Garcia-Roves 2008 J Biol Chem: Difference between revisions
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{{Publication | {{Publication | ||
|title=Garcia-Roves PM, Osler ME, Holmstroem MH, Zierath JR (2008) Gain-of-function R225Q mutation in AMP-activated protein kinase gamma3 subunit increases mitochondrial biogenesis in glycolytic skeletal muscle. J Biol Chem 283: 35724- | |title=Garcia-Roves PM, Osler ME, Holmstroem MH, Zierath JR (2008) Gain-of-function R225Q mutation in AMP-activated protein kinase gamma3 subunit increases mitochondrial biogenesis in glycolytic skeletal muscle. J Biol Chem 283:35724-34. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18838377 PMID: 18838377] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/18838377 PMID: 18838377 Open Access] | ||
|authors=Garcia-Roves PM, Osler ME, Holmstroem MH, Zierath JR | |authors=Garcia-Roves PM, Osler ME, Holmstroem MH, Zierath JR | ||
|year=2008 | |year=2008 | ||
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{{Labeling | {{Labeling | ||
|area=Respiration, mt-Biogenesis;mt-density, Genetic knockout;overexpression, Comparative MiP;environmental MiP | |||
|tissues=Skeletal muscle | |||
|preparations=Permeabilized tissue | |||
|couplingstates=OXPHOS | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
|discipline=Mitochondrial Physiology, Biomedicine | |discipline=Mitochondrial Physiology, Biomedicine | ||
}} | }} | ||
Latest revision as of 09:46, 15 December 2014
| Garcia-Roves PM, Osler ME, Holmstroem MH, Zierath JR (2008) Gain-of-function R225Q mutation in AMP-activated protein kinase gamma3 subunit increases mitochondrial biogenesis in glycolytic skeletal muscle. J Biol Chem 283:35724-34. |
Garcia-Roves PM, Osler ME, Holmstroem MH, Zierath JR (2008) J Biol Chem
Abstract: AMP-activated protein kinase (AMPK) is a heterotrimeric complex, composed of a catalytic subunit (ฮฑ) and two regulatory subunits (ฮฒ and ฮณ), that works as a cellular energy sensor. The existence of multiple heterotrimeric complexes provides a molecular basis for the multiple roles of this highly conserved signaling system. The AMPKฮณ3 subunit is predominantly expressed in skeletal muscle, mostly in type II glycolytic fiber types. We determined whether the AMPKฮณ3 subunit has a role in signaling pathways that mediate mitochondrial biogenesis in skeletal muscle. We provide evidence that overexpression or ablation of the AMPKฮณ3 subunit does not appear to play a critical role in defining mitochondrial content in resting skeletal muscle. However, overexpression of a mutant form (R225Q) of the AMPKฮณ3 subunit (Tg-AMPKฮณ3225Q) increases mitochondrial biogenesis in glycolytic skeletal muscle. These adaptations are associated with an increase in expression of the co-activator PGC-1ฮฑ and several transcription factors that regulate mitochondrial biogenesis, including NRF-1, NRF-2, and TFAM. Succinate dehydrogenase staining, a marker of the oxidative profile of individual fibers, was also increased in transversal skeletal muscle sections of white gastrocnemius muscle from Tg-AMPKฮณ3225Q mice, independent of changes in fiber type composition. In conclusion, a single nucleotide mutation (R225Q) in the AMPK gamma3 subunit is associated with mitochondrial biogenesis in glycolytic skeletal muscle, concomitant with increased expression of the co-activator PGC-1ฮฑ and several transcription factors that regulate mitochondrial proteins, without altering fiber type composition. โข Keywords: AMP-activated protein kinase (AMPK)
โข O2k-Network Lab: ES Barcelona Garcia-Roves PM
Labels: MiParea: Respiration, mt-Biogenesis;mt-density, Genetic knockout;overexpression, Comparative MiP;environmental MiP
Tissue;cell: Skeletal muscle Preparation: Permeabilized tissue
Coupling state: OXPHOS
HRR: Oxygraph-2k
