Glucose transport and GLUT4 protein distribution in skeletal muscle of GLUT4 transgenic mice

Brozinick, Joseph T.; Yaspelkis, Ben B.; Wilson, C M; Grant, Kristen E.; Gibbs, E. Michael; Cushman, Samuel W.; Ivy, J. L.

doi:10.1042/bj3130133

Cited by 45 publications

(44 citation statements)

References 26 publications

(27 reference statements)

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“…A survey of the literature suggests that there is a disparity between the extent of GLUT4 translocation and the stimulation of glucose uptake in mature muscle (14,(28)(29)(30)(31)(32)(33)(34)(35). In primary and cultured adipocytes, diverse conditions also dissociate stimulation of glucose uptake from GLUT4 translocation (8,36,37).…”

Section: Discussionmentioning

confidence: 99%

Activation of p38 mitogen-activated protein kinase alpha and beta by insulin and contraction in rat skeletal muscle: potential role in the stimulation of glucose transport.

et al. 2000

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The stress-activated p38 mitogen-activated protein kinase (MAPK) was recently shown to be activated by insulin in muscle and adipose cells in culture. Here, we explore whether such stimulation is observed in rat skeletal muscle and whether muscle contraction can also affect the enzyme. Insulin injection (2 U over 3.5 min) resulted in increases in p38 MAPK phosphorylation measured in soleus (3.2-fold) and quadriceps (2.2-fold) muscles. Increased phosphorylation (3.5-fold) of an endogenous substrate of p38 MAPK, cAMP response element binder (CREB), was also observed. After in vivo insulin treatment, p38 MAPK␣ and p38 MAPK␤ isoforms were found to be activated (2.1-and 2.4-fold, respectively), using an in vitro kinase assay, in immunoprecipitates from quadriceps muscle extracts. In vitro insulin treatment (1 nmol/l over 4 min) and electrically-induced contraction of isolated extensor digitorum longus (EDL) muscle also doubled the kinase activity of p38 MAPK␣ and p38 MAPK␤. The activity of both isoforms was inhibited in vitro by 10 µmol/l SB203580 in all muscles. To explore the possible participation of p38 MAPK in the stimulation of glucose uptake, EDL and soleus muscles were exposed to increasing doses of SB203580 before and during stimulation by insulin or contraction. SB203580 caused a significant reduction in the insulin-or contractionstimulated 2-deoxyglucose uptake. Maximal inhibition (50-60%) occurred with 10 µmol/l SB203580. These results show that p38 MAPK␣ and -␤ isoforms are activated by insulin and contraction in skeletal muscle. The data further suggest that activation of p38 MAPK may participate in the stimulation of glucose uptake by both stimuli in rat skeletal muscle.

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Section: Discussionmentioning

confidence: 99%

Activation of p38 mitogen-activated protein kinase alpha and beta by insulin and contraction in rat skeletal muscle: potential role in the stimulation of glucose transport.

et al. 2000

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“…Thus, the ability of insulin to stimulate the "intrinsic activity" of the basal pool of GLUT4 in the plasma membrane may not be dependent on cortical F-actin. Another possibility may be that a pre-docked population of GLUT4 protein exists at the membrane, and this pool can fuse and function in the absence of actin regulation, as previously noted in GLUT4 transgenic mice (63). Hence, the ability of insulin to stimulate glucose uptake to some extent during latrunculin B exposure may reflect the uptake of glucose by a pre-existing pool of GLUT4 (possibly obscured to some extent in the t-tubule network), whose activity may also be enhanced by insulin.…”

Section: Discussionmentioning

confidence: 99%

Disruption of Cortical Actin in Skeletal Muscle Demonstrates an Essential Role of the Cytoskeleton in Glucose Transporter 4 Translocation in Insulin-sensitive Tissues

