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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 024 01 - Diskussion
Zuletzt bearbeitet: 2014-12-01 17:22:47 Singulus
Fragment, Gesichtet, KomplettPlagiat, Rlm, SMWFragment, Schutzlevel sysop, Ward and Weigel 2009

Typus
KomplettPlagiat
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 24, Zeilen: 1 ff. (entire page)
Quelle: Ward and Weigel 2009
Seite(n): 6, 7 (author manuscript), Zeilen: 6: last paragraph; 7: 1 ff.
Several studies have suggested that AKT-mediated phosphorylation of Ser213 and Ser791 (numbered based on an AR length of 919 amino acids) reduces AR activity (40). Mutation of the AR Ser213 to alanine caused resistance to AKT-mediated suppression of activity in DU145 cells(41) . Palazzolo et al. found that substituting alanines for both of the sites also prevented AKT-mediated inhibition of AR transcriptional activity. Surprisingly, substitution of aspartic acids at either site blocked hormone binding and, therefore, ligand-dependent AR protein stabilization, ligand-mediated translocation, and AR transcriptional activity(42).

The remaining sites in the AR NTD domain also have been shown to have important functional roles. When a fragment of the androgen receptor (amino acids 507-660) is expressed, Ser515 and Ser578 are phosphorylated in response to EGF treatment(43).

The AR Ser515Ala mutation exhibited a more severe phenotype than the Ser578Ala and the double mutant displayed little to no activity; furthermore, EGF treatment had no effect on the activity of this mutant.


40) Wen, Y., Hu, M. C., Makino, K., Spohn, B., Bartholomeusz, G., Yan, D. H., and Hung, M. C. (2000) HER-2/neu promotes androgenindependent survival and growth of prostate cancer cells through the Akt pathway. Cancer Res. 60, 6841–6845..

41) Taneja, S. S., Ha, S., Swenson, N. K., Huang, H. Y., Lee, P., Melamed, J., Shapiro, E., Garabedian, M. J., and Logan, S. K. (2005) Cell-specific regulation of androgen receptor phosphorylation in vivo. J. Biol. Chem. 280, 40916–40924..

42) Palazzolo, I., Burnett, B. G., Young, J. E., Brenne, P. L., La Spada, A. R., Fischbeck, K. H., Howell, B. W., and Pennuto, M. (2007) Akt blocks ligand binding and protects against expanded polyglutamine androgen receptor toxicity. Hum. Mol. Genet. 16, 1593–1603.

43) Ponguta, L. A., Gregory, C. W., French, F. S., and Wilson, E. M. (2008) Site-specific androgen receptor serine phosphorylation linked to epidermal growth factor-dependent growth of castration-recurrent prostate cancer. J. Biol. Chem. 283, 20989–21001.

Several studies have suggested that AKT mediated phosphorylation of Ser213 and Ser791 (numbered based on an AR length of 919 amino acids) reduces AR activity. Both sites are phosphorylated by the P13K/Akt signaling pathways (62-64). Mutation of the AR Ser213 to alanine caused AR to be resistant to AKT mediated suppression of activity in DU145 cells (64,65). Palazzolo et al found that substituting alanines for both of the sites also prevented

[page 7]

AKT mediated inhibition of AR transcriptional activity. Surprisingly, substitution of aspartic acids at either site blocked hormone binding and, therefore, ligand dependent AR protein stabilization, ligand-mediated translocation, and AR transcriptional activity (66).

The remaining sites in the AR NTD also have been shown to have important functional roles. When a fragment of the androgen receptor (amino acids 507-660) is expressed, Ser515 and Ser578 are phosphorylated in response to EGF treatment (67). The AR Ser515Ala mutation exhibited a more severe phenotype than the Ser578Ala and the double mutant displayed little to no activity; furthermore, EGF treatment had no effect on the activity of this mutant.


62. Wen Y, Hu MC, Makino K, Spohn B, Bartholomeusz G, Yan DH, Hung MC. HER-2/neu promotes androgen-independent survival and growth of prostate cancer cells through the Akt pathway. Cancer Res. 2000; 60:6841–6845. [PubMed: 11156376]

63. Taneja SS, Ha S, Swenson NK, Huang HY, Lee P, Melamed J, Shapiro E, Garabedian MJ, Logan SK. Cell-specific regulation of androgen receptor phosphorylation in vivo. J Biol Chem. 2005; 280:40916–40924. [PubMed: 16210317]

64. Lin HK, Yeh S, Kang HY, Chang C. Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor. Proc Natl Acad Sci U S A. 2001; 98:7200– 7205. [PubMed: 11404460]

65. Lin HK, Hu YC, Yang L, Altuwaijri S, Chen YT, Kang HY, Chang C. Suppression versus induction of androgen receptor functions by the phosphatidylinositol 3-kinase/Akt pathway in prostate cancer LNCaP cells with different passage numbers. J Biol Chem. 2003; 278:50902– 50907. [PubMed: 14555644]

66. Palazzolo I, Burnett BG, Young JE, Brenne PL, La Spada AR, Fischbeck KH, Howell BW, Pennuto M. Akt blocks ligand binding and protects against expanded polyglutamine androgen receptor toxicity. Hum Mol Genet. 2007; 16:1593–1603. [PubMed: 17470458]

67. Ponguta LA, Gregory CW, French FS, Wilson EM. Site-specific androgen receptor serine phosphorylation linked to epidermal growth factor-dependent growth of castration-recurrent prostate cancer. J Biol Chem. 2008; 283:20989–21001. [PubMed: 18511414]

Anmerkungen

The source is not mentioned.

Sichter
(Hindemith), SleepyHollow02


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