Impaired glucose transport in skeletal muscle but normal GLUT-4 tissue distribution in glucose-infused rats

Davidson, Mayer B.; Bouch, C.; Venkatesan, Natarajan; Karjala, Robert G.

doi:10.1152/ajpendo.1994.267.6.e808

Cited by 16 publications

(15 citation statements)

References 23 publications

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“…There was significant impairment of insulin-induced glucose uptake and glycogen synthesis in isolated soleus muscle. This may be explicable on the basis of glucose toxicity since impaired muscle glucose uptake and oxidation has been previously documented in hyperglycemic states (19). Alternatively, it may represent an intrinsic defect in insulin action resulting from inhibition of the IGF-I effect in muscle.…”

Section: Discussionmentioning

confidence: 95%

Impaired glucose homeostasis in insulin-like growth factor binding protein-1 transgenic mice.

Rajkumar

Kršek²,

Dheen³

et al. 1996

J. Clin. Invest.

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Transgenic mice that overexpressed IGFBP-1 are hyperinsulinemic in the first week of life and gradually develop fasting hyperglycemia. In adult transgenic mice, the hypoglycemic response to IGF-I but not insulin or des (1-3) IGF-I was attenuated ( P Ͻ 0.05) compared with wild-type mice. Furthermore, in isolated adipocytes from transgenic mice, the stimulatory effect of IGF-I but not insulin on 2-deoxy-[ 3 H]-glucose uptake was reduced ( P Ͻ 0.02). In contrast, in isolated soleus muscle, the effects of both IGF-I and insulin on 2-deoxy-3 H-glucose uptake and on [ 3 H]-glucose incorporation into glycogen were significantly reduced compared to wild-type mice. The decline in specific activity of the 2-deoxy-3 H-glucose, a measure of glucose appearance in the circulation, was more marked in transgenic animals ( P Ͻ 0.05). In addition, tissue uptake of glucose was significantly higher in diaphragm, heart, intestine, liver, soleus muscle, and adipose tissue from fasting transgenic mice. Plasma concentrations of alanine, lysine, and methionine were also elevated in transgenic mice. These data suggest that overexpression of IGFBP-1 attenuates the hypoglycemic effect of endogenous IGF-I, which is initially compensated for by enhanced pancreatic insulin production. However, in adult mice pancreatic insulin content is reduced, insulin resistance is demonstrable in skeletal muscle and fasting hyperglycemia develops. ( J. Clin. Invest. 1996. 98: 1818-1825.) Key words: diabetes • IGF-I • insulin • 2-deoxyglucose uptake • pancreatic islets

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Section: Discussionmentioning

confidence: 95%

Impaired glucose homeostasis in insulin-like growth factor binding protein-1 transgenic mice.

Rajkumar

Kršek²,

Dheen³

et al. 1996

J. Clin. Invest.

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“…This glucose toxicity form of insulin resistance can also be induced by prolonged glucose infusions that result in high levels of blood glucose and insulin (7,25,31) and by incubation of isolated muscles or fat cells with high concentrations of glucose and insulin (11,24,25,30). Glucose toxicity insulin resistance may also develop in type 1 diabetics with high blood glucose levels whose hyperglycemia is reversed by insulin therapy (47).…”

Section: Discussionmentioning

confidence: 99%

Glucosamine and glucose induce insulin resistance by different mechanisms in rat skeletal muscle

Han

Chen

Holloszy

2003

American Journal of Physiology-Endocrinology and Metabolism

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It has been hypothesized that glucose-induced insulin resistance is mediated by accumulation of UDP- N-acetylhexosamines (UDP-HexNAcs). In a previous study on rat epitrochlearis muscles incubated with high concentrations of glucose and insulin (Kawanaka K, D-H Han, J Gao, LA Nolte, and JO Holloszy. J Biol Chem 276: 20101–20107, 2001), we found that insulin resistance developed even when the increase in UDP-Hex-NAcs was prevented. Furthermore, actinomycin D completely prevented glucose-induced insulin resistance despite a greater accumulation of UDP-HexNAcs. In the present study, we used the same epitrochlearis muscle preparation, as well as the rat hemidiaphragm, to determine whether, like glucose, glucosamine causes insulin resistance by an actinomycin D-inhibitable process. Incubation of diaphragm muscles with 10 mM glucosamine for 3 h resulted in an approximately fivefold increase in UDP-HexNAcs, an ∼50% reduction in insulin responsiveness of glucose transport, and a 58% reduction in ATP concentration. These effects of glucosamine were not prevented by actinomycin D. Incubation of epitrochlearis muscles with 20 mM glucosamine for 3 h or with 10 mM glucosamine for 5 h also caused large decreases in insulin responsiveness of glucose transport but with no reduction in ATP concentration. Actinomycin D did not prevent the glucosamine-induced insulin resistance. The insulin-induced increases in tyrosine phosphorylation of insulin receptor substrate (IRS)-1 and the binding of PI 3-kinase to IRS-1 were decreased ∼60% in epitrochlearis muscles exposed to glucosamine. This is in contrast to glucose-induced insulin resistance, which was not associated with impaired insulin signaling. These results provide evidence that glucosamine and glucose induce insulin resistance by different mechanisms.

