scholarly journals Scriptaid enhances skeletal muscle insulin action and cardiac function in obese mice

2017 ◽  
Vol 19 (7) ◽  
pp. 936-943 ◽  
Author(s):  
Vidhi Gaur ◽  
Timothy Connor ◽  
Kylie Venardos ◽  
Darren C. Henstridge ◽  
Sheree D. Martin ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cardiac Function ◽  
Insulin Action ◽  
Obese Mice ◽  
Muscle Insulin Action

scholarly journals Reciprocity Between Skeletal Muscle AMPK Deletion and Insulin Action in Diet-Induced Obese Mice

Diabetes ◽  
2020 ◽  
Vol 69 (8) ◽  
pp. 1636-1649
Author(s):  
Louise Lantier ◽  
Ashley S. Williams ◽  
Ian M. Williams ◽  
Amanda Guerin ◽  
Deanna P. Bracy ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Insulin Action ◽  
Obese Mice

scholarly journals Reduced Expression of Focal Adhesion Kinase Disrupts Insulin Action in Skeletal Muscle Cells

Endocrinology ◽  
2006 ◽  
Vol 147 (7) ◽  
pp. 3333-3343 ◽  
Author(s):  
Danshan Huang ◽  
Michelle Khoe ◽  
Dusko Ilic ◽  
Michael Bryer-Ash
Keyword(s):  
Skeletal Muscle ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Insulin Action ◽  
Glucose Transporter ◽  
Glycogen Synthesis ◽  
Growth Factor Signaling ◽  
L6 Myotubes ◽  
Normal Glucose ◽  
Muscle Insulin Action

Integrins mediate interactions between cells and extracellular matrix proteins that modulate growth factor signaling. Focal adhesion kinase (FAK) is a key multifunctional integrin pathway protein. We recently reported that disruption of FAK impairs insulin-mediated glycogen synthesis in hepatocytes. To test the hypothesis that FAK regulates skeletal muscle insulin action, we reduced FAK expression in L6 myotubes using FAK antisense. In untransfected myotubes, insulin stimulated both FAK tyrosine phosphorylation and kinase activity. Cells treated with antisense FAK showed 78 and 53% reductions in FAK mRNA and FAK protein, respectively, whereas insulin receptor substrate 1/2 and paxillin abundance were unaffected. Insulin-stimulated U-14C-glucose incorporation into glycogen was abolished by FAK antisense, and 2-deoxy-glucose uptake and glucose transporter 4 (GLUT4) translocation were both markedly attenuated. Antisense FAK did not alter GLUT1 or GLUT3 protein abundance. Immunofluorescence staining showed decreased FAK Tyr397 phosphorylation and reduced actin stress fibers. Thus, in skeletal myotubes, FAK regulates the insulin-mediated cytoskeletal rearrangement essential for normal glucose transport and glycogen synthesis. Integrin signaling may play an important regulatory role in muscle insulin action.

scholarly journals Acute inhibition of protein deacetylases does not impact skeletal muscle insulin action

2019 ◽  
Vol 317 (5) ◽  
pp. C964-C968
Author(s):  
Vitor F. Martins ◽  
Maedha Begur ◽  
Shivani Lakkaraju ◽  
Kristoffer Svensson ◽  
Ji Park ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glucose Uptake ◽  
Insulin Action ◽  
Trichostatin A ◽  
Hdac Inhibitors ◽  
Protein Acetylation ◽  
L6 Myotubes ◽  
Muscle Insulin Action ◽  
Nicotinamide Treatment

