Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells

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Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells. / Suchankova, Gabriela; Nelson, Lauren E.; Gerhart-Hines, Zachary; Kelly, Meghan; Gauthier, Marie Soleil; Saha, Asish K.; Ido, Yasuo; Puigserver, Pere; Ruderman, Neil B.

In: Biochemical and Biophysical Research Communications, Vol. 378, No. 4, 23.01.2009, p. 836-841.

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

Harvard

Suchankova, G, Nelson, LE, Gerhart-Hines, Z, Kelly, M, Gauthier, MS, Saha, AK, Ido, Y, Puigserver, P & Ruderman, NB 2009, 'Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells', Biochemical and Biophysical Research Communications, vol. 378, no. 4, pp. 836-841. https://doi.org/10.1016/j.bbrc.2008.11.130

APA

Suchankova, G., Nelson, L. E., Gerhart-Hines, Z., Kelly, M., Gauthier, M. S., Saha, A. K., Ido, Y., Puigserver, P., & Ruderman, N. B. (2009). Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells. Biochemical and Biophysical Research Communications, 378(4), 836-841. https://doi.org/10.1016/j.bbrc.2008.11.130

Vancouver

Suchankova G, Nelson LE, Gerhart-Hines Z, Kelly M, Gauthier MS, Saha AK et al. Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells. Biochemical and Biophysical Research Communications. 2009 Jan 23;378(4):836-841. https://doi.org/10.1016/j.bbrc.2008.11.130

Author

Suchankova, Gabriela ; Nelson, Lauren E. ; Gerhart-Hines, Zachary ; Kelly, Meghan ; Gauthier, Marie Soleil ; Saha, Asish K. ; Ido, Yasuo ; Puigserver, Pere ; Ruderman, Neil B. / Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells. In: Biochemical and Biophysical Research Communications. 2009 ; Vol. 378, No. 4. pp. 836-841.

Bibtex

@article{240ed2bf565e4f7cb4e488ef148867df,
title = "Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells",
abstract = "We examined in HepG2 cells whether glucose-induced changes in AMP-activated protein kinase (AMPK) activity could be mediated by SIRT1, an NAD+-dependent histone/protein deacetylase that has been linked to the increase in longevity caused by caloric restriction. Incubation with 25 vs. 5 mM glucose for 6 h concurrently diminished the phosphorylation of AMPK (Thr 172) and ACC (Ser 79), increased lactate release, and decreased the abundance and activity of SIRT1. In contrast, incubation with pyruvate (0.1 and 1 mM) for 2 h increased AMPK phosphorylation and SIRT1 abundance and activity. The putative SIRT1 activators resveratrol and quercetin also increased AMPK phosphorylation. None of the tested compounds (low or high glucose, pyruvate, and resveratrol) significantly altered the AMP/ATP ratio. Collectively, these findings raise the possibility that glucose-induced changes in AMPK are linked to alterations in SIRT1 abundance and activity and possibly cellular redox state.",
keywords = "AMPK, Redox state, Resveratrol, SIRT1",
author = "Gabriela Suchankova and Nelson, {Lauren E.} and Zachary Gerhart-Hines and Meghan Kelly and Gauthier, {Marie Soleil} and Saha, {Asish K.} and Yasuo Ido and Pere Puigserver and Ruderman, {Neil B.}",
note = "Funding Information: This work was supported by NIH Grants R01 DK19514, P01 HL08758, and DK67509 (N.R.). G.S. was the recipient of a mentor based grant from the ADA (N.R.). L.N. was supported by NIH Training Grant T32DK07201-31 and a Fellowship Award F30DK082136 from NIDDK. The authors would like to thank Jose Cacicedo and Fan Lan for helpful comments and technical advice.",
year = "2009",
month = jan,
day = "23",
doi = "10.1016/j.bbrc.2008.11.130",
language = "English",
volume = "378",
pages = "836--841",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "4",

}

RIS

TY - JOUR

T1 - Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells

AU - Suchankova, Gabriela

AU - Nelson, Lauren E.

AU - Gerhart-Hines, Zachary

AU - Kelly, Meghan

AU - Gauthier, Marie Soleil

AU - Saha, Asish K.

AU - Ido, Yasuo

AU - Puigserver, Pere

AU - Ruderman, Neil B.

N1 - Funding Information: This work was supported by NIH Grants R01 DK19514, P01 HL08758, and DK67509 (N.R.). G.S. was the recipient of a mentor based grant from the ADA (N.R.). L.N. was supported by NIH Training Grant T32DK07201-31 and a Fellowship Award F30DK082136 from NIDDK. The authors would like to thank Jose Cacicedo and Fan Lan for helpful comments and technical advice.

PY - 2009/1/23

Y1 - 2009/1/23

N2 - We examined in HepG2 cells whether glucose-induced changes in AMP-activated protein kinase (AMPK) activity could be mediated by SIRT1, an NAD+-dependent histone/protein deacetylase that has been linked to the increase in longevity caused by caloric restriction. Incubation with 25 vs. 5 mM glucose for 6 h concurrently diminished the phosphorylation of AMPK (Thr 172) and ACC (Ser 79), increased lactate release, and decreased the abundance and activity of SIRT1. In contrast, incubation with pyruvate (0.1 and 1 mM) for 2 h increased AMPK phosphorylation and SIRT1 abundance and activity. The putative SIRT1 activators resveratrol and quercetin also increased AMPK phosphorylation. None of the tested compounds (low or high glucose, pyruvate, and resveratrol) significantly altered the AMP/ATP ratio. Collectively, these findings raise the possibility that glucose-induced changes in AMPK are linked to alterations in SIRT1 abundance and activity and possibly cellular redox state.

AB - We examined in HepG2 cells whether glucose-induced changes in AMP-activated protein kinase (AMPK) activity could be mediated by SIRT1, an NAD+-dependent histone/protein deacetylase that has been linked to the increase in longevity caused by caloric restriction. Incubation with 25 vs. 5 mM glucose for 6 h concurrently diminished the phosphorylation of AMPK (Thr 172) and ACC (Ser 79), increased lactate release, and decreased the abundance and activity of SIRT1. In contrast, incubation with pyruvate (0.1 and 1 mM) for 2 h increased AMPK phosphorylation and SIRT1 abundance and activity. The putative SIRT1 activators resveratrol and quercetin also increased AMPK phosphorylation. None of the tested compounds (low or high glucose, pyruvate, and resveratrol) significantly altered the AMP/ATP ratio. Collectively, these findings raise the possibility that glucose-induced changes in AMPK are linked to alterations in SIRT1 abundance and activity and possibly cellular redox state.

KW - AMPK

KW - Redox state

KW - Resveratrol

KW - SIRT1

UR - http://www.scopus.com/inward/record.url?scp=57849131142&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2008.11.130

DO - 10.1016/j.bbrc.2008.11.130

M3 - Journal article

C2 - 19071085

AN - SCOPUS:57849131142

VL - 378

SP - 836

EP - 841

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -

ID: 347795022