Fandom

VroniPlag Wiki

Dsa/023

< Dsa

31.377Seiten in
diesem Wiki
Seite hinzufügen
Diskussion0 Teilen

Störung durch Adblocker erkannt!


Wikia ist eine gebührenfreie Seite, die sich durch Werbung finanziert. Benutzer, die Adblocker einsetzen, haben eine modifizierte Ansicht der Seite.

Wikia ist nicht verfügbar, wenn du weitere Modifikationen in dem Adblocker-Programm gemacht hast. Wenn du sie entfernst, dann wird die Seite ohne Probleme geladen.

Nierenfunktion Kinase-defizienter Mäuse

von Dr. Diana Sandulache

vorherige Seite | zur Übersichtsseite | folgende Seite
Statistik und Sichtungsnachweis dieser Seite findet sich am Artikelende
[1.] Dsa/Fragment 023 02 - Diskussion
Zuletzt bearbeitet: 2016-08-07 21:47:09 WiseWoman
BauernOpfer, Dsa, Fragment, Gesichtet, Lang et al 2006, SMWFragment, Schutzlevel sysop

Typus
BauernOpfer
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 23, Zeilen: 2-40
Quelle: Lang et al 2006
Seite(n): 1152, 1153, Zeilen: 1152: l.col: 2ff, 1153: l.col: 1ff
SGK1 was originally cloned as an immediate early gene transcriptionally stimulated by serum and glucocorticoids in rat mammary tumor cells (Firestone G. et al., (2003) Cell Physiol Biochem). The human isoform has been discovered as a cell volume regulated gene upregulated by cell shrinkage.

Transcription of SGK1 is upregulated by both serum and glucocorticoids. Several other hormones and mediators stimulate SGK1 transcription, including mineralocorticoids, gonadotropins (Lang F. et al., (2006) Physiol Rev), 1.25-dihydroxyvitamin D3 [sic] (1.25(OH)2D3), transforming growth factor-α (TGF-α) (Kumar JM. et al., (1999) J Am Soc Nephrol; Lang F. et al., (2000) Proc Natl Acad Sci USA), interleukin-6 (Mc Ewen BS. et al., (1995) Vitam Horm), fibroblast and platelet-derived growth factor (Mizuno H. et al., (2001) Genes Cell), thrombin (Belaiba R. et al., (2006) Circ Res), endothelin (Wolf Sc. et al., (2006) Biochem Pharmacol), as well as other cytokines (Verenivov A. et al., (2001) Physiol Biochem). Moreover, activation of peroxisome proliferator-activated receptor γ (PPAR γ) stimulates SGK1 gene transcription (Hong G. et al., (2003) Faseb J). The human isoform has been identified as a cell volume-regulated gene that is transcriptionally upregulated by cell shrinkage.

In renal epithelial (A6) cells, SGK1 expression is stimulated by cell swelling rather than cell shrinkage (Rozansky DJ. et al., (2002) Am J Physiol Renal Physiol). SGK1 transcription is further stimulated by excessive glucose concentrations (Lang F. et al., (2000) Proc Natl Acad Sci USA; Saad S. et al., (2005) Kidney Int), heat shock, ultraviolet (UV) radiation, and oxidative stress. SGK1 transcription is inhibited by heparin (Delmolino LM. et al., (1997) J Cell Physiol) and by mutations in the gene MECP2, which underlies Rett syndrome (RTT), a disorder with severe mental retardation (Nuber UA. et al., (2005) Hum Mol Genet).

Intestinal SGK1 transcription is further regulated by dietary iron (Marzullo L. et al., (2004) Gene). Signaling molecules involved in the transcriptional regulation of SGK1 include protein kinase C (Lang F. et al., (2000) Proc Natl Acad Sci USA; Mizuno H and Nishida E., (2001) Genes Cells), the protein kinase Raf (Mizuno H and Nishida E., (2001) Genes Cells), mammalian mitogen-activated protein kinase (BMK1) (Hayashi M. et al., (2001) J Biol Chem), mitogen-activated protein kinase (MKK1) (Davies SP. et al., (2000) Biochem J; Mizuno H and Nishida E., (2001) Genes Cells), stress-activated protein kinase-2 (SAPK2, p38 kinase) (Bell LM. et al., (2000) J Biol Chem; Chen S. et al., (2004) Hypertension; Waldegger S. et al., (2000) Cell Physiol Biochem) and phosphatidylinositol (PI) 3-kinase.

