RGD Reference Report - Contraction regulation of Akt in rat skeletal muscle. - Rat Genome Database

Send us a Message



Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   

Contraction regulation of Akt in rat skeletal muscle.

Authors: Sakamoto, K  Hirshman, MF  Aschenbach, WG  Goodyear, LJ 
Citation: Sakamoto K, etal., J Biol Chem. 2002 Apr 5;277(14):11910-7. Epub 2002 Jan 23.
RGD ID: 2313393
Pubmed: PMID:11809761   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M112410200   (Journal Full-text)

The protein serine/threonine kinase Akt/protein kinase B has been recognized as a critical signaling mediator for multiple cell systems. The function of Akt in skeletal muscle is not well understood, and whether contractile activity stimulates Akt activity has been controversial. In the current study, contraction in situ, induced via sciatic nerve stimulation, significantly increased Akt Ser(473) phosphorylation in multiple muscle types including the extensor digitorum longus (13-fold over basal), plantaris (5.8-fold), red gastrocnemius (4.7-fold), white gastrocnemius (3.3-fold), and soleus (1.6-fold). In addition to increasing phosphorylation, contraction in situ significantly increased the activity of all three Akt isoforms (Akt1 > Akt2 > Akt3) with maximal activation occurring at 2.5 min and returning to base line with 15 min of contraction. Akt phosphorylation and activity were also increased when isolated muscles were contracted in vitro in the absence of systemic factors, although to a much lesser extent. The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 fully inhibited contraction-stimulated Akt phosphorylation and activity but did not diminish contraction-stimulated glycogen synthase kinase-3 phosphorylation and glycogen synthase activity. These results demonstrate that contraction increases Akt phosphorylation and activity in skeletal muscle and that this stimulation is rapid, transient, muscle fiber type-specific, and wortmannin- and LY294002-inhibitable. Akt signaling is not necessary for the regulation of glycogen synthase activity in contracting skeletal muscle.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
response to muscle activity  IEP 2313393 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Akt2  (AKT serine/threonine kinase 2)


Additional Information