- ►shouxi.net HF Kramer, CA Witczak, N Fujii, N Jessen, … - Diabetes, 2006 - Am Diabetes Assoc Insulin and contraction increase GLUT4 translocation in skeletal muscle via
distinct signaling mechanisms. Akt substrate of 160 kDa (AS160) mediates
insulin-stimulated GLUT4 translocation in L6 myotubes, presumably through ... Cited by 84 - Related articles - BL Direct - All 6 versions
- ►shouxi.net JT Treebak, S Glund, A Deshmukh, DK Klein, … - Diabetes, 2006 - Am Diabetes Assoc AMP-activated protein kinase (AMPK) is a heterotrimeric protein that regulates
glucose transport mediated by cellular stress or pharmacological agonists such
as 5-aminoimidazole-4-carboxamide 1 β-d-ribonucleoside (AICAR). AS160, a ... Cited by 81 - Related articles - BL Direct - All 7 versions
- ►shouxi.net HF Kramer, CA Witczak, EB Taylor, N Fujii, … - Journal of Biological Chemistry, 2006 - ASBMB Insulin and contraction are potent stimulators of GLUT4 translocation and
increase skeletal muscle glucose uptake. We recently identified the Rab
GTPase-activating protein (GAP) AS160 as a putative point of convergence ... Cited by 62 - Related articles - All 6 versions
- ►shouxi.net MD Bruss, EB Arias, GE Lienhard, GD Cartee - Diabetes, 2005 - Am Diabetes Assoc In 3T3-L1 adipocytes, insulin-stimulated GLUT4 translocation requires
phosphorylation of the protein designated Akt substrate of 160 kDa (AS160). Both
insulin and contractions activate Akt in skeletal muscle. Therefore, we ... Cited by 100 - Related articles - All 8 versions
- ►shouxi.net A Deshmukh, VG Coffey, Z Zhong, AV Chibalin … - Diabetes, 2006 - Am Diabetes Assoc Skeletal muscle contraction stimulates multiple signaling cascades that govern a
variety of metabolic and transcriptional events. Akt/protein kinase B regulates
metabolism and growth/muscle hypertrophy, but contraction effects on this ... Cited by 43 - Related articles - BL Direct - All 5 versions
- ►physiology.org JT Treebak, JB Birk, AJ Rose, B Kiens, EA … - American Journal of Physiology- Endocrinology And …, 2007 - Am Physiological Soc We investigated time- and intensity-dependent effects of exercise on
phosphorylation of Akt substrate of 160 kDa (AS160) in human skeletal muscle.
Subjects performed cycle exercise for 90 min (67% O 2 peak , n = 8), 20 min ... Cited by 26 - Related articles - BL Direct - All 4 versions
- ►jbc.org N Fujii, MF Hirshman, EM Kane, RC Ho, LE … - Journal of Biological Chemistry, 2005 - ASBMB To examine the role of AMP-activated protein kinase (AMPK) in muscle glucose
transport, we generated muscle-specific transgenic mice (TG) carrying cDNAs of
inactive 2 ( 2i TG) and 1 ( 1i TG) catalytic subunits. Extensor digitorum ... Cited by 72 - Related articles - BL Direct - All 5 versions
- ►shouxi.net G Ramm, M Larance, M Guilhaus, DE James - Journal of Biological Chemistry, 2006 - ASBMB Translocation of the insulin-regulated glucose transporter GLUT4 to the cell
surface is dependent on the phosphatidylinositol 3-kinase/Akt pathway. The
RabGAP (Rab GTPase-activating protein) AS160 (Akt substrate of 160 kDa) is ... Cited by 42 - Related articles - All 6 versions
- ►shouxi.net FSL Thong, PJ Bilan, A Klip - Diabetes, 2007 - Am Diabetes Assoc Insulin-dependent phosphorylation of Akt target AS160 is required for GLUT4
translocation. Insulin and platelet-derived growth factor (PDGF) (Akt
activators) or activation of conventional/novel (c/n) protein kinase C ... Cited by 42 - Related articles - BL Direct - All 5 versions
H Sano, S Kane, E Sano, CP Miinea, JM … - Journal of Biological Chemistry, 2003 - ASBMB Insulin stimulates the rapid translocation of intracellular glucose transporters
of the GLUT4 isotype to the plasma membrane in fat and muscle cells. The
connections between known insulin signaling pathways and the protein ... Cited by 249 - Related articles - BL Direct - All 4 versions
