scholarly journals Dietary ω 3 fatty acid alters prostaglandin synthesis, glucose transport and protein turnover in skeletal muscle of healthy and diabetic rats

1992 ◽  
Vol 286 (2) ◽  
pp. 405-411 ◽  
Author(s):  
P S Sohal ◽  
V E Baracos ◽  
M T Clandinin

The present study was designed to determine if dietary-fat-induced alterations in the fatty acid composition of skeletal-muscle lipid alters insulin-dependent and basal muscle metabolism, including glucose and amino acid transport, prostaglandin (PG) synthesis and protein turnover. Rats were fed on high-fat semi-purified diets providing 19% or 1% omega 3 fatty acids in the form of fish oil, for 6 weeks. After 3 weeks, half of the rats were made diabetic by a single injection of streptozotocin (50 mg/kg body wt.). After a further 3 weeks, contralateral epitrochlearis and extensor digitorum longus (EDL) muscles from each rat were incubated in vitro. High levels of dietary omega 3 fatty acids decreased PGE2 and PGF2 alpha synthesis in EDL and epitrochlearis muscle (P less than 0.0001). Diabetes and insulin had no effect on PG synthesis. Diet did not alter basal glucose or amino acid transport in EDL muscle from healthy or diabetic rats. Insulin increased glucose and amino acid transport (P less than 0.0001); the increase in glucose transport by insulin was significantly greater in muscles of rats fed on high levels of omega 3 fatty acids (P less than 0.05). Epitrochlearis from rats fed on high levels of omega 3 fatty acids showed decreased net protein degradation in the presence and absence of insulin, owing to decreased rates of protein degradation and synthesis. The data suggest that high levels of dietary omega 3 fatty acids that alter muscle membrane composition also result in alterations in glucose transport and the metabolism of muscle protein.

1992 ◽  
Vol 263 (2) ◽  
pp. E340-E344 ◽  
Author(s):  
E. J. Henriksen ◽  
L. L. Louters ◽  
C. S. Stump ◽  
C. M. Tipton

Prior exercise increases insulin sensitivity for glucose and system A neutral amino acid transport activities in skeletal muscle. Insulin-like growth factor I (IGF-I) also activates these transport processes in resting muscle. It is not known, however, whether prior exercise increases IGF-I action in muscle. Therefore we determined the effect of a single exhausting bout of swim exercise on IGF-I-stimulated glucose transport activity [assessed by 2-deoxy-D-glucose (2-DG) uptake] and system A activity [assessed by alpha-(methylamino)isobutyric acid (MeAIB) uptake] in the isolated rat epitrochlearis muscle. When measured 3.5 h after exercise, the responses to a submaximal concentration (0.2 nM), but not a maximal concentration (13.3 nM), of insulin for activation of 2-DG uptake and MeAIB uptake were enhanced. In contrast, prior exercise increased markedly both the submaximal (5 nM) and maximal (20 nM) responses to IGF-I for activation of 2-DG uptake, whereas only the submaximal response to IGF-I (3 nM) for MeAIB uptake was enhanced after exercise. We conclude that 1) prior exercise significantly enhances the response to a submaximal concentration of IGF-I for activation of the glucose transport and system A neutral amino acid transport systems in skeletal muscle and 2) the enhanced maximal response for IGF-I action after exercise is restricted to the signaling pathway for activation of the glucose transport system.


2019 ◽  
Vol 18 ◽  
pp. 100622
Author(s):  
Katie M. Brown ◽  
Sunita Sharma ◽  
Ella Baker ◽  
William Hawkins ◽  
Marie van der Merwe ◽  
...  

2004 ◽  
Vol 19 (3) ◽  
pp. 1-24 ◽  
Author(s):  
Russell Hyde ◽  
Eric Hajduch ◽  
Darren J. Powell ◽  
Peter M. Taylor ◽  
Harinder S. Hundal

1963 ◽  
Vol 41 (1) ◽  
pp. 397-407 ◽  
Author(s):  
E. Stachiewicz ◽  
J. H. Quastel

Nystatin, an antifungal antibiotic, inhibits the accumulation, by yeast cells, of glycine, leucine, arginine, and alanine at concentrations that have no effect on the respiration of the cells. The uptake of glycine by yeast cells that have been preincubated with nystatin and then suspended in a nystatin-free medium is much lower than that of normal cells. The longer the preincubation with nystatin, the greater is the inhibition of glycine uptake. Nystatin produces two distinct effects. At concentrations below 0.8 μg/ml, nystatin inhibits glycine or arginine uptake. At concentrations from 0.8 to 2.0 μg/ml, it causes an efflux of previously accumulated glycine or arginine. Fatty acids, such as oleic, linoleic, stearic, or palmitic acid, can protect the yeast cell from the action of nystatin. The presence of citrate or versene abolishes the protective action of these fatty acids. Calcium ions also protect the cell from the action of nystatin. The concentration of calcium ions giving complete protection depends upon the nystatin concentration. The implications of these facts on amino acid transport in yeast are discussed.


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