Wyniki wyszukiwania

1

Glucose transport in human peripheral blood lymphocytes influenced by type 2 diabetes mellitus

100%

Pietkiewicz P., Czech A., Taton J.

Archivum Immunologiae et Therapiae Experimentalis

|

2007

|

tom 55

|

nr 2

2

Effects of genistein on insulin pathway-related genes in mouse differentiated myoblast C2C12 cell line: evidence for two independent modes of action

84%

Lewicki S., Lewicka A., Kalicki B., Sobolewska-Ruta A., Debski B., Zdanowski R., Syrylo T., Kloc M., Kubiak J. Z.

Folia Histochemica et Cytobiologica

|

2018

|

tom 56

|

nr 3

3

Effect of tachycardia on lipid metabolism and expression of fatty acid transporters in heart ventricles of the rat

84%

Wojcik B., Harasim E., Zabielski P., Chabowski A., Gorski J.

Journal of Physiology and Pharmacology

|

2015

|

tom 66

|

nr 5

4

Expression of glucocorticoid receptor and glucose transporter-1 during placental development in the diabetic rat

67%

Korgun E. T., Acar N., Sati L., Kipmen-Korgun D., Ozen A., Unek G., Ustunel I., Demir R.

Folia Histochemica et Cytobiologica

|

2011

|

tom 49

|

nr 2

5

Cellular glucose transport and glucotransporter 4 expression as a therapeutic target: clinical and experimental studies

67%

Czech A., Piatkiewicz P., Taton J.

Archivum Immunologiae et Therapiae Experimentalis

|

2009

|

tom 57

|

nr 6

467-473

6

Regulation by exercise of skeletal muscle content of mitochondria and GLUT4

67%

Holloszy J. O.

Journal of Physiology and Pharmacology. Supplement

|

2008

|

tom 59

|

nr 7

7

Treatment with TNF-alpha and IFN-gamma alters the activation of SER-THR protein kinases and the metabolic response to IGF-I in mouse C2C12 myogenic cells

67%

Grzelkowska-Kowalczyk K., Wietelska-Skrzeczynska W.

Cellular and Molecular Biology Letters

|

2010

|

tom 15

|

nr 1

13-31

The aim of this study was to compare the effects of TNF-α, IL-1β and IFN-γ on the activation of protein kinase B (PKB), p70S6k, mitogen-activated protein kinase (MAPK) and p90rsk, and on IGF-I-stimulated glucose uptake and protein synthesis in mouse C2C12 myotubes. 100 nmol/l IGF-I stimulated glucose uptake in C2C12 myotubes by 198.1% and 10 ng/ml TNF-α abolished this effect. Glucose uptake in cells differentiated in the presence of 10 ng/ml IFN-γ increased by 167.2% but did not undergo significant further modification upon the addition of IGF-I. IGF-I increased the rate of protein synthesis by 249.8%. Neither TNF-α nor IFN-γ influenced basal protein synthesis, but both cytokines prevented the IGF-I effect. 10 ng/ml IL-1β did not modify either the basal or IGF-I-dependent glucose uptake and protein synthesis. With the exception of TNF-α causing an 18% decrease in the level of PKB protein, the cellular levels of PKB, p70S6k, p42MAPK, p44MAPK and p90rsk were not affected by the cytokines. IGF-I caused the phosphorylation of PKB (an approximate 8-fold increase above the basal value after 40 min of IGF-I treatment), p42MAPK (a 2.81-fold increase after 50 min), and the activation of p70S6k and p90rsk, manifesting as gel mobility retardation. In cells differentiated in the presence of TNF-α or IFN-γ, this IGF-I-mediated PKB and p70S6k phosphorylation was significantly diminished, and the increase in p42MAPK and p90rsk phosphorylation was prevented. The basal p42MAPK phosphorylation in C2C12 cells treated with IFN-γ was high and comparable with the activation of this kinase by IGF-I. Pretreatment of myogenic cells with IL-1β did not modify the IGF-I-stimulated phosphorylation of PKB, p70S6k, p42MAPK and p90rsk. In conclusion: i) TNF-α and IFN-γ, but not IL-1β, if present in the extracellular environment during C2C12 myoblast differentiation, prevent the stimulatory action of IGF-I on protein synthesis. ii) TNF-α- and IFN-γ-induced IGF-I resistance of protein synthesis could be associated with the decreased phosphorylation of PKB and p70S6k. iii) The activation of glucose uptake in C2C12 myogenic cells treated with IFN-γ is PKB independent. iv) The similar effects of TNF-α and IFN-γ on the signalling and action of IGF-I on protein synthesis in myogenic cells could suggest the involvement of both of these cytokines in protein loss in skeletal muscle.

