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Nierenfunktion Kinase-defizienter Mäuse

von Dr. Diana Sandulache

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[1.] Dsa/Fragment 033 00 - Diskussion
Zuletzt bearbeitet: 2016-08-09 20:57:11 WiseWoman
Dsa, Fragment, Gesichtet, KomplettPlagiat, Lang et al 2006, SMWFragment, Schutzlevel sysop

Typus
KomplettPlagiat
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 33, Zeilen: figure+caption
Quelle: Lang et al 2006
Seite(n): 1154, Zeilen: figure
Dsa 033a diss.png

Figure nr. 6 - Left: model for the Serum- and Glucocorticoid-inducible Kinase-1 (SGK1)-dependent regulation of Na+ reabsorption and K+ secretion in the aldosterone-sensitive distal nephron.

Aldosterone binds to mineralocorticoid receptors (MR) and stimulates the expression of SGK1, α-epithelial Na+ channel (αENaC), renal outer medullary K+ channel (ROMK), and the Na+-K+-ATPase. αENaC associates with constitutive β- and γ-subunits to form fully active ENaC. SGK1 can be phosphorylated on 422Ser by insulin or insulin-like growth factor I (IGF-I) through a signaling cascade involving phosphatidylinositol 3-kinase (PI3K) and an unknown kinase (PDK2?/hydrophobic motif kinase). Phosphorylated 422Ser allows binding of PDK1 and/or NHERF2 with subsequent phosphorylation of SGK1 at 256Thr. PDK1 might activate SGK1 indirectly through phosphorylation of WNK1 kinase. The mechanism of SGK1 activation by WNK1 is yet unknown but does not require SGK1 phosphorylation. Activated SGK1 increases Na+ reabsorption in part by phosphorylation of the ubiquitin ligase Nedd4–2, allowing binding of the chaperone 14–3-3 to phosphorylated 444Ser. This interaction prevents Nedd4–2-mediated ubiquitination of the ENaC-PY motif and thus internalization and degradation of ENaC. SGK1 further stimulates ENaC by upregulation of transcription, by direct phosphorylation of the channel protein and by inhibition of the inducible nitric oxide synthase (iNOS). In addition to its effect on ENaC, SGK1 stimulates the Na+-K+-ATPase and K+ channels including ROMK. Right: arithmetic means ± SE of ENaC-induced currents in Xenopus oocytes coexpression experiments showing that coexpression of wild-type SGK1 but not of the inactive mutant K127NSGK1 leads to stimulation of an ENaC mutant lacking the SGK1 phosphorylation consensus sequence (S622AENaC).

Dsa 033a source.png

FIG. 1. Left: model for the Serum- and Glucocorticoid-inducible Kinase-1 (SGK1)-dependent regulation of Na+ reabsorption and K+ secretion in the aldosterone-sensitive distal nephron. Aldosterone binds to mineralocorticoid receptors (MR) and stimulates the expression of SGK1, α-epithelial Na+ channel (αENaC), renal outer medullary K+ channel (ROMK), and the Na+-K+-ATPase. αENaC associates with constitutive β- and γ-subunits to form fully active ENaC. SGK1 can be phosphorylated on 422Ser by insulin or insulin-like growth factor I (IGF-I) through a signaling cascade involving phosphatidylinositol 3-kinase (PI 3K) and an unknown kinase (PDK2?/hydrophobic motif kinase). Phosphorylated 422Ser allows binding of PDK1 and/or NHERF2 with subsequent phosphorylation of SGK1 at 256Thr. PDK1 might activate SGK1 indirectly through phosphorylation of WNK1 kinase. Phosphorylated 422Ser allows binding of PDK1 and/or NHERF2 with subsequent phosphorylation of SGK1 at 256Thr. PDK1 might activate SGK1 indirectly through phosphorylation of WNK1 kinase. The mechanism of SGK1 activation by WNK1 is yet unknown but does not require SGK1 phosphorylation. Activated SGK1 increases Na+ reabsorption in part by phosphorylation of the ubiquitin ligase Nedd4–2, allowing binding of the chaperone 14–3-3 to phosphorylated 444Ser. This interaction prevents Nedd4–2-mediated ubiquitination of the ENaC-PY motif and thus internalization and degradation of ENaC. SGK1 further stimulates ENaC by upregulation of transcription, by direct phosphorylation of the channel protein, and by inhibition of the inducible nitric oxide synthase (iNOS). In addition to its effect on ENaC, SGK1 stimulates the Na+-K+-ATPase and K+ channels including ROMK. Right: arithmetic means ± SE of ENaC-induced currents in Xenopus oocyte coexpression experiments showing that coexpression of wild-type SGK1 but not of the inactive mutant K127NSGK1 leads to stimulation of an ENaC mutant lacking the SGK1 phosphorylation consensus sequence (S622AENaC).

Anmerkungen

The source is not given.

Sichter
(Hindemith), WiseWoman

[2.] Dsa/Fragment 033 01 - Diskussion
Zuletzt bearbeitet: 2016-08-03 17:18:33 WiseWoman
Boini 2006, Dsa, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop

Typus
KomplettPlagiat
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 33, Zeilen: 1-13
Quelle: Boini 2006
Seite(n): 16, Zeilen: 21ff
The stimulatory effect of SGK1 on ENaC is related both to an increased number of channels in the plasma membrane (Lang F. et al., (2000) Proc Natl Acad Sci USA; Loffing J. et al., (2001) Am J Physiol Renal Physiol; Alvarez de la Rosa D. et al., (1999) J Biol Chem) and an activation of channels already present in the membrane (Diakov A. and Korbmacher C., (2004) J Biol Chem). The first effect likely involves the action of Nedd4-2, as there are several consensus phosphorylation motifs (2–3 depending on the splice variant) on Nedd4-2 and a PY-motif on SGK1 that may serve as a binding site for Nedd4-2.

In Xenopus oocytes, SGK1 induces Nedd4-2 phosphorylation on two of these phosphorylation sites (primarily Ser444, but also Ser338) (Embark HM. et al., (2004) Cell Physiol Biochem; Palmada M. et al., (2004) Am J Physiol Gastrointest Liver Physiol; Debonneville C. et al., (2001) EMBO J), which decreases the interaction of Nedd4-2 with ENaC and finally leads to an enhanced expression and activity of ENaC at the cell surface (Debonneville C. et al., (2001) EMBO J).

The stimulatory effect of SGK1 on ENaC is related both to an increased number of channels in the plasma membrane (Lang et al., 2000; Loffing et al., 2001; Alvarez de la Rosa et al., 1999) and an activation of channels already present in the membrane (Diakov and Korbmacher 2004). The first effect likely involves the action of Nedd4-2, as there are several consensus phosphorylation motifs (2–3 depending on the splice variant) on Nedd4-2 and a PY-motif on SGK1 that may serve as a binding site for Nedd4-2. In Xenopus oocytes, SGK1 induces Nedd4-2 phosphorylation on two of these phosphorylation sites (primarily Ser444, but also Ser338) (Embark et al., 2004; Palmada et al., 2004; Debonneville et al., 2001), which decreases the interaction of Nedd4-2 with ENaC and finally leads to an enhanced expression and activity of ENaC at the cell surface (Debonneville et al., 2001).
Anmerkungen

The source is not given.

Sichter
(Hindemith), WiseWoman


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