochem J) the originally cloned kinase is labeled SGK1. SGK1 is expressed in renal tubular epithelial cells (Naray-Fejes-Toth A. et al., (1999) J Biol Chem; Loffing J. et al., (2001) Am J Physiol Renal Physiol) and its transcription is strongly stimulated by mineralocorticoids (Chen SY. et al., (1999) Proc Natl Acad Sci USA) suggesting a role in renal Na+ regulation. Indeed, coexpression of SGK1 with the renal epithelial Na+ channel (ENaC), in Xenopus oocytes markedly upregulates Na+ channel activity by enhancing channel protein abundance in the cell membrane. |
The serum- and glucocorticoid-regulated kinase (SGK) was originally cloned from rat mammary tumor cells as a glucocorticoid responsive gene.1 The human isoform was subsequently cloned as a cell volume–sensitive gene upregulated by both hypertonic and isotonic cell shrinkage.2,3 Because of the discovery of the 2 isoforms SGK2 and SGK3,4 the originally cloned kinase is labeled SGK1. SGK1 is expressed in renal tubular epithelial cells,5,6 and its transcription is strongly stimulated by mineralocortcoids,7 suggesting a role in renal Na+ regulation. Indeed, coexpression of SGK1 with the renal epithelial Na+ channel (ENaC) in Xenopus oocytes markedly upregulates Na+ channel activity by enhancing channel protein abundance in the cell membrane.5–9
1. Webster MK, Goya L, Ge Y, Maiyar AC, Firestone GL. Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum. Mol Cell Biol. 1993;13:2031–2040. 2. Waldegger S, Barth P, Raber G, Lang F. Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume. Proc Natl Acad Sci U S A. 1997;94:4440–4445. 3. Waldegger S, Gabrysch S, Barth P, Fillon S, Lang F. h-sgk serine threonine protein kinase as transcriptional target of p38/MAP kinase pathway in HepG2 human hepatoma cells. Cell Physiol Biochem. 2000;10:203–208. 4. Kobayashi T, Deak M, Morrice N, Cohen P. Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase. Biochem J. 1999;344:189–197. 5. Naray-Fejes-Toth A, Canessa C, Cleaveland ES, Aldrich G, Fejes-Toth G. Sgk is an aldosterone-induced kinase in the renal collecting duct: effects on epithelial Na+ channels. J Biol Chem. 1999;274:16973–16978. 6. Loffing J, Zecevic M, Feraille E, Kaissling B, Asher C, Rossier BC, Firestone GL, Pearce D, Verrey F. Aldosterone induces rapid apical translocation of ENaC in early portion of renal collecting system: possible role of SGK. Am J Physiol Renal Physiol. 2001;280:F675–F682. 7. Chen SY, Bhargava A, Mastroberardino L, Meijer OC, Wang J, Buse P, Firestone GL, Verrey F, Pearce D. Epithelial sodium channel regulated by aldosterone-induced protein sgk. Proc Natl Acad Sci U S A. 1999;96: 2514–2519. 8. Bohmer C, Wagner CA, Beck S, Moschen V, Melzig J, Werner A, Lin JT, Lang F, Wehner F. The shrinkage-activated Na+ conductance of rat hepatocytes and its possible correlation to rENaC. Cell Physiol Biochem. 2000;10: 187–194. 9. Wagner CA, Ott M, Klingel K, Beck S, Melzig J, Friedrich B, Wild KN, Broer S, Moschen I, Albers A, Waldegger S, Tummler B, Egan ME, Geibel JP, Kandolf R, Lang F. Effects of the serine/threonine kinase SGK1 on the epithelial Na+ channel (ENaC) and CFTR: implications for cystic fibrosis. Cell Physiol Biochem. 2001;11:209–218. |
The source is not mentioned. |
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| [2.] Dsa/Fragment 022 15 - Diskussion Zuletzt bearbeitet: 2016-08-07 21:24:47 WiseWoman | Dsa, Fragment, Gesichtet, KomplettPlagiat, Lang et al 2006, SMWFragment, Schutzlevel sysop |
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| Untersuchte Arbeit: Seite: 22, Zeilen: 15-21 |
Quelle: Lang et al 2006 Seite(n): 1151, 1152, 1153, Zeilen: 1151: last lines; 1152: l.col: 20ff; 1153: r.col: 10ff |
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| SGK kinases are expressed in a wide variety of species including shark and Caenorhabditis elegans. Yeast expresses two orthologs, Ypk1 and Ypk2, which are involved in endocytosis and required for survival. Yeast lacking Ypk1 and Ypk2 can be rescued by mammalian SGK1. SGKs participate in the regulation of transport, hormone release, neuroexcitability, cell proliferation, and apoptosis.
