Research ExplorerPublicationsTemperature sensitivity of phospho-Ser(473)-PKB/AKT.

Temperature sensitivity of phospho-Ser(473)-PKB/AKT.

Standard

Temperature sensitivity of phospho-Ser(473)-PKB/AKT. / Oehler-Jänne, Christoph; von Bueren, André; André, O; Vuong, Van; Hollenstein, Andreas; Grotzer, Michael A; Pruschy, Martin.

In: BIOCHEM BIOPH RES CO, Vol. 375, No. 3, 3, 2008, p. 399-404.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Oehler-Jänne, C, von Bueren, A, André, O, Vuong, V, Hollenstein, A, Grotzer, MA & Pruschy, M 2008, 'Temperature sensitivity of phospho-Ser(473)-PKB/AKT.', BIOCHEM BIOPH RES CO, vol. 375, no. 3, 3, pp. 399-404. <http://www.ncbi.nlm.nih.gov/pubmed/18721797?dopt=Citation>

APA

Oehler-Jänne, C., von Bueren, A., André, O., Vuong, V., Hollenstein, A., Grotzer, M. A., & Pruschy, M. (2008). Temperature sensitivity of phospho-Ser(473)-PKB/AKT. BIOCHEM BIOPH RES CO, 375(3), 399-404. [3]. http://www.ncbi.nlm.nih.gov/pubmed/18721797?dopt=Citation

Vancouver

Oehler-Jänne C, von Bueren A, André O, Vuong V, Hollenstein A, Grotzer MA et al. Temperature sensitivity of phospho-Ser(473)-PKB/AKT. BIOCHEM BIOPH RES CO. 2008;375(3):399-404. 3.

Bibtex

@article{0952cf75c018420ca75b9b7f7a27e03c,
title = "Temperature sensitivity of phospho-Ser(473)-PKB/AKT.",
abstract = "The phospho-PKB/Akt status is often used as surrogate marker to measure activation of the PI3K/Akt/mTOR signal transduction pathway. Though, inconsistencies of the p-Ser(473)-PKB/Akt status have raised doubts in the validity of p-Ser(473)-PKB/Akt phosphorylation as endpoint. Here, we determined that p-Ser(473)-PKB/Akt but not p-Thr(308)-PKB/Akt phosphorylation is highly temperature sensitive. p-Ser(473)-PKB/Akt phosphorylation was rapidly reduced to levels below 50% on exposure to 20-25 degrees C in murine and human cell lines including cells expressing constitutively active PI3K or lacking PTEN. Down-regulation of p-Ser(473)-PKB/Akt was reversible and re-exposure to physiological temperature resulted in increased p-Ser(473)-PKB/Akt phosphorylation levels. Phosphatase activity at low temperature was sustained at 75% baseline level and phosphatase inhibition prevented p-Ser(473)-PKB/Akt dephosphorylation induced by the low temperature shift. Interestingly temperature-dependent deregulation of the p-Ser(473)-PKB/Akt status was also observed in response to irradiation. Thus our data demonstrate that minimal additional stress factors deregulate the PI3K/Akt-survival pathway and the p-Ser(473)-PKB/Akt status as experimental endpoint.",
author = "Christoph Oehler-J{\"a}nne and {von Bueren}, Andr{\'e} and O Andr{\'e} and Van Vuong and Andreas Hollenstein and Grotzer, {Michael A} and Martin Pruschy",
year = "2008",
language = "Deutsch",
volume = "375",
pages = "399--404",
journal = "BIOCHEM BIOPH RES CO",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

RIS

TY - JOUR

T1 - Temperature sensitivity of phospho-Ser(473)-PKB/AKT.

AU - Oehler-Jänne, Christoph

AU - von Bueren, André

AU - André, O

AU - Vuong, Van

AU - Hollenstein, Andreas

AU - Grotzer, Michael A

AU - Pruschy, Martin

PY - 2008

Y1 - 2008

N2 - The phospho-PKB/Akt status is often used as surrogate marker to measure activation of the PI3K/Akt/mTOR signal transduction pathway. Though, inconsistencies of the p-Ser(473)-PKB/Akt status have raised doubts in the validity of p-Ser(473)-PKB/Akt phosphorylation as endpoint. Here, we determined that p-Ser(473)-PKB/Akt but not p-Thr(308)-PKB/Akt phosphorylation is highly temperature sensitive. p-Ser(473)-PKB/Akt phosphorylation was rapidly reduced to levels below 50% on exposure to 20-25 degrees C in murine and human cell lines including cells expressing constitutively active PI3K or lacking PTEN. Down-regulation of p-Ser(473)-PKB/Akt was reversible and re-exposure to physiological temperature resulted in increased p-Ser(473)-PKB/Akt phosphorylation levels. Phosphatase activity at low temperature was sustained at 75% baseline level and phosphatase inhibition prevented p-Ser(473)-PKB/Akt dephosphorylation induced by the low temperature shift. Interestingly temperature-dependent deregulation of the p-Ser(473)-PKB/Akt status was also observed in response to irradiation. Thus our data demonstrate that minimal additional stress factors deregulate the PI3K/Akt-survival pathway and the p-Ser(473)-PKB/Akt status as experimental endpoint.

AB - The phospho-PKB/Akt status is often used as surrogate marker to measure activation of the PI3K/Akt/mTOR signal transduction pathway. Though, inconsistencies of the p-Ser(473)-PKB/Akt status have raised doubts in the validity of p-Ser(473)-PKB/Akt phosphorylation as endpoint. Here, we determined that p-Ser(473)-PKB/Akt but not p-Thr(308)-PKB/Akt phosphorylation is highly temperature sensitive. p-Ser(473)-PKB/Akt phosphorylation was rapidly reduced to levels below 50% on exposure to 20-25 degrees C in murine and human cell lines including cells expressing constitutively active PI3K or lacking PTEN. Down-regulation of p-Ser(473)-PKB/Akt was reversible and re-exposure to physiological temperature resulted in increased p-Ser(473)-PKB/Akt phosphorylation levels. Phosphatase activity at low temperature was sustained at 75% baseline level and phosphatase inhibition prevented p-Ser(473)-PKB/Akt dephosphorylation induced by the low temperature shift. Interestingly temperature-dependent deregulation of the p-Ser(473)-PKB/Akt status was also observed in response to irradiation. Thus our data demonstrate that minimal additional stress factors deregulate the PI3K/Akt-survival pathway and the p-Ser(473)-PKB/Akt status as experimental endpoint.

M3 - SCORING: Zeitschriftenaufsatz

VL - 375

SP - 399

EP - 404

JO - BIOCHEM BIOPH RES CO

JF - BIOCHEM BIOPH RES CO

SN - 0006-291X

IS - 3

M1 - 3

ER -