von Dr. Diana Sandulache
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| [1.] Dsa/Fragment 045 01 - Diskussion Zuletzt bearbeitet: 2016-08-07 10:40:42 WiseWoman | Dsa, Fragment, Gesichtet, Hoenderop et al 2003, KomplettPlagiat, SMWFragment, Schutzlevel sysop |
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| Untersuchte Arbeit: Seite: 45, Zeilen: 1-5 |
Quelle: Hoenderop et al 2003 Seite(n): 1907, Zeilen: l.col: 19ff |
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| TRPV5 and TRPV6 are Ca2+- selective channels that belong, together with the temperature-activated vanilloid receptors, to the TRPV subfamily. Genomic cloning has demonstrated that TRPV5 and TRPV6 form a unique pair of novel Ca2+ channels that are transcribed from distinct genes juxtaposed on human chromosome 7q35. | TRPV5 and TRPV6 are Ca2+-selective channels that belong, together with the temperature-activated vanilloid receptors, to the TRPV subfamily (3, 4). Genomic cloning has demonstrated that TRPV5 and TRPV6 form a unique pair of novel Ca2+ channels that are transcribed from distinct genes juxtaposed on human chromosome 7q35 (4).
3. Montell, C., Birnbaumer, L., and Flockerzi, V. 2002. The TRP channels, a remarkably functional family. Cell. 108:595–598. 4. Hoenderop, J.G., Nilius, B., and Bindels, R.J. 2002. Molecular mechanisms of active Ca2+ reabsorption in the distal nephron. Ann. Rev. Physiol. 64:529–549. |
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| [2.] Dsa/Fragment 045 06 - Diskussion Zuletzt bearbeitet: 2016-08-09 21:02:38 WiseWoman | Dsa, Fragment, Gesichtet, KomplettPlagiat, Lang et al 2006, SMWFragment, Schutzlevel sysop |
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| Untersuchte Arbeit: Seite: 45, Zeilen: 6-12 |
Quelle: Lang et al 2006 Seite(n): 1156, Zeilen: r.col: 16ff |
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| As shown in Xenopus oocytes, SGK1 and SGK3 activate the renal epithelial Ca2+ channel TRPV5 by enhancing channel abundance in the plasma membrane, an effect again requiring cooperation with NHERF2 (Embark HM. et al., (2004) Cell Physiol Biochem; Palmada M. et al., (2005) Cell Physiol Biochem). The TRPV5 C-tail interacts in a Ca2+- independent manner with NHERF2. Deletion of the second, but not the first, PDZ domain in NHERF2 abrogates the stimulating effect of SGK1 on TRPV5 protein abundance (Palmada M. et al., (2005) Cell Physiol Biochem). | As shown in Xenopus oocytes, SGK1 and SGK3 activate the renal epithelial Ca2+ channel TRPV5 by enhancing channel abundance in the plasma membrane, an effect again requiring cooperation with NHERF2 (101, 246). The TRPV5 C-tail interacts in a Ca2+-independent manner with NHERF2. Deletion of the second, but not the first, PDZ domain in NHERF2 abrogates the stimulating effect of SGK1 on TRPV5 protein abundance (246).
101. Embark HM, Setiawan I, Poppendieck S, van de Graaf SF, Boehmer C, Palmada M, Wieder T, Gerstberger R, Cohen P, Yun CC, Bindels RJ, and Lang F. Regulation of the epithelial Ca2+ channel TRPV5 by the NHE regulating factor NHERF2 and the serum and glucocorticoid inducible kinase isoforms SGK1 and SGK3 expressed in Xenopus oocytes. Cell Physiol Biochem 14: 203–212, 2004. 246. Palmada M, Poppendieck S, Embark HM, van de Graaf SF, Boehmer C, Bindels RJ, and Lang F. Requirement of PDZ domains for the stimulation of the epithelial Ca2+ channel TRPV5 by the NHE regulating factor NHERF2 and the serum and glucocorticoid inducible kinase SGK1. Cell Physiol Biochem 15: 175–182, 2005. |
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Letzte Bearbeitung dieser Seite: durch Benutzer:WiseWoman, Zeitstempel: 20160809215047