Little is known about genomic regulation of SGK2 and SGK3, which appear to be less sensitive to hormonal regulation than SGK1. |
SGKs participate in the regulation of transport, hormone release, neuroexcitability, cell proliferation, and apoptosis.
[page 1152] SGK kinases are expressed in a wide variety of species including shark (348) and Caenorhabditis elegans (142). Yeast express two orthologs, Ypk1 and Ypk2, which are involved in endocytosis (87) and required for survival (60). Yeast lacking Ypk1 and Ypk2 can be rescued by mammalian SGK1 (60). [page 1153] Little is known about genomic regulation of SGK2 and SGK3, which appear to be less sensitive to hormonal regulation than SGK1 (182). 60. Casamayor A, Torrance PD, Kobayashi T, Thorner J, and Alessi DR. Functional counterparts of mammalian protein kinases PDK1 and SGK in budding yeast. Curr Biol 9: 186–197, 1999. 87. DeHart AK, Schnell JD, Allen DA, and Hicke L. The conserved Pkh-Ypk kinase cascade is required for endocytosis in yeast. J Cell Biol 156: 241–248, 2002. 142. Hertweck M, Gobel C, and Baumeister R. C. elegans SGK-1 is the critical component in the Akt/PKB kinase complex to control stress response and life span. Dev Cell 6: 577–588, 2004. 182. Lang F and Cohen P. Regulation and physiological roles of serumand glucocorticoid-induced protein kinase isoforms. Sci STKE 2001: RE17, 2001. 348. Waldegger S, Barth P, Forrest JN Jr, Greger R, and Lang F. Cloning of sgk serine-threonine protein kinase from shark rectal gland: a gene induced by hypertonicity and secretagogues. Pflügers Arch 436: 575–580, 1998 |
The source is not mentioned. |
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| [3.] Dsa/Fragment 022 21 - Diskussion Zuletzt bearbeitet: 2016-08-20 19:19:25 WiseWoman | BauernOpfer, BelAiba et al 2006, Dsa, Fragment, Gesichtet, SMWFragment, Schutzlevel sysop |
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| Untersuchte Arbeit: Seite: 22, Zeilen: 21-42 |
Quelle: BelAiba et al 2006 Seite(n): 828, 829, Zeilen: 828: r.col: 4ff; 829: l.col: 1ff |
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| The serum- and glucocorticoid-inducible kinase-1, SGK1, is a known downstream effector of the PI3K cascade. SGK1 belongs to the “AGC” family of serine-threonine kinases and shares approximately 45% to 55% homology with Akt in its catalytic domain.
In contrast to Akt, SGK1 is also regulated at the transcriptional level in response to various hormones, growth factors, and extracellular stresses in a cell type – dependent manner, allowing sgk1 to be available for its targets only when needed. SGK1 was originally cloned from murine mammary tumor cells as a glucocorticoid-responsive gene. Human SGK1 was subsequently cloned as a cell volume-sensitive gene upregulated by hypertonic cell shrinkage. Increasing evidence suggests that expression, enzymatic activity, and cellular localization of SGK1 are regulated in response to various stimuli controlling not only cell volume and epithelial transport, but also cardiac action potential and cell proliferation, survival, and apoptosis. Excessive transcription of SGK1 has been shown to parallel diabetic nephropathy, glomerulonephritis, hepatic cirrhosis, pulmonary fibrosis, and polymorphisms of the SGK1 gene correlated with hypertension. Despite the wide tissue distribution of sgk1 and its sensitivity to various stimuli, the role of SGK-1 in the cardiovascular and pulmonary system remained ill defined. Because heparin, an inhibitor of thrombin formation, has been shown to decrease SGK1 mRNA in aortic smooth muscle cells, we hypothesized that SGK1 may play a role in thrombin signaling in human pulmonary artery smooth muscle cells (PASMC). We found that SGK1 is activated and induced by thrombin, that it regulates TF expression and activity in PASMC, and that it is present in remodeled pulmonary vessels with media hypertrophy associated with ph (Rachida S. et al., (2006) Circ Res). |
