Insulin sensitivity of muscle tissue isolated from rats with manifest alloxan diabetes of varied duration

1979 ◽  
Vol 88 (4) ◽  
pp. 1126-1128
Author(s):  
Yu. A. Yaroshevskii

2012 ◽  
Vol 302 (3) ◽  
pp. E365-E373 ◽  
Author(s):  
Richard A. M. Jonkers ◽  
Marlou L. Dirks ◽  
Christine I. H. C. Nabuurs ◽  
Henk M. De Feyter ◽  
Stephan F. E. Praet ◽  
...  

Lack of physical activity has been related to an increased risk of developing insulin resistance. This study aimed to assess the impact of chronic muscle deconditioning on whole body insulin sensitivity, muscle oxidative capacity, and intramyocellular lipid (IMCL) content in subjects with paraplegia. Nine subjects with paraplegia and nine able-bodied, lean controls were recruited. An oral glucose tolerance test was performed to assess whole body insulin sensitivity. IMCL content was determined both in vivo and in vitro using1H-magnetic resonance spectroscopy and fluorescence microscopy, respectively. Muscle biopsy samples were stained for succinate dehydrogenase (SDH) activity to measure muscle fiber oxidative capacity. Subcellular distributions of IMCL and SDH activity were determined by defining subsarcolemmal and intermyofibrillar areas on histological samples. SDH activity was 57 ± 14% lower in muscle fibers derived from subjects with paraplegia when compared with controls ( P < 0.05), but IMCL content and whole body insulin sensitivity did not differ between groups. In muscle fibers taken from controls, both SDH activity and IMCL content were higher in the subsarcolemmal region than in the intermyofibrillar area. This typical subcellular SDH and IMCL distribution pattern was lost in muscle fibers collected from subjects with paraplegia and had changed toward a more uniform distribution. In conclusion, the lower metabolic demand in deconditioned muscle of subjects with paraplegia results in a significant decline in muscle fiber oxidative capacity and is accompanied by changes in the subcellular distribution patterns of SDH activity and IMCL. However, loss of muscle activity due to paraplegia is not associated with substantial lipid accumulation in skeletal muscle tissue.



Obesity ◽  
2021 ◽  
Vol 29 (3) ◽  
pp. 550-561
Author(s):  
Josiane L. Broussard ◽  
Leigh Perreault ◽  
Emily Macias ◽  
Sean A. Newsom ◽  
Kathleen Harrison ◽  
...  


2011 ◽  
Vol 31 (5-6) ◽  
pp. 237-238 ◽  
Author(s):  
N.R. Liburt ◽  
M.N. Fugaro ◽  
E.K. Wunderlich ◽  
J.L. Zambito ◽  
D.W. Horohov ◽  
...  


2006 ◽  
Vol 291 (1) ◽  
pp. E108-E114 ◽  
Author(s):  
Rikke Krogh-Madsen ◽  
Peter Plomgaard ◽  
Kirsten Møller ◽  
Bettina Mittendorfer ◽  
Bente K. Pedersen

Inflammation is associated with insulin resistance, and both tumor necrosis factor (TNF)-α and interleukin (IL)-6 may affect glucose uptake. TNF induces insulin resistance, whereas the role of IL-6 is controversial. High plasma levels of IL-18 are associated with insulin resistance in epidemiological studies. We investigated the effects of TNF and IL-6 on IL-18 gene expression in skeletal muscle and adipose tissue. Nine human volunteers underwent three consecutive interventions, receiving an infusion of recombinant human (rh)IL-6, rhTNF, and saline. Insulin sensitivity was assessed by measurement of whole body glucose uptake with the stable isotope tracer method during a euglycemic hyperinsulinemic clamp (20 mU·min−1·kg−1), which was initiated 1 h after the IL-6-TNF-saline infusion. Cytokine responses were measured in plasma, muscle, and fat biopsies. Plasma concentrations of TNF and IL-6 increased 10- and 38-fold, respectively, during the cytokine infusions. Whole body insulin-mediated glucose uptake was significantly reduced during TNF infusion but remained unchanged during IL-6 infusion. TNF induced IL-18 gene expression in muscle tissue, but not in adipose tissue, whereas IL-6 infusion had no effect on IL-18 gene expression in either tissue. We conclude that TNF-induced insulin resistance of whole body glucose uptake is associated with increased IL-18 gene expression in muscle tissue, indicating that TNF and IL-18 interact, and both may have important regulatory roles in the pathogenesis of insulin resistance.



2011 ◽  
Vol 2011 ◽  
pp. 1-8
Author(s):  
Dennis C. Mynarcik ◽  
Margaret A. McNurlan ◽  
Mark M. Melendez ◽  
James A. Vosswinkel ◽  
Marie C. Gelato

Rosiglitazone, an agonist of peroxisome proliferator activated receptor (PPARγ), improves insulin sensitivity by increasing insulin-stimulated glucose uptake into muscle tissue. This study was undertaken to assess changes in expression of PPAR-regulated genes in muscle tissue following treatment of HIV-associated insulin resistance with rosiglitazone. Muscle gene expression was assessed in twenty-two seronegative HIV subjects (control), 21 HIV-infected individuals with normal insulin sensitivity (HIV-IS) and 19 HIV-infected individuals with insulin resistance (HIV-IR). A subset of the HIV-IR group (N=10) were re-evaluated 12 weeks after treatment with 8 mg/d of rosiglitazone. The HIV-IR group's rosiglitazone-mediated improvement in insulin sensitivity was highly correlated with increased expression of PPARγ and carnitine palmitoyl transferase-1 (CPT-1), (r=0.87, P<.001) and (r=0.95, P<.001), respectively. The changes in PPARγ expression were also correlated with the changes in CPT1 expression (r=0.75, P=.009). The results suggest that rosiglitazone; may have a direct effect on muscle tissue to improve insulin sensitivity.



