The mechanism of action of insulin on phospholipid metabolism in rat adipose tissue. Requirement for protein synthesis and a carbohydrate source, and relationship to activation of pyruvate dehydrogenase

Diabetes ◽  
1984 ◽  
Vol 33 (7) ◽  
pp. 648-655 ◽  
Author(s):  
R. V. Farese ◽  
R. V. Farese ◽  
M. A. Sabir ◽  
R. E. Larson ◽  
W. L. Trudeau ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Adipose Tissue ◽  
Mechanism Of Action ◽  
Pyruvate Dehydrogenase ◽  
Phospholipid Metabolism ◽  
Carbohydrate Source ◽  
Rat Adipose Tissue

scholarly journals Phosphatidic acid and phosphatidylinositol labelling in adipose tissue. Relationship to the metabolic effects of insulin and insulin-like agents

1983 ◽  
Vol 212 (2) ◽  
pp. 489-498 ◽  
Author(s):  
T W Honeyman ◽  
W Strohsnitter ◽  
C R Scheid ◽  
R J Schimmel
Keyword(s):  
Adipose Tissue ◽  
Phospholipase C ◽  
Pyruvate Dehydrogenase ◽  
Enzyme Activities ◽  
Glycogen Synthase ◽  
Sugar Transport ◽  
Phospholipid Metabolism ◽  
Metabolic Effects ◽  
Isolated Adipocytes ◽  
Rat Adipose Tissue

Exposure to phospholipase C increased the incorporation of [32P]Pi into phosphatidate, CMP-phosphatidate and phosphatidylinositol in rat adipose tissue and isolated adipocytes. A similar effect was observed in response to insulin and oxytocin. Theophylline, 3-isobutyl-1-methylxanthine and adenosine deaminase decreased [32P]Pi incorporation, and adenosine and N6-phenylisopropyladenosine reversed these effects. As with insulin, exposure of adipose tissue to phospholipase C stimulated oxidation of glucose, pyruvate and leucine and activated pyruvate dehydrogenase. Oxytocin and adenosine also mimicked the effects of insulin on leucine oxidation and pyruvate dehydrogenase. However, only insulin stimulated glycogen synthase activity, indicating that the regulation of synthase may be achieved by intracellular events distinct from those regulating changes in phospholipid metabolism, sugar transport and mitochondrial enzyme activities. It is postulated that exposure to phospholipase C forms diacylglycerol, which is phosphorylated to yield phosphatidate. The increased labelling of CMP-phosphatidate and phosphatidylinositol results from the conversion of phosphatidate into these lipids. The correlation between the effects of phospholipase C on phosphatidate synthesis and changes in adipose-tissue metabolism suggests the possibility that increased phosphatidate may directly or indirectly produce changes in membrane transport and enzyme activities. The pattern of phospholipid labelling produced by insulin, adenosine and oxytocin suggests that these stimuli may also increase phosphatidate synthesis, and, if so, changes in phospholipid metabolism could account for some of the metabolic actions of these stimuli.

scholarly journals Effects of glucose and insulin on the activation of lipoprotin lipase and on protein-synthesis in rat adipose tissue

1980 ◽  
Vol 188 (1) ◽  
pp. 193-199 ◽  
Author(s):  
S M Parkin ◽  
K Walker ◽  
P Ashby ◽  
D S Robinson
Keyword(s):  
Protein Synthesis ◽  
Enzyme Activity ◽  
Adipose Tissue ◽  
Lipoprotein Lipase ◽  
Specific Activity ◽  
The Other ◽  
Lipoprotein Lipase Activity ◽  
Fat Bodies ◽  
Rat Adipose Tissue ◽  
Adipose Tissue Lipoprotein Lipase

Glucose, and certain sugars that can readily be converted to glucose 6-phosphate, bring about an activation of adipose-tissue lipoprotein lipase when epididymal fat-bodies from starved rats are incubated in the presence of cycloheximide. Other substrates do not support the activation. If the tissue is preincubated in the presence of cycloheximide for longer than 2h, the ability of added glucose to activate the enzyme is lost. On the other hand, the addition of glucose still brings about an increase in lipoprotein lipase activity after preincubation in the absence of cycloheximide for as long as 4h. The magnitude of the increase in enzyme activity brought about by the addition of glucose is increased when protein synthesis is stimulated during the preincubation period by insulin. The results are interpreted in terms of the existence in adipose tissue of a proenzyme pool of lipoprotein lipase that is normally maintained by protein synthesis and that is converted to complete enzyme of higher specific activity by a process that specifically requires glucose.

scholarly journals The effect of insulin and glucocorticoids on the synthesis and degradation of phosphoenolpyruvate carboxykinase (GTP) in rat adipose tissue cultured in vitro

