Characterization of the relation between sodium channels and electrical activity in cultured rat skeletal myotubes: regulatory aspects

Brodie, Chaya; Brody, Michael J.; Sampson, Sanford R.

doi:10.1016/0006-8993(89)90708-7

Cited by 49 publications

(39 citation statements)

References 25 publications

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“…The preparation of primary skeletal muscle cultures obtained from neonatal rat pups is a useful model for the study of blood glucose regulation by insulin. The mature fibers display resting membrane action potentials that are nearly identical to those seen in vivo, and the physiological expression of a number of membrane proteins in these cells, in contrast to muscle cell lines, closely resembles that observed in vivo (7,8). The first step of insulin-induced glucose transport is the binding of insulin to its receptor and the initiation of receptor tyrosine kinase activity.…”

mentioning

confidence: 62%

Activation of Protein Kinase Cζ Induces Serine Phosphorylation of VAMP2 in the GLUT4 Compartment and Increases Glucose Transport in Skeletal Muscle

Braiman

Alt

Kuroki

et al. 2001

Molecular and Cellular Biology

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Insulin stimulates glucose uptake into skeletal muscle tissue mainly through the translocation of glucose transporter 4 (GLUT4) to the plasma membrane. The precise mechanism involved in this process is presently unknown. In the cascade of events leading to insulin-induced glucose transport, insulin activates specific protein kinase C (PKC) isoforms. In this study we investigated the roles of PKC in insulin-stimulated glucose uptake and GLUT4 translocation in primary cultures of rat skeletal muscle. We found that insulin initially caused PKC to associate specifically with the GLUT4 compartments and that PKC together with the GLUT4 compartments were then translocated to the plasma membrane as a complex. PKC and GLUT4 recycled independently of one another. To further establish the importance of PKC in glucose transport, we used adenovirus constructs containing wild-type or kinase-inactive, dominant-negative PKC (DNPKC) cDNA to overexpress this isoform in skeletal muscle myotube cultures. We found that overexpression of PKC was associated with a marked increase in the activity of this isoform. The overexpressed, active PKC coprecipitated with the GLUT4 compartments. Moreover, overexpression of PKC caused GLUT4 translocation to the plasma membrane and increased glucose uptake in the absence of insulin. Finally, either insulin or overexpression of PKC induced serine phosphorylation of the GLUT4-compartment-associated vesicle-associated membrane protein 2. Furthermore, DNPKC disrupted the GLUT4 compartment integrity and abrogated insulin-induced GLUT4 translocation and glucose uptake. These results demonstrate that PKC regulates insulin-stimulated GLUT4 translocation and glucose transport through the unique colocalization of this isoform with the GLUT4 compartments.

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mentioning

confidence: 62%

Activation of Protein Kinase Cζ Induces Serine Phosphorylation of VAMP2 in the GLUT4 Compartment and Increases Glucose Transport in Skeletal Muscle

Braiman

Alt

Kuroki

et al. 2001

Molecular and Cellular Biology

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“…Na ϩ currents in developing cortical neurons also show a corresponding upregulation when electrical activity is blocked chronically with TTX (143). Similar activity-dependent downregulation of Na ϩ channels occurs in skeletal and cardiac muscle cells (77,105,452,538), where there is direct evidence that the effects are secondary to Ca 2ϩ entry. Activity has been reported to upregulate Na ϩ channel density in a Ca 2ϩ -dependent manner in GH3 cells (417 (528).…”

Section: ؉ -Gated Channelsmentioning

confidence: 76%

Ion Channel Development, Spontaneous Activity, and Activity-Dependent Development in Nerve and Muscle Cells

Moody¹,

Bosma²

2005

Physiological Reviews

345

323

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At specific stages of development, nerve and muscle cells generate spontaneous electrical activity that is required for normal maturation of intrinsic excitability and synaptic connectivity. The patterns of this spontaneous activity are not simply immature versions of the mature activity, but rather are highly specialized to initiate and control many aspects of neuronal development. The configuration of voltage- and ligand-gated ion channels that are expressed early in development regulate the timing and waveform of this activity. They also regulate Ca2+ influx during spontaneous activity, which is the first step in triggering activity-dependent developmental programs. For these reasons, the properties of voltage- and ligand-gated ion channels expressed by developing neurons and muscle cells often differ markedly from those of adult cells. When viewed from this perspective, the reasons for complex patterns of ion channel emergence and regression during development become much clearer.

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“…The mature fibers display resting membrane and action potentials that are nearly identical to those seen in vivo. In addition, the physiological expression of a number of membrane proteins in this preparation, in contrast to muscle cell lines such as L6, closely resemble that obtained in vivo (31)(32)(33). In this study, we investigated the possibility that TNF-␣ may differentially affect the interaction of specific PKC isoforms with upstream elements in the IR signaling cascade to modulate IR signaling.…”

mentioning

confidence: 92%

Differential Effects of Tumor Necrosis Factor-α on Protein Kinase C Isoforms α and δ Mediate Inhibition of Insulin Receptor Signaling

et al. 2002

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Tumor necrosis factor-␣ (TNF-␣) is a multifunctional cytokine that interferes with insulin signaling, but the molecular mechanisms of this effect are unclear. Because certain protein kinase C (PKC) isoforms are activated by insulin, we examined the role of PKC in TNF-␣ inhibition of insulin signaling in primary cultures of mouse skeletal muscle. TNF-␣, given 5 min before insulin, inhibited insulin-induced tyrosine phosphorylation of insulin receptor (IR), IR substrate (IRS)-1, insulin-induced association of IRS-1 with the p85 subunit of phosphatidylinositol 3-kinase (PI3-K), and insulin-induced glucose uptake. Insulin and TNF-␣ each caused tyrosine phosphorylation and activation of PKCs ␦ and ␣, but when TNF-␣ preceded insulin, the effects were less than that produced by each substance alone.

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Characterization of the relation between sodium channels and electrical activity in cultured rat skeletal myotubes: regulatory aspects

Cited by 49 publications

References 25 publications

Activation of Protein Kinase Cζ Induces Serine Phosphorylation of VAMP2 in the GLUT4 Compartment and Increases Glucose Transport in Skeletal Muscle

Activation of Protein Kinase Cζ Induces Serine Phosphorylation of VAMP2 in the GLUT4 Compartment and Increases Glucose Transport in Skeletal Muscle

Ion Channel Development, Spontaneous Activity, and Activity-Dependent Development in Nerve and Muscle Cells

Differential Effects of Tumor Necrosis Factor-α on Protein Kinase C Isoforms α and δ Mediate Inhibition of Insulin Receptor Signaling

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