ArticleDiabetes2009
Inhibition of contraction-stimulated AMP-activated protein kinase inhibits contraction-stimulated increases in PAS-TBC1D1 and glucose transport without altering PAS-AS160 in rat skeletal muscle.
Article in Diabetes, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
35 citing papers in PubMed, 74 citations in OpenAlex.
- N-Acetylcysteine infusion does not affect glucose disposal during prolonged moderate-intensity exercise in humans.The Journal of physiology · 2010Trial
- The role of skeletal muscle Akt in the regulation of muscle mass and glucose homeostasis.Molecular metabolism · 2019Article
- Exercise and Glycemic Control: Focus on Redox Homeostasis and Redox-Sensitive Protein Signaling.Frontiers in endocrinology · 2017Review
- Immobilization rapidly induces muscle insulin resistance together with the activation of MAPKs (JNK and p38) and impairment of AS160 phosphorylation.Physiological reports · 2016Article
- Emerging role of the brain in the homeostatic regulation of energy and glucose metabolism.Experimental & molecular medicine · 2016Review
- Skeletal Muscle Phospholipid Metabolism Regulates Insulin Sensitivity and Contractile Function.Diabetes · 2016Article
- Caffeine and contraction synergistically stimulate 5'-AMP-activated protein kinase and insulin-independent glucose transport in rat skeletal muscle.Physiological reports · 2015Article
- Reduced efficiency of sarcolipin-dependent respiration in myocytes from humans with severe obesity.Obesity (Silver Spring, Md.) · 2015Article
- Mechanisms for independent and combined effects of calorie restriction and acute exercise on insulin-stimulated glucose uptake by skeletal muscle of old rats.American journal of physiology. Endocrinology and metabolism · 2015Article
- Fiber type effects on contraction-stimulated glucose uptake and GLUT4 abundance in single fibers from rat skeletal muscle.American journal of physiology. Endocrinology and metabolism · 2015Article
- 17-β estradiol attenuates ovariectomy-induced changes in cardiomyocyte contractile function via activation of AMP-activated protein kinase.Toxicology letters · 2015Article
- Roles of TBC1D1 and TBC1D4 in insulin- and exercise-stimulated glucose transport of skeletal muscle.Diabetologia · 2015Review
- Increased postexercise insulin sensitivity is accompanied by increased AS160 phosphorylation in slow-twitch soleus muscle.Physiological reports · 2014Article
- Exercise and type 2 diabetes: molecular mechanisms regulating glucose uptake in skeletal muscle.Advances in physiology education · 2014Review
- Identification and Association of SNPs in TBC1D1 Gene with Growth Traits in Two Rabbit Breeds.Asian-Australasian journal of animal sciences · 2013Article
- Elevation of muscle temperature stimulates muscle glucose uptake in vivo and in vitro.The journal of physiological sciences : JPS · 2013Article
- Muscle lipogenesis balances insulin sensitivity and strength through calcium signaling.The Journal of clinical investigation · 2013Article
- AMPK and Exercise: Glucose Uptake and Insulin Sensitivity.Diabetes & metabolism journal · 2013Article
- Thr649Ala-AS160 knock-in mutation does not impair contraction/AICAR-induced glucose transport in mouse muscle.American journal of physiology. Endocrinology and metabolism · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
objectivePhosphorylation of two members of the TBC1 domain family of proteins, Akt substrate of 160 kDa (AS160, also known as TBC1D4) and TBC1D1, has been implicated in the regulation of glucose transport in skeletal muscle. Insulin-stimulated phosphorylation (measured using the phospho-Akt substrate [PAS] antibody) of AS160 and TBC1D1 appears to occur in an Akt-dependent manner, but the kinases responsible for contraction-stimulated PAS-AS160 and PAS-TBC1D1 remain unclear. AMP-activated protein kinase (AMPK) and Akt, both activated by contraction, can each phosphorylate AS160 and TBC1D1 in cell-free assays. RESEARCH DESIGN AND
methodsTo evaluate the roles of AMPK and Akt on insulin- or contraction-stimulated PAS-AS160, PAS-TBC1D1, and glucose transport, rat epitrochlearis was incubated with and without compound C (inhibitor of AMPK) or Wortmannin (inhibitor of phosphatidylinositol [PI] 3-kinase, which is upstream of Akt) before and during insulin stimulation or contraction.
resultsInsulin-stimulated glucose transport and phosphorylation of both AS160 and TBC1D1 were completely inhibited by Wortmannin. Wortmannin eliminated contraction stimulation of phospho-Ser(21/9)glycogen synthase kinase 3alpha/beta (pGSK3; Akt substrate) and PAS-AS160 but did not significantly alter pAMPK, phospho-Ser79acetyl CoA carboxylase (pACC; AMPK substrate), PAS-TBC1D1, or glucose transport in contraction-stimulated muscle. Compound C completely inhibited contraction-stimulated pACC and PAS-TBC1D1 and partially blocked glucose transport, but it did not significantly alter pAkt, pGSK3, or PAS-AS160.
conclusionsThese data suggest that 1) insulin stimulates glucose transport and phosphorylation of AS160 and TBC1D1 in a PI 3-kinase/Akt-dependent manner, 2) contraction stimulates PAS-AS160 (but not PAS-TBC1D1 or glucose transport) in a PI 3-kinase/Akt-dependent manner, and 3) contraction stimulates PAS-TBC1D1 and glucose transport (but not PAS-AS160) in an AMPK-dependent manner.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.