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Pyruvate dehydrogenase kinase 4 expression is synergistically induced by AMP-activated protein kinase and fatty acids. / Houten, S. M.; Chegary, M.; te Brinke, H. et al.

In: Cellular and molecular life sciences, Vol. 66, No. 7, 2009, p. 1283-1294.

Research output: Contribution to journal › Article › Academic › peer-review

Harvard

Houten, SM, Chegary, M, te Brinke, H, Wijnen, WJ, Glatz, JFC, Luiken, JJFP, Wijburg, FA & Wanders, RJA 2009, 'Pyruvate dehydrogenase kinase 4 expression is synergistically induced by AMP-activated protein kinase and fatty acids', Cellular and molecular life sciences, vol. 66, no. 7, pp. 1283-1294. https://doi.org/10.1007/s00018-009-9066-x

APA

Houten, S. M., Chegary, M., te Brinke, H., Wijnen, W. J., Glatz, J. F. C., Luiken, J. J. F. P., Wijburg, F. A., & Wanders, R. J. A. (2009). Pyruvate dehydrogenase kinase 4 expression is synergistically induced by AMP-activated protein kinase and fatty acids. Cellular and molecular life sciences, 66(7), 1283-1294. https://doi.org/10.1007/s00018-009-9066-x

Vancouver

Houten SM, Chegary M, te Brinke H, Wijnen WJ, Glatz JFC, Luiken JJFP et al. Pyruvate dehydrogenase kinase 4 expression is synergistically induced by AMP-activated protein kinase and fatty acids. Cellular and molecular life sciences. 2009;66(7):1283-1294. doi: 10.1007/s00018-009-9066-x

Author

Houten, S. M. ; Chegary, M. ; te Brinke, H. et al. / Pyruvate dehydrogenase kinase 4 expression is synergistically induced by AMP-activated protein kinase and fatty acids. In: Cellular and molecular life sciences. 2009 ; Vol. 66, No. 7. pp. 1283-1294.

BibTeX

@article{dce8916b7b9b44f4b69c5f4a2263c957,
title = "Pyruvate dehydrogenase kinase 4 expression is synergistically induced by AMP-activated protein kinase and fatty acids",
abstract = "Organs are flexible as to which substrates they will use to maintain energy homeostasis. Under well-fed conditions, glucose is a preferred substrate for oxidation. During fasting, fatty acid oxidation will become a more important energy source. Glucose oxidation is decreased by fatty acids, a process in which the pyruvate dehydrogenase complex (PDH) and its regulator pyruvate dehydrogenase kinase 4 (PDK4) play important roles. It is currently unknown how energy status influences PDH activity. We show that AMP-activated protein kinase (AMPK) activation by hypoxia and AICAR treatment combined with fatty acid administration synergistically induce PDK4 expression. We provide evidence that AMPK activation modulates ligand-dependent activation of peroxisome proliferator-activated receptor. Finally, we show that this synergistic induction of PDK4 decreases cellular glucose oxidation. In conclusion, AMPK and fatty acids play a direct role in fuel selection in response to cellular energy status in order to spare glucose",
author = "Houten, {S. M.} and M. Chegary and {te Brinke}, H. and Wijnen, {W. J.} and Glatz, {J. F. C.} and Luiken, {J. J. F. P.} and Wijburg, {F. A.} and Wanders, {R. J. A.}",
year = "2009",
doi = "10.1007/s00018-009-9066-x",
language = "English",
volume = "66",
pages = "1283--1294",
journal = "Cellular and molecular life sciences",
issn = "1420-682X",
publisher = "Birkhauser Verlag Basel",
number = "7",

}

RIS

TY - JOUR

T1 - Pyruvate dehydrogenase kinase 4 expression is synergistically induced by AMP-activated protein kinase and fatty acids

AU - Houten, S. M.

AU - Chegary, M.

AU - te Brinke, H.

AU - Wijnen, W. J.

AU - Glatz, J. F. C.

AU - Luiken, J. J. F. P.

AU - Wijburg, F. A.

AU - Wanders, R. J. A.

PY - 2009

Y1 - 2009

N2 - Organs are flexible as to which substrates they will use to maintain energy homeostasis. Under well-fed conditions, glucose is a preferred substrate for oxidation. During fasting, fatty acid oxidation will become a more important energy source. Glucose oxidation is decreased by fatty acids, a process in which the pyruvate dehydrogenase complex (PDH) and its regulator pyruvate dehydrogenase kinase 4 (PDK4) play important roles. It is currently unknown how energy status influences PDH activity. We show that AMP-activated protein kinase (AMPK) activation by hypoxia and AICAR treatment combined with fatty acid administration synergistically induce PDK4 expression. We provide evidence that AMPK activation modulates ligand-dependent activation of peroxisome proliferator-activated receptor. Finally, we show that this synergistic induction of PDK4 decreases cellular glucose oxidation. In conclusion, AMPK and fatty acids play a direct role in fuel selection in response to cellular energy status in order to spare glucose

AB - Organs are flexible as to which substrates they will use to maintain energy homeostasis. Under well-fed conditions, glucose is a preferred substrate for oxidation. During fasting, fatty acid oxidation will become a more important energy source. Glucose oxidation is decreased by fatty acids, a process in which the pyruvate dehydrogenase complex (PDH) and its regulator pyruvate dehydrogenase kinase 4 (PDK4) play important roles. It is currently unknown how energy status influences PDH activity. We show that AMP-activated protein kinase (AMPK) activation by hypoxia and AICAR treatment combined with fatty acid administration synergistically induce PDK4 expression. We provide evidence that AMPK activation modulates ligand-dependent activation of peroxisome proliferator-activated receptor. Finally, we show that this synergistic induction of PDK4 decreases cellular glucose oxidation. In conclusion, AMPK and fatty acids play a direct role in fuel selection in response to cellular energy status in order to spare glucose

U2 - 10.1007/s00018-009-9066-x

DO - 10.1007/s00018-009-9066-x

M3 - Article

C2 - 19224132

VL - 66

SP - 1283

EP - 1294

JO - Cellular and molecular life sciences

JF - Cellular and molecular life sciences

SN - 1420-682X

IS - 7

ER -

ID: 885348