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Androgen Receptor and PIN1 in Prostate Cancer

von Dott. Raffaele La Montagna

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[1.] Rlm/Fragment 019 01 - Diskussion
Zuletzt bearbeitet: 2014-12-03 07:52:59 Singulus
Fragment, Gesichtet, KomplettPlagiat, Rlm, SMWFragment, Schutzlevel sysop, Wong et al 2004

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KomplettPlagiat
Bearbeiter
Graf Isolan
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Untersuchte Arbeit:
Seite: 19, Zeilen: 1 ff. (entire page)
Quelle: Wong et al 2004
Seite(n): 267-268, Zeilen: 267:right col. 25-42 - 268:left col. 1-2
Furthermore, phosphorylation is correlated with the three AR isoforms that appear on an SDS/polyacrylamide gel (26).

Within minutes after the start of de novo synthesis, the AR appears as a 110 kDa isoform, whereas the generation of the second (112 kDa) isoform appear within 15 min as shown by radioactive methioninelabelling studies. Only after hormone binding does the third (114 kDa) isoform appear. The AR isoform pattern is correlated with AR phosphorylation as was shown in previous studies by using phosphatases. The dephosphorylation of AR by phosphatases resulted in the loss of one isoform either in the presence or absence of hormone . This effect was also observed when AR phosphosites were mutated . Furthermore, several phosphorylation sites have been identified. The first identified phosphosites, Ser-81, Ser-94 and Ser-650, were found by mutagenesis analyses in combination with SDS/PAGE (27). Ser-308 was the first phosphosite identified by mutagenesis and MS Ser-16, Ser-81, Ser-94, Ser-256, Ser-308, Ser- 424 and Ser-650 were all identified and confirmed as phosphosites by mutagenesis, peptide mapping and MS (28).


26) Jenster, G., de Ruiter, P. E., van der Korput, H. A., Kuiper, G. G., Trapman, J. and Brinkmann, A. O. (1994) Changes in the abundance of androgen receptor isotypes: effects of ligand treatment, glutamine-stretch variation, and mutation of putative phosphorylation sites. Biochemistry 33, 14064–14072.

27) ). [sic] Zhou, Z. X., Kemppainen, J. A. and Wilson, E. M. (1995) Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol. Endocrinol. 9, 605–615

28) Zhu, Z., Becklin, R. R., Desiderio, D. M. and Dalton, J. T. (2001) Identification of a novel phosphorylation site in human androgen receptor by mass spectrometry. Biochem. Biophys. Res. Commun. 284, 836–844.

38) Gioeli, D., Ficarro, S. B., Kwiek, J. J., Aaronson, D., Hancock, M., Catling, A. D., White, F. M., Christian, R. E., Settlage, R. E., Shabanowitz, J., Hunt, D. F., and Weber, M. J. (2002) Androgen receptor phosphorylation. Regulation and identification of the phosphorylation sites. J. Biol. Chem. 277, 29304–29314.].

[Page 267]

Furthermore, phosphorylation is correlated with the three AR isoforms that appear on an SDS/polyacrylamide gel [19]. Within minutes after the start of de novo synthesis, the AR appears as a 110 kDa isoform, whereas generation of the second (112 kDa) isoform follows within 15 min as shown by radioactive methioninelabelling studies [20,21]. Only after hormone binding does the third (114 kDa) isoform appear [19]. The AR isoform pattern is correlated with AR phosphorylation as was shown in previous studies by using phosphatases. The dephosphorylation of AR by phosphatases resulted in the loss of one isoform either in the presence or absence of hormone [19]. This effect was also observed when AR phosphosites were mutated [19]. Furthermore, several phosphorylation sites have been identified. The first identified phosphosites, Ser-81, Ser-94 and Ser-650, were found by mutagenesis analyses in combination with SDS/PAGE [19,22]. Ser-308 was the first phosphosite identified by mutagenesis and MS [23]. Ser-16, Ser-81, Ser-94, Ser-256, Ser-308, Ser-424

[Page 268]

and Ser-650 were all identified and confirmed as phosphosites by mutagenesis, peptide mapping and MS [16].


16 Gioeli, D., Ficarro, S. B., Kwiek, J. J., Aaronson, D., Hancock, M., Catling, A. D., White, F. M., Christian, R. E., Settlage, R. E., Shabanowitz, J. et al. (2002) Androgen receptor phosphorylation. Regulation and identification of the phosphorylation sites. J. Biol. Chem. 277, 29304–29314

19 Jenster, G., de Ruiter, P. E., van der Korput, H. A., Kuiper, G. G., Trapman, J. and Brinkmann, A. O. (1994) Changes in the abundance of androgen receptor isotypes: effects of ligand treatment, glutamine-stretch variation, and mutation of putative phosphorylation sites. Biochemistry 33, 14064–14072

20 Kuiper, G. G., de Ruiter, P. E., Grootegoed, J. A. and Brinkmann, A. O. (1991) Synthesis and post-translational modification of the androgen receptor in LNCaP cells. Mol. Cell. Endocrinol. 80, 65–73

21 Kuiper, G. G., de Ruiter, P. E. and Brinkmann, A. O. (1992) Androgen receptor heterogeneity in LNCaP cells is caused by a hormone independent phosphorylation step. J. Steroid Biochem. Mol. Biol. 41, 697–700

22 Zhou, Z. X., Kemppainen, J. A. and Wilson, E. M. (1995) Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol. Endocrinol. 9, 605–615

23 Zhu, Z., Becklin, R. R., Desiderio, D. M. and Dalton, J. T. (2001) Identification of a novel phosphorylation site in human androgen receptor by mass spectrometry. Biochem. Biophys. Res. Commun. 284, 836–844

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Sichter
(Graf Isolan), SleepyHollow02


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