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| Untersuchte Arbeit: Seite: 24, Zeilen: 1ff (entire page) |
Quelle: Lang et al 2006 Seite(n): 1151, 1153, Zeilen: 1151: abstract; 1153: l.col: 28ff |
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| Moreover, SGK1 transcription is stimulated by an increased cytosolic Ca2+ concentration (Klingel K. et al., (2000) Am J Physiol Gastrointest Liver Physiol) and by nitric oxide (Turpaev K. et al., (2005) Free Radic Biol Med). SGK1 transcript levels are increased by ischemia of brain (Nishida Y. et al., (2004) Brain Res) and kidney (Feng Y. et al., (2006) Kidney Blood Pressure Res). SGK1 expression is decreased during rejection of transplanted kidneys (Velic A. et al., (2005) Am J Transplant).
Similar to its isoforms SGK2 and SGK3, SGK1 is activated by insulin and growth factors via phosphatidylinositol 3-kinase and the 3-phosphoinositide-dependent kinase PDK1. SGKs activate ion channels (e.g.: ENaC, TRPV5, ROMK, Kv1.3, KCNE1/KCNQ1, GluR1, GluR6), carriers (e.g., NHE3, GLUT1, SGLT1, EAAT1–5), and the Na+-K+-ATPase. They regulate the activity of enzymes (e.g., glycogen synthase kinase-3, ubiquitin ligase Nedd4–2, phosphomannose mutase-2) and transcription factors (e.g., forkhead transcription factor FKHRL1, α-catenin, nuclear factor kB). Leukocyte SGK1 transcript levels are enhanced by treatment with dialysis (Friedrich B. et al., (2005) Nephrol Dial Transplant). A striking increase of SGK1 expression is observed during wound healing (Iyer V. et al., (1999) Science) and in fibrosing tissue, such as diabetic nephropathy (Kumar J. M et al., (1999) J Am Soc Nephrol), glomerulonephritis (Friedrich B. et al., (2002) Kidney Blood Press Res), liver cirrhosis (Fillon S. et al., (2002) Cell Physiol Biochem), fibrosing pancreatitis (Klingel K. et al., (2000) Am J Physiol Gastrointest Liver Physiol), Crohn’s disease (Waldegger S. et al., (1999) Gastroenterology), lung fibrosis and cardiac fibrosis (Vallon V. et al., (2006) J Mol Med). SGK1 gene transcription is stimulated by DNA damage through p53 and activation of extracellular signalregulated kinase (ERK1/2) (Mizuno H. et al., (2001) Genes Cells; You H. et al., (2004) Proc Natl Acad Sci USA), and is also upregulated after neuronal injury (Imaizumi K. et al., (1994) Brain Res), neuronal excitotoxicity (Hollister R. et al., (1997) Neuroscience), and neuronal challenge by exposure to microgravity (David S. et al., (2005) J Neurosci). The promoter of the rat SGK1 gene carries several putative and confirmed transcription factor binding sites including those for the glucocorticoid receptor (GR), the mineralocorticoid receptor (MR), the progesterone receptor (PR), the vitamin D receptor (VDR), the retinoid X receptor (RXR), the farnesoid X receptor (FXR), the sterol regulatory element binding protein (SREBP), PPARγ, the cAMP response element binding protein (CREB), the p53 tumor suppressor protein, the Sp1 transcription factor, the activating protein 1 (AP1), the activating transcription factor 6 (ATF6), the heat shock factor (HSF), reticuloendotheliosis viral oncogene homolog (c-Rel) and nuclear factor κB (NFκB), signal transducers and activators of transcription (STAT), the TGF-α-dependent transcription factors SMAD3 and SMAD4, and forkhead activin signal transducer (FAST) (Firestone G. et al., (2003) Cell Physiol Biochem). The regulation of SGK1 transcript levels is fast; appearance and disappearance of SGK1 mRNA require circa 20 min (Waldegger S. et al., (1997) Proc Natl Acad Sci USA). |
[page 1151]
