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Angaben zur Quelle [Bearbeiten]

Autor     Hao Yun Wong, Jan A Burghoorn, Marije Van Leeuwen, Petra E De Ruiter, Esther Schippers, Leen J Blok, Ka Wan Li, Henk L Dekker, Luitzen De Jong, Jan Trapman, J Anton Grootegoed, Albert O Brinkmann
Titel    Phosphorylation of androgen receptor isoforms
Zeitschrift    Biochem. J
Ausgabe    383 (Pt 2)
Datum    October 2004
Seiten    267-276
Anmerkung    Published as BJ Immediate Publication 8 July 2004
DOI    10.1042/BJ20040683
URL    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1134067/pdf/bj3830267.pdf

Literaturverz.   

yes
Fußnoten    yes
Fragmente    2


Fragmente der Quelle:
[1.] Rlm/Fragment 018 05 - Diskussion
Zuletzt bearbeitet: 2014-12-03 07:53:56 Singulus
Fragment, Gesichtet, KomplettPlagiat, Rlm, SMWFragment, Schutzlevel sysop, Wong et al 2004

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KomplettPlagiat
Bearbeiter
Graf Isolan
Gesichtet
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Untersuchte Arbeit:
Seite: 18, Zeilen: 5-13, 19
Quelle: Wong et al 2004
Seite(n): 267, Zeilen: right col. 16-25
Post-translational modifications such as acetylation and sumoylation have been shown to influence the transactivation potential of the AR (19,20). However, it is not clear whether phosphorylation has an effect on the properties and activity of the AR. It has been shown that the AR is a phosphoprotein (21,22) and extra phosphorylation of the AR is induced when cells are exposed to androgens, in addition to the so-called basal AR phosphorylation observed in the absence of androgens(23). Phosphorylation occurs predominantly at serine residues, which are mainly located in the N-terminal domain.

[...] (24,25).


19) Fu, M., Wang, C., Wang, J., Zhang, X., Sakamaki, T., Yeung, Y. G., Chang, C., Hopp, T., Fuqua, S. A., Jaffray, E. et al. (2002) Androgen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function. Mol. Cell. Biol. 22, 3373–3388

20) Poukka, H., Karvonen, U., Janne, O. A. and Palvimo, J. J. (2000) Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. U.S.A. 97, 14145–14150

21) van Laar, J. H., Bolt-de Vries, J., Zegers, N. D., Trapman, J. and Brinkmann, A. O. (1990) Androgen receptor heterogeneity and phosphorylation in human LNCaP cells. Biochem. Biophys. Res. Commun. 166, 193–200

22) van Laar, J. H., Berrevoets, C. A., Trapman, J., Zegers, N. D. and Brinkmann, A. O. (1991) Hormone-dependent androgen receptor phosphorylation is accompanied by receptor transformation in human lymph node carcinoma of the prostate cells. J. Biol. Chem. 266, 3734–3738

23) 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.

24) Kuiper, G. G. and Brinkmann, A. O. (1995) Phosphotryptic peptide analysis of the human androgen receptor: detection of a hormone-induced phosphopeptide. Biochemistry 34, 1851–1857

25) Kuiper, G. G., de Ruiter, P. E., Trapman, J., Boersma, W. J., Grootegoed, J. A. and Brinkmann, A. O. (1993) Localization and hormonal stimulation of phosphorylation sites in the LNCaP-cell androgen receptor. Biochem. J. 291, 95–101

Post-translational modifications such as acetylation and sumoylation have been shown to influence the transactivation potential of the AR [12,13]. However, it is not clear whether phosphorylation has an effect on the properties and activity of the AR. It has been shown that the AR is a phosphoprotein [14,15] and extra phosphorylation of the AR is induced when cells are exposed to androgens, in addition to the so-called basal AR phosphorylation observed in the absence of androgens [15,16]. Phosphorylation occurs predominantly at serine residues [16,17], which are mainly located in the N-terminal domain [18].

12 Fu, M., Wang, C., Wang, J., Zhang, X., Sakamaki, T., Yeung, Y. G., Chang, C., Hopp, T., Fuqua, S. A., Jaffray, E. et al. (2002) Androgen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function. Mol. Cell. Biol. 22, 3373–3388

13 Poukka, H., Karvonen, U., Janne, O. A. and Palvimo, J. J. (2000) Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. U.S.A. 97, 14145–14150

14 van Laar, J. H., Bolt-de Vries, J., Zegers, N. D., Trapman, J. and Brinkmann, A. O. (1990) Androgen receptor heterogeneity and phosphorylation in human LNCaP cells. Biochem. Biophys. Res. Commun. 166, 193–200

15 van Laar, J. H., Berrevoets, C. A., Trapman, J., Zegers, N. D. and Brinkmann, A. O. (1991) Hormone-dependent androgen receptor phosphorylation is accompanied by receptor transformation in human lymph node carcinoma of the prostate cells. J. Biol. Chem. 266, 3734–3738

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

17 Kuiper, G. G. and Brinkmann, A. O. (1995) Phosphotryptic peptide analysis of the human androgen receptor: detection of a hormone-induced phosphopeptide. Biochemistry 34, 1851–1857

18 Kuiper, G. G., de Ruiter, P. E., Trapman, J., Boersma, W. J., Grootegoed, J. A. and Brinkmann, A. O. (1993) Localization and hormonal stimulation of phosphorylation sites in the LNCaP-cell androgen receptor. Biochem. J. 291, 95–101

Anmerkungen

Identical, with identical references. Nothing has been marked as a citation.

Sichter
(Graf Isolan), SleepyHollow02

[2.] 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
Gesichtet
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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

Anmerkungen

Nothing has been marked as a citation.

Sichter
(Graf Isolan), SleepyHollow02

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