Brozinick

Hawkins

Strawbridge³

et al. 2004

Journal of Biological Chemistry

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103

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Cell culture work suggests that signaling to polymerize cortical filamentous actin (F-actin) represents a required pathway for the optimal redistribution of the insulin-responsive glucose transporter, GLUT4, to the plasma membrane. Recent in vitro study further suggests that the actin-regulatory neural Wiskott-Aldrich syndrome protein (N-WASP) mediates the effect of insulin on the actin filament network. Here we tested whether similar cytoskeletal mechanics are essential for insulin-regulated glucose transport in isolated rat epitrochlearis skeletal muscle. Microscopic analysis revealed that cortical F-actin is markedly diminished in muscle exposed to latrunculin B. Depolymerization of cortical F-actin with latrunculin B caused a time-and concentration-dependent decline in 2-deoxyglucose transport. The loss of cortical F-actin and glucose transport was paralleled by a decline in insulin-stimulated GLUT4 translocation, as assessed by photolabeling of cell surface GLUT4 with Bio-LC-ATB-BMPA. Although latrunculin B impaired insulin-stimulated GLUT4 translocation and glucose transport, activation of phosphatidylinositol 3-kinase and Akt by insulin was not rendered ineffective. In contrast, the ability of insulin to elicit the cortical F-actin localization of N-WASP was abrogated. These data provide the first evidence that actin cytoskeletal mechanics are an essential feature of the glucose transport process in intact skeletal muscle. Furthermore, these findings support a distal actin-based role for N-WASP in insulin action in vivo.

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“…The membrane blocking, probing, and visualization procedure was the same as described in the next paragraph, except that the GLUT4 antibody was used. For the preparation of plasma membranes, ϳ200 mg frozen hindlimb muscle was prepared as described previously by us and others (32). Briefly, muscle was homogenized in a buffer consisting of 255 mmol/l sucrose, 100 mmol/l Tris/HCl, pH 7.6, and 0.2 mmol/l EDTA and centrifuged at 3,400g for 20 min.…”

Section: Methodsmentioning

confidence: 99%

Phosphatidylinositol 3-Kinase Redistribution Is Associated With Skeletal Muscle Insulin Resistance in Gestational Diabetes Mellitus

et al. 2002

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Insulin resistance during pregnancy provokes gestational diabetes mellitus (GDM); however, the cellular mechanisms for this type of insulin resistance are not well understood. We evaluated the mechanisms(s) for insulin resistance in skeletal muscle from an animal model of spontaneous GDM, the heterozygous C57BL/ KsJdb/؉ mouse. Pregnancy triggered a novel functional redistribution of the insulin-signaling environment in skeletal muscle in vivo. This environment preferentially increases a pool of phosphatidylinositol (PI) 3-kinase activity associated with the insulin receptor, away from insulin receptor substrate (IRS)-1. In conjunction with the redistribution of PI 3-kinase to the insulin receptor, there is a selective increase in activation of downstream serine kinases Akt and p70S6. Furthermore, we show that redistribution of PI 3-kinase to the insulin receptor increases insulin-stimulated IRS-1 serine phosphorylation, impairs IRS-1 expression and its tyrosine phosphorylation, and decreases the ability of IRS-1 to bind and activate PI 3-kinase in response to insulin. Thus, the pool of IRS-1-associated PI 3-kinase activity is reduced, resulting in the inability of insulin to stimulate GLUT4 translocation to the plasma membrane. These defects are unique to pregnancy and suggest that redistribution of PI 3-kinase to the insulin receptor may be a primary defect underlying insulin resistance in skeletal muscle during gestational diabetes.

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Glucose transport and GLUT4 protein distribution in skeletal muscle of GLUT4 transgenic mice

Cited by 45 publications

References 26 publications

Activation of p38 mitogen-activated protein kinase alpha and beta by insulin and contraction in rat skeletal muscle: potential role in the stimulation of glucose transport.

Activation of p38 mitogen-activated protein kinase alpha and beta by insulin and contraction in rat skeletal muscle: potential role in the stimulation of glucose transport.

Disruption of Cortical Actin in Skeletal Muscle Demonstrates an Essential Role of the Cytoskeleton in Glucose Transporter 4 Translocation in Insulin-sensitive Tissues

Phosphatidylinositol 3-Kinase Redistribution Is Associated With Skeletal Muscle Insulin Resistance in Gestational Diabetes Mellitus

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