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Kim MS, Lee J, Ha J, Kim SS, Kong Y, Cho YH, Baik HH, Kang I. ATP
stimulates glucose transport through activation of P2 purinergic receptors
in C(2)C(12) skeletal muscle cells. Arch Biochem Biophys. 2002;May15;401(2):205-214.
Department of Biochemistry, School of Medicine, Kyung Hee University,
1 Hoegi-dong, Dongdaemun-ku, Seoul 130-701, Republic of Korea.
Extracellular ATP acts as a signal that regulates a variety of cellular
processes via binding to P2 purinergic receptors (P2 receptors). We herein
investigated the effects and signaling pathways of ATP on glucose uptake
in C(2)C(12) skeletal muscle cells. ATP as well as P2 receptor agonists
(ATP-gamma S) stimulated the rate of glucose uptake, while P2 receptor
antagonists (suramin) inhibited the stimulatory effect of ATP, indicating
that P2 receptors are involved. This ATP-stimulated glucose transport
was blocked by specific inhibitors of Gi protein (pertusiss toxin), phospholipase
C (U73122), protein kinase C (GF109203X), and phosphatidylinositol (PI)
3-kinase (LY294002). ATP stimulated PI 3-kinase activity and P2 receptor
antagonists blocked this activation. In C(2)C(12) myotubes expressing
glucose transporter GLUT4, ATP increased basal and insulin-stimulated
glucose transport. Finally, ATP facilitated translocation of GLUT1 and
GLUT4 into plasma membrane. These results together suggest that cells
respond to extracellular ATP to increase glucose transport through P2
receptors. (c) 2002 Elsevier Science (USA).
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Abstracts