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Androgen Receptor and PIN1 in Prostate Cancer

von Dott. Raffaele La Montagna

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Statistik und Sichtungsnachweis dieser Seite findet sich am Artikelende
[1.] Rlm/Fragment 027 01 - Diskussion
Zuletzt bearbeitet: 2014-12-01 17:25:28 Singulus
Fragment, Gesichtet, KomplettPlagiat, Rlm, SMWFragment, Schutzlevel sysop, Ward and Weigel 2009

Typus
KomplettPlagiat
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 27, Zeilen: 1 ff. (entire page)
Quelle: Ward and Weigel 2009
Seite(n): 7 (author manuscript), Zeilen: 35 ff.
The Tyr534Phe mutant also exhibited reduced activity and DNA binding at low doses of ligand and defective nuclear translocation in response to various stimuli . Finally, Tyr534Phe mutant expression caused growth inhibition in both cell lines and tumor xenografts containing the Tyr534Phe mutant grew more slowly than tumors expressing WT AR in castrated mice, thereby demonstrating a role for Tyr534 phosphorylation in prostate cancer cell growth under androgen-depleted conditions. Two additional tyrosine phosphorylation sites have been identified in cells treated with heregulin or transfected with constitutively active Ack (Cdc42 associated kinase).

Mutation of these sites, Tyr267 and Tyr363 to phenylalanine (Tyr267Phe and Tyr363Phe, respectively), reduced Ackinduced reporter activation and recruitment to the enhancer, thus demonstrating the importance of these sites in AR basal and liganddependent activity as well as in potentiation of AR activity by kinase signaling. In addition, substituting Phe at both of these sites also reduced tumor growth of Ack-driven tumor xenografts in castrated nude mice.

The Tyr534Phe mutant also exhibited reduced activity and DNA binding at low doses of ligand and defective nuclear translocation in response to various stimuli (71). Finally, Tyr534Phe mutant expression caused growth inhibition in both cell lines and tumor xenografts containing the Tyr534Phe mutant grew more slowly than tumors expressing WT AR in castrated mice, thereby demonstrating a role for Tyr534 phosphorylation in prostate cancer cell growth under androgen-depleted conditions (71). Two additional tyrosine phosphorylation sites have been identified in cells treated with heregulin or transfected with constitutively active Ack (Cdc42 associated kinase) (72). Mutation of these sites, Tyr267 and Tyr363 to phenylalanine (Tyr267Phe and Tyr363Phe, respectively), reduced Ack-induced reporter activation and recruitment to the enhancer, thus demonstrating the importance of these sites in AR basal and liganddependent activity as well as in potentiation of AR activity by kinase signaling (72). In addition, substituting Phe at both of these sites also reduced tumor growth of Ack-driven tumor xenografts in castrated nude mice (72).

71. Guo Z, Dai B, Jiang T, Xu K, Xie Y, Kim O, Nesheiwat I, Kong X, Melamed J, Handratta VD, Njar VC, Brodie AM, Yu LR, Veenstra TD, Chen H, Qiu Y. Regulation of androgen receptor activity by tyrosine phosphorylation. Cancer Cell. 2006; 10:309–319. [PubMed: 17045208]

72. Mahajan NP, Liu Y, Majumder S, Warren MR, Parker CE, Mohler JL, Earp HS, Whang YE. Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation. Proc Natl Acad Sci U S A. 2007; 104:8438–8443. [PubMed: 17494760]

Anmerkungen

The source is not mentioned.

Sichter
(Hindemith), SleepyHollow02


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