8

Exposure to TNF-alpha but not IL-1beta impairs insulin-dependent phosphorylation of protein kinase B and p70S6k in mouse C2C12 myogenic cells

67%

Grzelkowska-Kowalczyk K., Wieteska-Skrzeczynska W.

Polish Journal of Veterinary Sciences

|

2006

|

tom 09

|

nr 1

Tumor necrosis factor (TNF)-a is a proinflammatory cytokine considered to play an important role in muscle catabolism, but little is known about the mechanisms of its action. The aim of the present study was therefore to examine the effect of TNF-α pretreatment on glucose uptake and protein synthesis as well as the cellular content and phosphorylation of protein kinase B (PKB), p70S6k, Mitogen Activated Protein (MAP) kinase and p90 rsk in mouse C2C12 myotubes stimulated with insulin. To determine whether interleukin (IL)-lß might be involved in the catabolic action of TNF-α, the effects of IL-lß were also tested. Experiments were performed on mouse C2C12 myoblasts subjected to differentiation in the presence of increasing concentrations of TNF-α (0.1-100 ng/ml) or IL-lß (5-50 ng/ml) for 5 or 6 days. Insulin (100 nmol/1) markedly stimulated glucose uptake in C2C12 myotubes (202.6% of control). This effect was profoundly attenuated by pretreatment with TNF-a at a concentration of 1 ng/ml (122.2% of control) and completely abolished by higher cytokine concentrations. Pretreatment of cells with TNF-a at a concentration of 1 ng/ml was also effective in diminishing the effect of insulin on protein synthesis, whereas higher cytokine concentrations prevented hormonal stimulation of protein synthesis in C2C12 myotubes. Pretreatment with TNF-a caused a significant decrease in PKB protein content. Insulin-mediated activation of protein kinase B was significantly diminished in cells differentiated in the presence of TNF-a. Treatment of C2C12 cells with insulin led to the gel mobility retardation of p70S6k indicating its phosphorylation and activation. In cells differentiated in the presence of TNF-a an approximately 2-fold decrease of insulin-mediated p70s6k phosphorylation was noted. Six-day differentiation of myogenic cells in the presence of TNF-α did not affect the protein content of p42MAPK, p44MAPK, p90rsk and phosphorylation of p42MAPK. Neither glucose uptake nor protein synthesis stimulated by insulin were affected significantly by pretreatment with IL-lß. Preincubation of myogenic cells with IL-lß did not modify either the protein content of PKB and p70S6k or the insulin-stimulated phosphorylation of these kinases. In conclusion: i) high concentrations of TNF-α, but not IL-1 ß, present in the extracellular environment during myoblast differentiation prevent the stimulatory action of insulin on glucose uptake and protein synthesis; ii) insulin resistance induced by TNF-α in C2C12 myogenic cells could be associated with the decreased insulin-mediated phosphorylation of PKB and p70S6k, but not with the basal phosphorylation of p42MAPK.

9

Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik

The influence of oral glucose intake on binding and degradation of 125I-insulin by receptors on erythrocytes as well as on insulin and C-peptide serum levels in patients after myocardial infarction and healthy individuals

59%

Rychlewski T., Szczesniak L., Dylewicz P., Deskur E., Przywarska I., Kasprzak Z., Karolkiewicz J., Konys L.