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“…Fasting plasma free fatty acid levels were measured with Wako NEFA C kit (Wako Chemicals, Richmond, VA), and triglycerides were measured with the Infinity triglyceride reagent (Sigma-Aldrich). For analyzing glucose utilization by skeletal muscle, an intravenous injection of 1Ci of the non-metabolizable glucose analog 2-deoxy-D- [1][2][3] H]glucose (GE Healthcare) and an intraperitoneal injection of insulin (0.75 milliunits/kg of body weight) were administered to random-fed mice. The specific blood 2-deoxy-D- [1-3 H]glucose clearance was determined with 25-l blood samples collected from the tail vein obtained 1, 15, and 30 min after injection as previously reported (33).…”

Section: Ages Determination Metabolite Assays and 2-deoxy-d-[1-3 H]mentioning

confidence: 99%

“…These acquired and secondary factors further impair insulin action in diabetic individuals. For instance, chronic hyperglycemia per se promotes insulin resistance (2,3). A number of mechanisms have been proposed to explain hyperglycemia-induced insulin resistance.…”

mentioning

confidence: 99%

“…A number of mechanisms have been proposed to explain hyperglycemia-induced insulin resistance. These include abnormalities in the protein kinase C (PKC) 3 signaling system (4) and activation of the NF-B transcription factors by chronically elevated glucose concentrations (5,6). Chronic hyperglycemia also leads to the production of Amadori products through the nonenzymatic glycation reactions between glucose and reactive amino groups of serum proteins.…”

mentioning

confidence: 99%

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In Skeletal Muscle Advanced Glycation End Products (AGEs) Inhibit Insulin Action and Induce the Formation of Multimolecular Complexes Including the Receptor for AGEs

Cassese

Esposito

Fiory

et al. 2008

Journal of Biological Chemistry

106

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Chronic hyperglycemia promotes insulin resistance at least in part by increasing the formation of advanced glycation end products (AGEs). We have previously shown that in L6 myotubes human glycated albumin (HGA) induces insulin resistance by activating protein kinase C␣ (PKC␣). Here we show that HGA-induced PKC␣ activation is mediated by Src. Coprecipitation experiments showed that Src interacts with both the receptor for AGE (RAGE) and PKC␣ in HGA-treated L6 cells. A direct interaction of PKC␣ with Src and insulin receptor substrate-1 (IRS-1) has also been detected. In addition, silencing of IRS-1 expression abolished HGA-induced RAGE-PKC␣ co-precipitation. AGEs were able to induce insulin resistance also in vivo, as insulin tolerance tests revealed a significant impairment of insulin sensitivity in C57/BL6 mice fed a high AGEs diet (HAD). In tibialis muscle of HAD-fed mice, insulin-induced glucose uptake and protein kinase B phosphorylation were reduced. This was paralleled by a 2.5-fold increase in PKC␣ activity. Similarly to in vitro observations, Src phosphorylation was increased in tibialis muscle of HAD-fed mice, and co-precipitation experiments showed that Src interacts with both RAGE and PKC␣. These results indicate that AGEs impairment of insulin action in the muscle might be mediated by the formation of a multimolecular complex including RAGE/IRS-1/Src and PKC␣.

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Impaired glucose transport in skeletal muscle but normal GLUT-4 tissue distribution in glucose-infused rats

Cited by 16 publications

References 23 publications

Impaired glucose homeostasis in insulin-like growth factor binding protein-1 transgenic mice.

Impaired glucose homeostasis in insulin-like growth factor binding protein-1 transgenic mice.

Glucosamine and glucose induce insulin resistance by different mechanisms in rat skeletal muscle

In Skeletal Muscle Advanced Glycation End Products (AGEs) Inhibit Insulin Action and Induce the Formation of Multimolecular Complexes Including the Receptor for AGEs

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