RGD Reference Report - Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells. - Rat Genome Database

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Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells.

Authors: Fryer, LG  Foufelle, F  Barnes, K  Baldwin, SA  Woods, A  Carling, D 
Citation: Fryer LG, etal., Biochem J. 2002 Apr 1;363(Pt 1):167-74.
RGD ID: 8554594
Pubmed: PMID:11903059   (View Abstract at PubMed)
PMCID: PMC1222463   (View Article at PubMed Central)

Stimulation of AMP-activated protein kinase (AMPK) in skeletal muscle has been correlated with an increase in glucose transport. Here, we demonstrate that adenoviral-mediated expression of a constitutively active mutant of AMPK alpha leads to activation of glucose transport in a skeletal-muscle cell line, similar to that seen following treatment with 5-amino-imidazolecarboxamide (AICA) riboside, hyperosmotic stress or insulin. In contrast, expression of a dominant-negative form of AMPK blocked the stimulation of glucose transport by both AICA riboside and hyperosmotic stress, but was without effect on either insulin or phorbol-ester-stimulated transport. These results demonstrate that activation of AMPK is sufficient for stimulation of glucose uptake into muscle cells, and is a necessary component of the AICA riboside- and hyperosmotic-stress-induced pathway leading to increased glucose uptake. On the other hand, AMPK is not required in the insulin- or phorbol-ester-mediated pathways. Long-term (5 days) expression of the constitutively active AMPK mutant increased protein expression of GLUT1, GLUT4 and hexokinase II, consistent with previous reports on the chronic treatment of rats with AICA riboside. Expression of constitutively active AMPK had no detectable effect on p38 mitogen-activated protein kinase levels, although interestingly the level of protein kinase B was decreased. These results demonstrate that long-term activation of AMPK is sufficient to cause increased expression of specific proteins in muscle. Our results add further support to the hypothesis that long-term activation of AMPK is involved in the adaptive response of muscle to exercise training.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
positive regulation of gluconeogenesis involved_inNAS 8554594PMID:11903059UniProt 
positive regulation of glucose import involved_inNAS 8554594PMID:11903059UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Prkaa1  (protein kinase AMP-activated catalytic subunit alpha 1)


Additional Information