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Exp. mol. med ; Exp. mol. med;: 535-543, 2007.
Article de Anglais | WPRIM | ID: wpr-174049

RÉSUMÉ

Insufficient intracellular fat oxidation is an important contributor to aging-related insulin resistance, while the precise mechanism underlying is unclear. AMP-activated protein kinase (AMPK) is an important regulator of intracellular fat oxidation and was evidenced to play a key role in high-glucose and high-fat induced glucose intolerance. In the present study, we investigated whether altered AMPK expression or activity was also involved in aging-related insulin resistance. Insulin sensitivity of rats' skeletal muscles was evaluated using in-vitro glucose uptake assay. Activity of alpha subunit of AMPK (AMPKalpha) was evaluated by measuring the phosphorylation of both AMPKalpha (P-AMPKalpha) and acetyl-CoA carboxylase (P-ACC), while expression of AMPKalpha was assessed by determining the mRNA levels of AMPKalpha1 and AMPKalpha2, and protein contents of AMPKalpha. Compared with 4-month old rats, 24-month old rats exhibited obviously impaired insulin sensitivity. At the same time, AMPKalpha activity significantly decreased, while AMPKalpha expression did not alter during aging. Glucose transporter 4 expression also decreased in old rats. Compared with 24-month old rats, administration of the specific activator of AMPK, 5-aminoimidazole-4-carboxamide riboside (AICAR), significantly elevated AMPKalpha activity and GluT4 expression. Also, aging-related insulin resistance was significantly ameliorated by AICAR treatment. In conclusion, aging-related insulin resistance is associated with impaired AMPKalpha activity and could be ameliorated by AICAR, thus indicating a possible role of AMPK in aging-induced insulin resistance.


Sujet(s)
Animaux , Mâle , Rats , AMP-Activated Protein Kinases , Acetyl-coA carboxylase/métabolisme , Vieillissement/physiologie , 5-Amino-imidazole-4-carboxamide/analogues et dérivés , Glucose/métabolisme , Transporteur de glucose de type 4/métabolisme , Insuline/sang , Insulinorésistance , Complexes multienzymatiques/antagonistes et inhibiteurs , Muscles squelettiques/métabolisme , Phosphorylation , Protein-Serine-Threonine Kinases/antagonistes et inhibiteurs , Rat Wistar , Ribonucléotides/pharmacologie
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