The serum- and glucocorticoid-inducible kinase-1, Sgk-1, is a known downstream effector of the PI3K cascade. Sgk-1 belongs to the “AGC” family of serine-threonine kinases and shares approximately 45% to 55% homology with Akt in its catalytic domain.6 In contrast to Akt, Sgk-1 is also regulated at the transcriptional level in response to various hormones, growth factors, and extracellular stresses in a cell type– dependent manner, allowing Sgk-1 to be available for its targets only when needed.7,8
Sgk-1 was originally cloned from murine mammary tumor cells as a glucocorticoid-responsive gene.6 Human Sgk-1 was subsequently cloned as a cell volume-sensitive gene upregulated by hypertonic cell shrinkage.9 Increasing evidence [page 829] suggests that expression, enzymatic activity, and cellular localization of Sgk-1 are regulated in response to various stimuli controlling not only cell volume and epithelial transport, but also cardiac action potential and cell proliferation, survival, and apoptosis.7,8 Excessive transcription of Sgk-1 has been shown to parallel diabetic nephropathy,10 glomerulonephritis,11 hepatic cirrhosis,12 pulmonary fibrosis,13 and polymorphisms of the Sgk-1 gene correlated with hypertension.14 Despite the wide tissue distribution of Sgk-1 and its sensitivity to various stimuli, the role of Sgk-1 in the cardiovascular and pulmonary system remained ill defined. Because heparin, an inhibitor of thrombin formation, has been shown to decrease Sgk-1 mRNA in aortic smooth muscle cells,15 we hypothesized that Sgk-1 may play a role in thrombin signaling in human pulmonary artery smooth muscle cells (PASMC), the main cell type involved in PH. We found that Sgk-1 is activated and induced by thrombin, that it regulates TF expression and activity in PASMC, and that it is present in remodeled pulmonary vessels with media hypertrophy associated with PH. 6. Webster MK, Goya L, Ge Y, Maiyar AC, Firestone GL. Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum. Mol Cell Biol. 1993;13:2031–2040. 7. Firestone GL, Giampaolo JR, O’Keeffe BA. Stimulus-dependent regulation of serum and glucocorticoid inducible protein kinase (SGK) transcription, subcellular localization and enzymatic activity. Cell Physiol Biochem. 2003;13:1–12. 8. Lang F, Cohen P. Regulation and physiological roles of serum- and glucocorticoid-induced protein kinase isoforms. Sci STKE. 2001; 108:RE17. 9. Waldegger S, Barth P, Raber G, Lang F. Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume. Proc Natl Acad Sci U S A. 1997;94:4440–4445. 10. Kumar JM, Brooks DP, Olson BA, Laping NJ. Sgk, a putative serine/ threonine kinase, is differentially expressed in the kidney of diabetic mice and humans. J Am Soc Nephrol. 1999;10:2488–2494. 11. Friedrich B, Warntges S, Klingel K, Sauter M, Kandolf R, Risler T, Muller GA, Witzgall R, Kriz W, Grone HJ, Lang F. Up-regulation of the human serum and glucocorticoid-dependent kinase 1 in glomerulonephritis. Kidney Blood Press Res. 2002;25:303–307. 12. Fillon S, Klingel K, Warntges S, Sauter M, Gabrysch S, Pestel S, Tanneur V, Waldegger S, Zipfel A, Viebahn R, Haussinger D, Broer S, Kandolf R, Lang F. Expression of the serine/threonine kinase hSGK1 in chronic viral hepatitis. Cell Physiol Biochem. 2002;12:47–54. 13. Waerntges S, Klingel K, Weigert C, Fillon S, Buck M, Schleicher E, Rodemann HP, Knabbe C, Kandolf R, Lang F. Excessive transcription of the human serum and glucocorticoid dependent kinase hSGK1 in lung fibrosis. Cell Physiol Biochem. 2002;12:135–142. 14. Busjahn A, Aydin A, Uhlmann R, Krasko C, Bahring S, Szelestei T, Feng Y, Dahm S, Sharma AM, Luft FC, Lang F. Serum- and glucocorticoidregulated kinase (SGK1) gene and blood pressure. Hypertension. 2002; 40:256–260. 15. Delmolino LM, Castellot JJ Jr. Heparin suppresses sgk, an early response gene in proliferating vascular smooth muscle cells. J Cell Physiol. 1997; 173:371–379. |
The reference to "Rachida S. et al., (2006) Circ Res" potentially indicates the source, as the first author of the source is named "Rachida S. BelAiba". No such entry cannot be found in the bibliography, and nothing indicates that text spanning two paragraphs has been copied from it, mostly verbatim. |
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Letzte Bearbeitung dieser Seite: durch Benutzer:WiseWoman, Zeitstempel: 20160820192016