Opposite transcriptional regulation in skeletal muscle of AMPK gamma 3 R225Q transgenic versus knock-out mice

doi:10.1074/jbc.M510461200

HOME

QUICK SEARCH:

	Author:		Keyword(s):
Year:		Vol:		Page:

A more recent version of this article appeared on March 17, 2006

This Article

	Full Text (Accepted Manuscript)
	Supplemental Data
	All Versions of this Article: 281/11/7244 most recent M510461200v1
	Alert me when this article is cited
	Alert me if a correction is posted

Services

	Email this article to a friend
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new issues of the journal
	Download to citation manager
	Request Permissions

Citing Articles

	Citing Articles via HighWire
	Citing Articles via Google Scholar

Google Scholar

	Articles by Nilsson, E. C.
	Articles by Mahlapuu, M.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Nilsson, E. C.
	Articles by Mahlapuu, M.

Social Bookmarking

	What's this?

Papers In Press, published online ahead of print January 12, 2006
J. Biol. Chem, 10.1074/jbc.M510461200
Submitted on September 23, 2005
Revised on January 9, 2006
Accepted on January 12, 2006

Opposite transcriptional regulation in skeletal muscle of AMPK $gamma$ 3 R225Q transgenic versus knock-out mice

Elisabeth C. Nilsson, Yun Chau Long, Sofia Martinsson, Stephan Glund, Pablo Garcia-Roves, L. Thomas Svensson, Leif Andersson, Juleen R. Zierath, and Margit Mahlapuu

Arexis AB, Göteborg SE-413 46

Corresponding Author: margit.mahlapuu{at}arexis.com

Adenosine monophosphate-activated protein kinase (AMPK) is an evolutionarily conserved heterotrimer important for metabolic sensing in all eukaryotes. The muscle-specific isoform of the regulatory $gamma$ -subunit of the kinase, AMPK $gamma$ 3, has an important role in glucose uptake, glycogen synthesis and fat oxidation in white skeletal muscle, as previously demonstrated by physiological characterization of AMPK $gamma$ 3 mutant (R225Q) transgenic (TgPrkag3^225Q) and $gamma$ 3 knock-out (Prkag3^-/-) mice. We determined AMPK $gamma$ 3-dependent regulation of gene expression by analyzing global transcription profiles in glycolytic skeletal muscle from $gamma$ 3 mutant transgenic and knock-out mice using oligonucleotide microarray technology. Evidence is provided for coordinated and reciprocal regulation of multiple key components in glucose and fat metabolism, as well as skeletal muscle ergogenics in TgPrkag3^225Q and Prkag3^-/- mice. The differential gene expression profile was consistent with the physiological differences between the models, providing a molecular mechanism for the observed phenotype. The striking pattern of opposing transcriptional changes between TgPrkag3^225Q versus Prkag3^-/- mice identifies differentially expressed targets being truly regulated by AMPK and is consistent with the view that R225Q is an activating mutation, in terms of its downstream effects. Additionally, we identified a wide array of novel targets and regulatory pathways for AMPK in skeletal muscle.

Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

S. Park, T. L. Scheffler, A. M. Gunawan, H. Shi, C. Zeng, K. M. Hannon, A. L. Grant, and D. E. Gerrard
Chronic elevated calcium blocks AMPK-induced GLUT-4 expression in skeletal muscle
Am J Physiol Cell Physiol, January 1, 2009; 296(1): C106 - C115.
[Abstract] [Full Text] [PDF]

P. M. Garcia-Roves, M. E. Osler, M. H. Holmstrom, and J. R. Zierath
Gain-of-function R225Q Mutation in AMP-activated Protein Kinase {gamma}3 Subunit Increases Mitochondrial Biogenesis in Glycolytic Skeletal Muscle
J. Biol. Chem., December 19, 2008; 283(51): 35724 - 35734.
[Abstract] [Full Text] [PDF]

E. Vieira, E. C. Nilsson, A. Nerstedt, M. Ormestad, Y. C. Long, P. M. Garcia-Roves, J. R. Zierath, and M. Mahlapuu
Relationship between AMPK and the transcriptional balance of clock-related genes in skeletal muscle
Am J Physiol Endocrinol Metab, November 1, 2008; 295(5): E1032 - E1037.
[Abstract] [Full Text] [PDF]

M. Yoshioka, A. Boivin, C. Bolduc, and J. St-Amand
Gender difference of androgen actions on skeletal muscle transcriptome
J. Mol. Endocrinol., August 1, 2007; 39(2): 119 - 133.
[Abstract] [Full Text] [PDF]

B. J. Krawiec, G. J. Nystrom, R. A. Frost, L. S. Jefferson, and C. H. Lang
AMP-activated protein kinase agonists increase mRNA content of the muscle-specific ubiquitin ligases MAFbx and MuRF1 in C2C12 cells
Am J Physiol Endocrinol Metab, June 1, 2007; 292(6): E1555 - E1567.
[Abstract] [Full Text] [PDF]

Opposite transcriptional regulation in skeletal muscle of AMPK 3 R225Q transgenic versus knock-out mice

Opposite transcriptional regulation in skeletal muscle of AMPK $gamma$ 3 R225Q transgenic versus knock-out mice