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Androgen Receptor and PIN1 in Prostate Cancer

von Dott. Raffaele La Montagna

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[1.] 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

Typus
Verschleierung
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 49, Zeilen: 1-11
Quelle: Bao et al 2004
Seite(n): 1727, Zeilen: r. col: 11 ff.
[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

[...]

Anmerkungen

The source is not mentioned.

Sichter
(Hindemith), SleepyHollow02

[2.] Rlm/Fragment 049 11 - Diskussion
Zuletzt bearbeitet: 2014-12-01 17:29:01 Singulus
BauernOpfer, Fragment, Gesichtet, Gioeli et al 2006, Rlm, SMWFragment, Schutzlevel sysop

Typus
BauernOpfer
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 49, Zeilen: 11-20
Quelle: Gioeli et al 2006
Seite(n): 503, 504, Zeilen: 503: r.col: last line; 504: l.col: 1 ff.
Diverse agonists including activators of protein kinase A (forskolin) and protein kinase C [phorbol-12-myristate-13-acetate (PMA)] increased Ser 650 phosphorylation. Ser 650 phosphorylation occurs by both hormone-dependent and hormone- independent mechanisms (androgen, protein kinase A, EGF, and protein kinase C) suggest that modification of this site might be used to regulate steroid receptor function in response to a variety of physiological stimuli. Gioeli et al. have investigated which signal transduction pathways regulate Ser 650 phosphorylation and determined the effect of these signaling pathways on AR function. Notably, diverse agonists

[page 504]

including activators of protein kinase A (forskolin) and protein kinase C [phorbol-12-myristate-13-acetate (PMA)] increased Ser 650 phosphorylation (15). [...] The fact that Ser 650 phosphorylation occurs by both hormone-dependent and hormone-independent mechanisms (androgen, protein kinase A, EGF, and protein kinase C) suggest that modification of this site might be used to regulate steroid receptor function in response to a variety of physiological stimuli.

[...] In this study, we have investigated which signal transduction pathways regulate Ser 650 phosphorylation and determined the effect of these signaling pathways on AR function.

Anmerkungen

The source is mentioned in the text, but not in a way that suggests to the reader that even the text before is taken from it literally.

Sichter
(Hindemith), SleepyHollow02


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