Follicle-stimulating hormone (FSH) stimulates phosphorylation and activation of protein kinase B (PKB/Akt) and serum and glucocorticoid-induced kinase (SGK): evidence for a kinase-independent signaling by FSH in granulosa cells, cAMP (Gonzalez-Robayna IJ. et al., (2000) Mol Endocrinol; Klingel K. et al., (2000) Am J Physiol Gastrointest Liver Physiol) and p53 (Maiyar AC. et al., (1996) J Biol Chem; Maiyar AC. et al., (1997) Mol Endocrinol).

[page 1152]

The serum- and glucocorticoid-inducible kinase-1 (SGK1) was originally cloned as an immediate early gene transcriptionally stimulated by serum and glucocorticoids in rat mammary tumor cells (112, 361, 362). The human isoform has been discovered as a cell volume-regulated gene upregulated by cell shrinkage (349). [...]

[...]

Transcription of SGK1 is upregulated by both serum and glucocorticoids (49, 78, 96, 112, 162, 167, 221, 232, 289, 361, 362, 388). Several other hormones and mediators stimulate SGK1 transcription, including mineralocorticoids (29, 49, 65, 96, 135, 168, 197, 206, 231, 290), gonad-

[page 1153]

otropins (68, 129, 263, 264, 278), 1,25-dihydroxyvitamin D [1,25(OH)2D3] (4), transforming growth factor-β (TGF-β) (178, 184, 352), interleukin-6 (216), fibroblast and plateletderived growth factor (222), thrombin (23), endothelin (366), as well as other cytokines (80, 182, 330). Moreover, activation of peroxisome proliferator-activated receptor γ (PPARγ) stimulates SGK1 gene transcription (146). The human isoform has been identified as a cell volume-regulated gene that is transcriptionally upregulated by cell shrinkage (349). In renal epithelial (A6) cells, SGK1 expression is stimulated by cell swelling rather than cell shrinkage (272). SGK1 transcription is further stimulated by excessive glucose concentrations (184, 275), heat shock, ultraviolet (UV) radiation, and oxidative stress (198).

SGK1 transcription is inhibited by heparin (90) and by mutations in the gene MECP2, which underlies Rett syndrome (RTT), a disorder with severe mental retardation (237). Intestinal SGK1 transcription is further regulated by dietary iron (212).

Signaling molecules involved in the transcriptional regulation of SGK1 include protein kinase C (184, 222), the protein kinase Raf (222), mammalian mitogen-activated protein kinase (BMK1) (137), mitogen-activated protein kinase (MKK1) (85, 222), stress-activated protein kinase-2 (SAPK2, p38 kinase) (24, 64, 351), phosphatidylinositol (PI) 3-kinase (129), cAMP (129, 170), and p53 (207, 209).


[...]

129. Gonzalez-Robayna IJ, Falender AE, Ochsner S, Firestone GL, and Richards JS. Follicle-stimulating hormone (FSH) stimulates phosphorylation and activation of protein kinase B (PKB/Akt) and serum and glucocorticoid-lnduced [sic] kinase (Sgk): evidence for A kinase-independent signaling by FSH in granulosa cells. Mol Endocrinol 14: 1283–1300, 2000.

[...]

170. Klingel K, Warntges S, Bock J, Wagner CA, Sauter M, Waldegger S, Kandolf R, and Lang F. Expression of cell volume-regulated kinase h-sgk in pancreatic tissue. Am J Physiol Gastrointest Liver Physiol 279: G998–G1002, 2000.

[...]

207. Maiyar AC, Huang AJ, Phu PT, Cha HH, and Firestone GL. p53 stimulates promoter activity of the sgk. Serum/glucocorticoid-inducible serine/threonine protein kinase gene in rodent mammary epithelial cells. J Biol Chem 271: 12414–12422, 1996.

209. Maiyar AC, Phu PT, Huang AJ, and Firestone GL. Repression of glucocorticoid receptor transactivation and DNA binding of a glucocorticoid response element within the serum/glucocorticoid-inducible protein kinase (sgk) gene promoter by the p53 tumor suppressor protein. Mol Endocrinol 11: 312–329, 1997

Anmerkungen

The source is mentioned once in the second reference, but without any indication that the entire page is taken from it.

For better readability, not all 53 bibliography entries of the source text have been documented.

Note also that the title of the publication Gonzalez-Robayna et al. (2000) has made it into the text of the thesis. There is also no entry Gonzales-Robayana et al. (2000) in the thesis bibliography, that author is only listed as second co-author for a different paper published 2000 in a different journal.

Sichter
(Hindemith), WiseWoman


vorherige Seite | zur Übersichtsseite | folgende Seite
Letzte Bearbeitung dieser Seite: durch Benutzer:WiseWoman, Zeitstempel: 20160807214801

Auch bei Fandom

Zufälliges Wiki