Abstract
The AMP-activated protein kinase (AMPK) functions as a metabolic sensor that monitors cellular AMP and ATP levels. Platelet-activating factor (PAF) activates endogeneous AMPKα1 in Chinese hamster ovary cells expressing the PAF receptor coupled with both Gi and Gq, but its activity was not inhibited after treatment with islet-activating protein. Norepinephrine and bradykinin also activated AMPKα1 in cells expressing the Gq-coupled α1b-adrenergic receptor and bradykinin receptor, respectively. Stimulations of the Gi-coupled α2A-adrenergic receptor, fMet-Leu-Phe receptor, prostaglandin EP3α receptor, and Gs-coupled β2-adrenergic receptor did not activate AMPKα1. AMPKα1 thus is activated specifically by stimulation of Gq-coupled receptors. Gq-coupled receptors transmit the signal for GLUT4 translocation and glucose uptake through an insulin-independent pathway. However, direct activation of AMPKα1 with treatment of 5-aminoimidazole-4-carboxamide-1-β-d-ribofuranoside did not trigger GLUT4 translocation nor stimulate glucose uptake in our cells. Thus, activation of AMPKα1 via Gq is not sufficient to trigger GLUT4 translocation or stimulate glucose uptake.
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