Similar to its isoforms SGK2 and SGK3, SGK1 is activated by insulin and growth factors via phosphatidylinositol 3-kinase and the 3-phosphoinositide-dependent kinase PDK1. SGKs activate ion channels (e.g., ENaC, TRPV5, ROMK, Kv1.3, KCNE1/KCNQ1, GluR1, GluR6), carriers (e.g., NHE3, GLUT1, SGLT1, EAAT1–5), and the Na+-K+-ATPase. They regulate the activity of enzymes (e.g., glycogen synthase kinase-3, ubiquitin ligase Nedd4–2, phosphomannose mutase-2) and transcription factors (e.g., forkhead transcription factor FKHRL1, α-catenin, nuclear factor κB). [page 1153] Moreover, SGK1 transcription is stimulated by an increased cytosolic Ca2+ concentration (170) and by nitric oxide (321). SGK1 transcript levels are increased by ischemia of brain (236) and kidney (108). SGK1 expression is decreased during rejection of transplanted kidneys (329). Leukocyte SGK1 transcript levels are enhanced by treatment with dialysis (116). A striking increase of SGK1 expression is observed during wound healing (164) and in fibrosing tissue, such as diabetic nephropathy (178, 184), glomerulonephritis (118), liver cirrhosis (110), fibrosing pancreatitis (170), Crohn’s disease (352), lung fibrosis (360), and cardiac fibrosis (323). SGK1 gene transcription is stimulated by DNA damage through p53 and activation of extracellular signal-regulated kinase (ERK1/2) (222, 375), and is also upregulated after neuronal injury (159), neuronal excitotoxicity (145), and neuronal challenge by exposure to microgravity (84). The promoter of the rat SGK1 gene carries several putative and confirmed transcription factor binding sites including those for the glucocorticoid receptor (GR), the mineralocorticoid receptor (MR), the progesterone receptor (PR), the vitamin D receptor (VDR), the retinoid X receptor (RXR), the farnesoid X receptor (FXR), the sterol regulatory element binding protein (SREBP), PPARγ, the cAMP response element binding protein (CREB), the p53 tumor suppressor protein, the Sp1 transcription factor, the activating protein 1 (AP1), the activating transcription factor 6 (ATF6), the heat shock factor (HSF), reticuloendotheliosis viral oncogene homolog (c-Rel) and nuclear factor κB (NFκB), signal transducers and activators of transcription (STAT), the TGF-β-dependent transcription factors SMAD3 and SMAD4, and forkhead activin signal transducer (FAST) (112). The regulation of SGK1 transcript levels is fast; appearance and disappearance of SGK1 mRNA require <20 min (349). 84. 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Deranged transcriptional regulation of cell-volume-sensitive kinase hSGK in diabetic nephropathy. Proc Natl Acad Sci USA 97: 8157–8162, 2000. 222. Mizuno H and Nishida E. The ERK MAP kinase pathway mediates induction of SGK (serum- and glucocorticoid-inducible kinase) by growth factors. Genes Cells 6: 261–268, 2001 236. Nishida Y, Nagata T, Takahashi Y, Sugahara-Kobayashi M, Murata A, and Asai S. Alteration of serum/glucocorticoid regulated kinase-1 (sgk-1) gene expression in rat hippocampus after transient global ischemia. Brain Res 123: 121–125, 2004 321. Turpaev K, Bouton C, Diet A, Glatigny A, and Drapier JC. Analysis of differentially expressed genes in nitric oxide-exposed human monocytic cells. Free Radic Biol Med 38: 1392–1400, 2005 323. Vallon V, Wyatt A, Klingel K, Huang DY, Hussain A, Berchtold S, Friedrich B, Grahammer F, BelAiba RS, Görlach A, Wulff P, Daut J, Dalton ND, Ross J Jr, Flögel U, Schrader J, Osswald H, Kandolf R, Kuhl D, and Lang F. SGK1-dependent cardiac CTGF formation and fibrosis following DOCA treatment. J Mol Med 84; 396–404, 2006. 329. Velic A, Gabriels G, Hirsch JR, Schroter R, Edemir B, Paasche S, and Schlatter E. Acute rejection after rat renal transplantation leads to downregulation of Na+ and water channels in the collecting duct. Am J Transplant 5: 1276–1285, 2005. 349. Waldegger S, Barth P, Raber G, and 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 USA 94: 4440–4445, 1997. 352. Waldegger S, Klingel K, Barth P, Sauter M, Rfer ML, Kandolf R, and Lang F. h-Sgk serine-threonine protein kinase gene as transcriptional target of transforming growth factor beta in human intestine. Gastroenterology 116: 1081–1088, 1999. 360. Wärntges S, Klingel K, Weigert C, Fillon S, Buck M, Schleicher E, Rodemann HP, Knabbe C, Kandolf R, and Lang F. Excessive transcription of the human serum and glucocorticoid dependent kinase hSGK1 in lung fibrosis. Cell Physiol Biochem 12: 135–142, 2002. 375. You H, Jang Y, You T, Okada H, Liepa J, Wakeham A, Zaugg K, and Mak TW. p53-dependent inhibition of FKHRL1 in response to DNA damage through protein kinase SGK1. Proc Natl Acad Sci USA"" 101: 14057–14062, 2004. |
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