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Autor | Lere Bao, Amy Kimzey, Guido Sauter, Janusz M. Sowadski, Kun Ping Lu, Da-Gong Wang |
Titel | Prevalent Overexpression of Prolyl Isomerase Pin1 in Human Cancers |
Zeitschrift | American Journal of Pathology |
Ausgabe | 164 |
Datum | May 2004 |
Nummer | 5 |
Seiten | 1727-1737 |
URL | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1615639/pdf/JPATH164001727.pdf |
Literaturverz. |
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Fußnoten | no |
Fragmente | 3 |
[1.] Rlm/Fragment 030 01 - Diskussion Zuletzt bearbeitet: 2014-12-01 17:31:44 Singulus | Bao et al 2004, Fragment, Gesichtet, Rlm, SMWFragment, Schutzlevel sysop, Verschleierung |
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Pin1 is normally expressed at very low levels in most normal tissues, although significant levels of Pin1 are often found in cell types that normally undergo active cell division. Pin1 is overexpressed in some human malignancies and that its expression closely correlates with the level of cyclin D1 in human breast cancer (54).
54) Wulf, G. M., Ryo, A., Wulf, G. G., Lee, S. W., Niu, T., and Lu, K. P. Pin1 is overexpressed in breast cancer and potentiates the transcriptional activity of phosphorylatedc-Jun towards the cyclin D1 gene. EMBO J., 20: 3459–3472, 2001. |
Recently, it has been reported that Pin1 is overexpressed in human breast cancer cell lines and breast cancer tissues, and its expression closely correlates with the level of cyclin D1 in tumors.15
[page 1731] These results indicate that Pin1 is normally expressed at very low levels in most normal tissues, although significant levels of Pin1 are often found in cell types that normally undergo active cell division. 15. Wulf GM, Ryo A, Wulf GG, Lee SW, Niu T, Lu KP: Pin1 is overexpressed in breast cancer and potentiates the transcriptional activity of phosphorylated c-Jun towards the cyclin D1 gene. EMBO J 2001, 20:3459–3472 |
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[2.] Rlm/Fragment 048 01 - Diskussion Zuletzt bearbeitet: 2014-12-01 16:33:13 SleepyHollow02 | Bao et al 2004, Fragment, Gesichtet, KeineWertung, Rlm, SMWFragment, Schutzlevel |
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Recently, it has been reported that Pin1 is overexpressed in human prostate cancer cell lines and prostate cancer tissues, and its expression closely correlates with the level of cyclin D1 in tumors. | Recently, it has been reported that Pin1 is overexpressed in human breast cancer cell lines and breast cancer tissues, and its expression closely correlates with the level of cyclin D1 in tumors.15
15. Wulf GM, Ryo A, Wulf GG, Lee SW, Niu T, Lu KP: Pin1 is overexpressed in breast cancer and potentiates the transcriptional activity of phosphorylated c-Jun towards the cyclin D1 gene. EMBO J 2001, 20:3459–3472 |
The source is not mentioned. By copying the passage from a seven year old source, the meaning of "recently" is somewhat stretched. |
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[3.] Rlm/Fragment 049 01 - Diskussion Zuletzt bearbeitet: 2015-02-08 20:46:57 Schumann | Bao et al 2004, Fragment, Gesichtet, Rlm, SMWFragment, Schutzlevel sysop, Verschleierung |
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[It is well known that one major regulatory] mechanism in cell proliferation and transformation is phosphorylation of proteins on serine or threonine residues preceding proline (pSer/Thr- Pro) by various prodirected protein kinases, such as MAP kinases, cyclin-dependent kinases, JNK, and GSK3β. Interestingly, the pSer/Thr-Pro motifs in proteins exist in two completely distinct cis and trans conformations, whose conversion is normally restrained by phosphorylation, but catalyzed specifically by the essential prolyl isomerase Pin1. By isomerizing pSer81, Pin1 induce conformational changes in androgen receptor. This, phosphorylation- dependent prolyl isomerization is a critical mechanism in phosphorylation signaling. | One major regulatory mechanism in cell proliferation and transformation is phosphorylation of proteins on serine or threonine residues preceding proline (pSer/Thr- Pro) by various prodirected protein kinases, such as MAP kinases, cyclin-dependent kinases, JNK, and GSK3β.1–3 Interestingly, the pSer/Thr-Pro motifs in proteins exist in two completely distinct cis and trans conformations, whose conversion is normally restrained by phosphorylation, but catalyzed specifically by the essential prolyl isomerase Pin1.3–6 By isomerizing specific pSer/Thr-Pro bonds, Pin1 has been shown to catalytically induce conformational changes in proteins after phosphorylation, thereby having profound effects on their catalytic activity, dephosphorylation, protein-protein interactions, subcellular location, and/or turnover.4,5,7–18 Thus, phosphorylation- dependent prolyl isomerization is a critical postphosphorylation regulatory mechanism in phosphorylation signaling.3
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