scholarly journals Statement of Retraction. Gerolama Condorelli, Giovanni Vigliotta, Alessandra Trencia, Maria Alessandra Maitan, Matilde Caruso, Claudia Miele, Francesco Oriente, Stefania Santopietro, Pietro Formisano, and Francesco Beguinot. Protein Kinase C (PKC)-α Activation Inhibits PKC-ζ and Mediates the Action of PED/PEA-15 on Glucose Transport in the L6 Skeletal Muscle Cells. Diabetes 2001;50:1244–1252. DOI: 10.2337/diabetes.50.6.1244. PMID: 11375323

Diabetes ◽  
2019 ◽  
Vol 68 (2) ◽  
pp. 464.2-465
Author(s):  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Glucose Transport ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Kinase C ◽  
Pkc Ζ ◽  
L6 Skeletal Muscle Cells

scholarly journals Protein Kinase C (PKC)-α Activation Inhibits PKC-ζ and Mediates the Action of PED/PEA-15 on Glucose Transport in the L6 Skeletal Muscle Cells

Diabetes ◽  
2001 ◽  
Vol 50 (6) ◽  
pp. 1244-1252 ◽  
Author(s):  
Gerolama Condorelli ◽  
Giovanni Vigliotta ◽  
Alessandra Trencia ◽  
Maria Alessandra Maitan ◽  
Matilde Caruso ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Glucose Transport ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Kinase C ◽  
Pkc Ζ ◽  
L6 Skeletal Muscle Cells

scholarly journals In L6 Skeletal Muscle Cells, Glucose Induces Cytosolic Translocation of Protein Kinase C-α and Trans-activates the Insulin Receptor Kinase

1999 ◽  
Vol 274 (40) ◽  
pp. 28637-28644 ◽  
Author(s):  
Matilde Caruso ◽  
Claudia Miele ◽  
Francesco Oriente ◽  
Alessandra Maitan ◽  
Giuseppe Bifulco ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Insulin Receptor ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Receptor Kinase ◽  
Kinase C ◽  
Insulin Receptor Kinase ◽  
L6 Skeletal Muscle Cells

scholarly journals Interplay and Effects of Temporal Changes in the Phosphorylation State of Serine-302, -307, and -318 of Insulin Receptor Substrate-1 on Insulin Action in Skeletal Muscle Cells

2008 ◽  
Vol 22 (12) ◽  
pp. 2729-2740 ◽  
Author(s):  
Cora Weigert ◽  
Matthias Kron ◽  
Hubert Kalbacher ◽  
Ann Kathrin Pohl ◽  
Heike Runge ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Insulin Receptor ◽  
Insulin Action ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Insulin Signal ◽  
Kinase C ◽  
Phosphorylation Pattern

Abstract Transduction of the insulin signal is mediated by multisite Tyr and Ser/Thr phosphorylation of the insulin receptor substrates (IRSs). Previous studies on the function of single-site phosphorylation, particularly phosphorylation of Ser-302, -307, and -318 of IRS-1, showed attenuating as well as enhancing effects on insulin action. In this study we investigated a possible cross talk of these opposedly acting serine residues in insulin-stimulated skeletal muscle cells by monitoring phosphorylation kinetics, and applying loss of function, gain of function, and combination mutants of IRS-1. The phosphorylation at Ser-302 was rapid and transient, followed first by Ser-318 phosphorylation and later by phosphorylation of Ser-307, which remained elevated for 120 min. Mutation of Ser-302 to alanine clearly reduced the subsequent protein kinase C-ζ-mediated Ser-318 phosphorylation. The Ser-307 phosphorylation was independent of Ser-302 and/or Ser-318 phosphorylation status. The functional consequences of these phosphorylation patterns were studied by the expression of IRS-1 mutants. The E302A307E318 mutant simulating the early phosphorylation pattern resulted in a significant increase in Akt and glycogen synthase kinase 3 phosphorylation. Furthermore, glucose uptake was enhanced. Because the down-regulation of the insulin signal was not affected, this phosphorylation pattern seems to be involved in the enhancement but not in the termination of the insulin signal. This enhancing effect was completely absent when Ser-302 was unphosphorylated and Ser-307 was phosphorylated as simulated by the A302E307E318 mutant. Phospho-Ser-318, sequentially phosphorylated at least by protein kinase C-ζ and a mammalian target of rapamycin/raptor-dependent kinase, was part of the positive as well as of the subsequent negative phosphorylation pattern. Thus we conclude that insulin stimulation temporally generates different phosphorylation statuses of the same residues that exert different functions in insulin signaling.

scholarly journals Phosphorylation of Ser357of Rat Insulin Receptor Substrate-1 Mediates Adverse Effects of Protein Kinase C-δ on Insulin Action in Skeletal Muscle Cells

2008 ◽  
Vol 283 (17) ◽  
pp. 11226-11233 ◽  
Author(s):  
Rizwana Sanaullah Waraich ◽  
Cora Weigert ◽  
Hubert Kalbacher ◽  
Anita M. Hennige ◽  
Stefan Z. Lutz ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Adverse Effects ◽  
Insulin Receptor ◽  
Insulin Action ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Insulin Receptor Substrate ◽  
Kinase C

scholarly journals Palmitate-Induced Interleukin 6 Production Is Mediated by Protein Kinase C and Nuclear-Factor κB Activation and Leads to Glucose Transporter 4 Down-Regulation in Skeletal Muscle Cells

Endocrinology ◽  
2005 ◽  
Vol 146 (7) ◽  
pp. 3087-3095 ◽  
Author(s):  
Mireia Jové ◽  
Anna Planavila ◽  
Juan Carlos Laguna ◽  
Manuel Vázquez-Carrera
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Glucose Transporter ◽  
Muscle Cells ◽  
Nuclear Factor Κb ◽  
Skeletal Muscle Cells ◽  
Mrna Levels ◽  
Nuclear Factor ◽  
Kinase C

Abstract The mechanisms by which elevated levels of free fatty acids cause insulin resistance are not well understood. In addition, accumulating evidence suggests a link between inflammation and type 2 diabetes. Here, we report that exposure of C2C12 skeletal muscle cells to 0.5 mm palmitate results in increased mRNA levels (3.5-fold induction; P < 0.05) and secretion (control 375 ± 57 vs. palmitate 1129 ± 177 pg/ml; P < 0.001) of the proinflammatory cytokine IL-6. Palmitate increased nuclear factor-κB activation and coincubation of the cells with palmitate and the nuclear factor-κB inhibitor pyrrolidine dithiocarbamate prevented both IL-6 expression and secretion. Furthermore, incubation of palmitate-treated cells with calphostin C, a strong and specific inhibitor of protein kinase C, and phorbol myristate acetate, that down-regulates protein kinase C in long-term incubations, abolished induction of IL-6 production. Finally, exposure of skeletal muscle cells to palmitate caused a fall in the mRNA levels of glucose transporter 4 and insulin-stimulated glucose uptake, whereas in the presence of anti-IL-6 antibody, which neutralizes the biological activity of mouse IL-6 in cell culture, these reductions were prevented. These findings suggest that IL-6 may mediate several of the prodiabetic effects of palmitate.

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