Diabetes ◽  
2018 ◽  
Vol 67 (Supplement 1) ◽  
pp. 158-OR
Author(s):  
JOSIANE L. BROUSSARD ◽  
LEIGH PERREAULT ◽  
SEAN A. NEWSOM ◽  
DARCY E. KAHN ◽  
ANNA KEREGE ◽  
...  


2019 ◽  
Vol 12 (4) ◽  
pp. 277-290 ◽  
Author(s):  
Mingxia Zhao ◽  
Lihong Shen ◽  
Zijun Ouyang ◽  
Manru Li ◽  
Guoliang Deng ◽  
...  

Abstract Impairment of glucose (Glu) uptake and storage by skeletal muscle is a prime risk factor for the development of metabolic diseases. Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a highly abundant RNA-binding protein that has been implicated in diverse cellular functions. The aim of this study was to investigate the function of hnRNP A1 on muscle tissue insulin sensitivity and systemic Glu homeostasis. Our results showed that conditional deletion of hnRNP A1 in the muscle gave rise to a severe insulin resistance phenotype in mice fed a high-fat diet (HFD). Conditional knockout mice fed a HFD showed exacerbated obesity, insulin resistance, and hepatic steatosis. In vitro interference of hnRNP A1 in C2C12 myotubes impaired insulin signal transduction and inhibited Glu uptake, whereas hnRNP A1 overexpression in C2C12 myotubes protected against insulin resistance induced by supraphysiological concentrations of insulin. The expression and stability of glycogen synthase (gys1) mRNA were also decreased in the absence of hnRNP A1. Mechanistically, hnRNP A1 interacted with gys1 and stabilized its mRNA, thereby promoting glycogen synthesis and maintaining the insulin sensitivity in muscle tissue. Taken together, our findings are the first to show that reduced expression of hnRNP A1 in skeletal muscle affects the metabolic properties and systemic insulin sensitivity by inhibiting glycogen synthesis.



1969 ◽  
Vol 44 (1) ◽  
pp. 1-12 ◽  
Author(s):  
M. GRIFFITHS ◽  
D. L. McINTOSH ◽  
R. M. C. LECKIE

SUMMARY Alloxan diabetes can be induced in red and in grey kangaroos and the initial changes in blood sugar levels after injection of the drug are similar to those in other herbivores, or in other vertebrates generally. In general the presence or absence and the severity of catabolic effects of diabetes in rabbits, sheep and red kangaroos all eating the same diet depends on the amount of food eaten. Injection of large amounts of cortisone into normal rabbits and a sheep induced the usual catabolic effects and injection of cortisone exacerbated the catabolism of diabetic rabbits and diabetic sheep. The same and larger dose rates of cortisone injected into 12 normal and two diabetic red kangaroos had no effect on N balance, hyperglycaemia, food intake, glycosuria, insulin sensitivity, or on intravenous glucose tolerance.



2018 ◽  
Vol 43 (2) ◽  
pp. 187-193 ◽  
Author(s):  
Dongmei Liu ◽  
Flor Elisa Morales ◽  
Heidi. B. IglayReger ◽  
Mary K. Treutelaar ◽  
Amy E. Rothberg ◽  
...  

Local inflammation in obese adipose tissue has been shown to contribute to insulin resistance; however, the role of macrophage infiltration within skeletal muscle is still debatable. This study aimed to evaluate the association of skeletal muscle macrophage gene expression with adiposity levels and insulin sensitivity in obese patients. Twenty-two nondiabetic obese patients and 23 healthy lean controls were included. Obese patients underwent a 3-month weight loss intervention. Macrophage gene expression in skeletal muscle (quantitative real-time polymerase chain reaction), body composition (dual-energy X-ray absorptiometry), and insulin sensitivity (homeostatic model assessment (HOMA) and oral glucose tolerance test) were compared between groups and their associations were analyzed. To validate skeletal muscle findings, we repeated the analyses with macrophage gene expression in adipose tissue. Expression levels of macrophage genes (CD68, CD11b, CD206, CD16, CD40, and CD163) were lower in skeletal muscle tissue of obese versus lean participants. Macrophage gene expression was also found to be inversely associated with adiposity, fasting insulin, and HOMA (r = −0.4 ∼ −0.6, p < 0.05), as well as positively associated with insulin sensitivity (r = 0.4 ∼ 0.8, p < 0.05). On the other hand, adipose tissue macrophage gene expression showed higher levels in obese versus lean participants, presenting a positive association with adiposity levels. Macrophage gene expression, in both skeletal and adipose tissue samples, was only minimally affected by the weight loss intervention. In contrast with the established positive relationship between adiposity and macrophage gene expression, an unexpected inverse correlation between these 2 variables was observed in skeletal muscle tissue. Additionally, muscle macrophage gene expression was inversely correlated with insulin resistance.



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