Whether the histone deacetylase (HDAC) and sirtuin families of protein deacetylases regulate insulin-stimulated glucose uptake, independent of their transcriptional effects, has not been studied. Our objective was to determine the nontranscriptional role of HDACs and sirtuins in regulation of skeletal muscle insulin action. Basal and insulin-stimulated glucose uptake and signaling and acetylation were assessed in L6 myotubes and skeletal muscle from C57BL/6J mice that were treated acutely (1 h) with HDAC (trichostatin A, panobinostat, TMP195) and sirtuin inhibitors (nicotinamide). Treatment of L6 myotubes with HDAC inhibitors or skeletal muscle with a combination of HDAC and sirtuin inhibitors increased tubulin and pan-protein acetylation, demonstrating effective impairment of HDAC and sirtuin deacetylase activities. Despite this, neither basal nor insulin-stimulated glucose uptake or insulin signaling was impacted. Acute reduction of the deacetylase activity of HDACs and/or sirtuins does not impact insulin action in skeletal muscle.

scholarly journals Metabolic and molecular changes associated with the increased skeletal muscle insulin action 24–48 h after exercise in young and old humans

2018 ◽  
Vol 46 (1) ◽  
pp. 111-118 ◽  
Author(s):  
Francis B. Stephens ◽  
Kostas Tsintzas
Keyword(s):  
Skeletal Muscle ◽  
Insulin Sensitivity ◽  
Insulin Action ◽  
Glucose Transporter ◽  
Glycogen Synthesis ◽  
Older Individuals ◽  
Hexokinase Ii ◽  
Molecular Changes ◽  
Single Bout ◽  
Muscle Insulin Action

The molecular and metabolic mechanisms underlying the increase in insulin sensitivity (i.e. increased insulin-stimulated skeletal muscle glucose uptake, phosphorylation and storage as glycogen) observed from 12 to 48 h following a single bout of exercise in humans remain unresolved. Moreover, whether these mechanisms differ with age is unclear. It is well established that a single bout of exercise increases the translocation of the glucose transporter, GLUT4, to the plasma membrane. Previous research using unilateral limb muscle contraction models in combination with hyperinsulinaemia has demonstrated that the increase in insulin sensitivity and glycogen synthesis 24 h after exercise is also associated with an increase in hexokinase II (HKII) mRNA and protein content, suggesting an increase in the capacity of the muscle to phosphorylate glucose and divert it towards glycogen synthesis. Interestingly, this response is altered in older individuals for up to 48 h post exercise and is associated with molecular changes in skeletal muscle tissue that are indicative of reduced lipid oxidation, increased lipogenesis, increased inflammation and a relative inflexibility of changes in intramyocellular lipid (IMCL) content. Reduced insulin sensitivity (insulin resistance) is generally related to IMCL content, particularly in the subsarcolemmal (SSL) region, and both are associated with increasing age. Recent research has demonstrated that ageing per se appears to cause an exacerbated lipolytic response to exercise that may result in SSL IMCL accumulation. Further research is required to determine if increased IMCL content affects HKII expression in the days after exercise in older individuals, and the effect of this on skeletal muscle insulin action.

scholarly journals The vascular actions of insulin control its delivery to muscle and regulate the rate-limiting step in skeletal muscle insulin action

Diabetologia ◽  
2009 ◽  
Vol 52 (5) ◽  
pp. 752-764 ◽  
Author(s):  
E. J. Barrett ◽  
E. M. Eggleston ◽  
A. C. Inyard ◽  
H. Wang ◽  
G. Li ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Insulin Action ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Insulin Control ◽  
Muscle Insulin Action ◽  
Rate Limiting

scholarly journals SIRT3 Is Crucial for Maintaining Skeletal Muscle Insulin Action and Protects Against Severe Insulin Resistance in High-Fat–Fed Mice

Diabetes ◽  
2015 ◽  
Vol 64 (9) ◽  
pp. 3081-3092 ◽  
Author(s):  
Louise Lantier ◽  
Ashley S. Williams ◽  
Ian M. Williams ◽  
Karen K. Yang ◽  
Deanna P. Bracy ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Insulin Action ◽  
High Fat ◽  
Severe Insulin Resistance ◽  
Muscle Insulin Action
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