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PRKAG3  -  protein kinase, AMP-activated, gamma 3 non...

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High impact information on PRKAG3

  • A dominant missense mutation (R225Q) in pig PRKAG3, encoding the muscle-specific gamma3 isoform, causes a marked increase in glycogen content [1].
  • An AMPK activator failed to increase skeletal muscle glucose uptake in AMPK gamma3 knock-out mice, whereas contraction effects were preserved [1].
  • Our results validate the muscle-specific AMPK gamma3 isoform as a therapeutic target for prevention and treatment of insulin resistance [1].
  • Haplotype analysis was shown to resolve the effects of PRKAG3 more clearly than analysis of individual polymorphisms [2].
  • PRKAG1, PRKAG2 and PRKAG3 encode three isoforms of AMP-activated protein kinase gamma chain [3].

Biological context of PRKAG3

  • The protein kinase AMP-activated gamma 3 subunit gene, PRKAG3, which encodes the gamma 3 isoform of AMP-activated protein kinase (AMPK), was identified as the causative gene for this phenotype by a pure positional cloning approach [4].
  • Identification of single-nucleotide polymorphisms in 5' end and exons of the PRKAG3 gene in Hubbard White broiler, Leghorn layer, and three Chinese indigenous chicken breeds [5].
  • Two SNPs in the 5'-end of the gene and 10 SNPs in exons 3, 4, 9 and 11, of which three caused amino acid substitutions, were identified in the PRKAG3 gene of the five chicken breeds [5].
  • Allele frequencies were analyzed in seven different pig breeds for these loci and for a polymorphism already described for GPI and for three polymorphic sites already reported at the PRKAG3 locus (T30N, G52S and I199V) [6].

Anatomical context of PRKAG3

  • A dominant mutation, denoted RN(-), in the porcine PRKAG3 gene, encoding the regulatory gamma3 subunit of AMPK, results in hyperaccumulation of glycogen in glycolytic skeletal muscle cells [7].

Associations of PRKAG3 with chemical compounds

  • Previous studies revealed that polymorphisms in 5'-AMP-activated protein kinase gamma 3 subunit (PRKAG3) gene are associated with meat quality in pigs [5].


  1. The 5'-AMP-activated protein kinase gamma3 isoform has a key role in carbohydrate and lipid metabolism in glycolytic skeletal muscle. Barnes, B.R., Marklund, S., Steiler, T.L., Walter, M., Hjälm, G., Amarger, V., Mahlapuu, M., Leng, Y., Johansson, C., Galuska, D., Lindgren, K., Abrink, M., Stapleton, D., Zierath, J.R., Andersson, L. J. Biol. Chem. (2004) [Pubmed]
  2. Evidence for new alleles in the protein kinase adenosine monophosphate-activated gamma(3)-subunit gene associated with low glycogen content in pig skeletal muscle and improved meat quality. Ciobanu, D., Bastiaansen, J., Malek, M., Helm, J., Woollard, J., Plastow, G., Rothschild, M. Genetics (2001) [Pubmed]
  3. Determination of PRKAG1 coding sequence and mapping of PRKAG1 and PRKAG2 relatively to porcine back fat thickness QTL. Demeure, O., Liaubet, L., Riquet, J., Milan, D. Anim. Genet. (2004) [Pubmed]
  4. Identification and characterization of AMPK gamma 3 mutations in the pig. Andersson, L. Biochem. Soc. Trans. (2003) [Pubmed]
  5. Identification of single-nucleotide polymorphisms in 5' end and exons of the PRKAG3 gene in Hubbard White broiler, Leghorn layer, and three Chinese indigenous chicken breeds. Zhao, C.J., Wang, C.F., Deng, X.M., Gao, Y., Wu, C.h. J. Anim. Breed. Genet. (2006) [Pubmed]
  6. Study of candidate genes for glycolytic potential of porcine skeletal muscle: identification and analysis of mutations, linkage and physical mapping and association with meat quality traits in pigs. Fontanesi, L., Davoli, R., Nanni Costa, L., Scotti, E., Russo, V. Cytogenet. Genome Res. (2003) [Pubmed]
  7. UDP-glucose pyrophosphorylase is upregulated in carriers of the porcine RN- mutation in the AMP-activated protein kinase. Hedegaard, J., Horn, P., Lametsch, R., Søndergaard Møller, H., Roepstorff, P., Bendixen, C., Bendixen, E. Proteomics (2004) [Pubmed]
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