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Article

5'-AMP-activated protein kinase regulates skeletal muscle glycogen content and ergogenics.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 May 2005

Barnes Brian R, Glund Stephan, Long Yun Chau, Hjälm Göran, Andersson Leif, Zierath Juleen R

Abstract excerpt

5'-AMP-activated protein kinase (AMPK) activity is increased during exercise in an intensity- and glycogen-dependent manner. We previously reported that a mutation in the AMPK3 subunit (Prkag3225Q) increases AMPK activity and skeletal muscle glycogen content. Transfection experiments revealed the R225Q mutation is associated with high basal AMPK activity and diminished AMP dependence. Thus, the R225Q mutation can...

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Identifiers

PMID: 15857891
DOI: 10.1096/fj.04-3221com

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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5'-AMP-activated protein kinase regulates skeletal muscle glycogen content and ergogenics.PMID 15857891Read ↗

Naturally occurring R225W mutation of the gene encoding AMP-activated protein kinase (AMPK)gamma(3) results in increased oxidative capacity and glucose uptake in human primary myotubes.Semantic proximity Read ↗

Gain of function AMP-activated protein kinase γ3 mutation (AMPKγ3R200Q) in pig muscle increases glycogen storage regardless of AMPK activation.Semantic proximity Read ↗

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The human AMPKγ3 R225W mutation negatively impacts site-1 nucleotide binding and does not enhance basal AMPKγ3-associated activity nor glycogen production in human or mouse skeletal muscle.Semantic proximity Read ↗

Gain-of-function R225W mutation in human AMPKgamma(3) causing increased glycogen and decreased triglyceride in skeletal muscle.Semantic proximity Read ↗

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