1976 ◽  
Vol 158 (1) ◽  
pp. 9-16 ◽  
Author(s):  
O Meyuhas ◽  
L Reshef ◽  
F J Ballard ◽  
R W Hanson
Keyword(s):  
Protein Synthesis ◽  
Adipose Tissue ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Epididymal Adipose Tissue ◽  
Large Size ◽  
A Value ◽  
Rat Adipose Tissue ◽  
Synthesis And Degradation

1. Epididymal adipose tissue from the rat was maintained in culture for periods of up to 96h. 2. After an initial decrease in protein synthesis during the first 24h of culture, the adipose tissue recovered its capacity to synthesize and accumulate proteins of a relatively large size. 3. The activity of phosphoenolpyruvate carboxykinase decreased in a parallel manner, but increased again after 24h of incubation of the tissue in culture, to a value twice that noted in the tissue in vivo. This increase in enzyme activity was due to an increase in its rate of synthesis. 4. Both insulin and dexamethasone (9alpha-fluoro-16alpha-methyl-11beta,17,-21-trihydroxypregna-1,4-diene-3,20-dione) inhibited phosphoenolpyruvate carboxykinase synthesis, but dexamethasone also decreased total protein synthesis. 5. The half-life of phosphoenolpyruvate carboxykinase in adipose tissue cultured in vitro was 5-7h and was not altered by insulin or dexamethasone. 6. It is concluded that both insulin and glucocroticoids lower the activity of phosphoenolpyruvate carboxykinase in rat adipose tissue by decreasing its rate of synthesis.

Specificity of insulin or oxytocin stimulation of protein synthesis in adipose tissue

1964 ◽  
Vol 207 (5) ◽  
pp. 1169-1172 ◽  
Author(s):  
M. E. Krahl
Keyword(s):  
Protein Synthesis ◽  
Adipose Tissue ◽  
Glucose Uptake ◽  
Lipid Synthesis ◽  
Specific Effect ◽  
Acetate Incorporation ◽  
Enhance Protein Synthesis ◽  
Rat Adipose Tissue ◽  
Synthetic Oxytocin

Insulin stimulates glucose uptake, fat synthesis, and incorporation of amino acids into protein of rat adipose tissue. Other agents having insulinlike effects on glucose metabolism have now been tested for their ability to promote protein synthesis in this in vitro system. Rat epididymal fat pads were incubated in Krebs bicarbonate medium containing glucose or pyruvate, acetate-1-C14 as precursor for lipids, or (in separate experiments) histidine-2(ring)-C14 as precursor for protein. Glucose uptake was measured by the glucose oxidase method, and radioactivity of lipid and protein fractions was estimated. Synthetic oxytocin (Sandoz), 0.1–10 U/ml, stimulated glucose uptake, acetate incorporation into lipid, and histidine-C14 incorporation into protein when glucose was present; unlike insulin, oxytocin did not enhance protein synthesis when pyruvate replaced glucose in the medium. RNA (1 mg/ml), nicotinic acid (0.001 m), and protamine sulfate (1 mg/ml) each stimulated glucose uptake and acetate incorporation into lipid, but did not enhance histidine-C14 incorporation into protein. It is concluded that in adipose tissue insulin has a specific effect on protein synthesis which cannot be mimicked by other agents which stimulate glucose uptake or lipid synthesis.

scholarly journals Effects of insulin, glucocorticoids and adrenaline on the activity of rat adipose-tissue lipoprotein lipase

1980 ◽  
Vol 188 (1) ◽  
pp. 185-192 ◽  
Author(s):  
P Ashby ◽  
D S Robinson
Keyword(s):  
Protein Synthesis ◽  
Adipose Tissue ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipoprotein Lipase Activity ◽  
Fat Bodies ◽  
Rat Adipose Tissue ◽  
Adipose Tissue Lipoprotein Lipase

The lipoprotein lipase activity of epididymal fat-bodies from starved rats was measured during incubations at 37 degrees C in vitro. Protein synthesis independent activation of the enzyme, previously observed during incubations at 25 decrease C, also occurs at 37 degrees C. Protein-synthesis-dependent increases in the activity of the enzyme occur in the presence of insulin and are markedly potentiated by glucocorticoids. The effects on the activity of the enzyme of insulin alone, or in the presence of glucocorticoids, are correlated with its effects on total protein synthesis in the tissue. Adrenaline antagonizes the increase in activity of the enzyme brought about by insulin and abolishes the potentiation of insulin action by glucocorticoids. These changes may be due, at least in part, to its stimulation of inactivation of the enzyme in the tissue. It is suggested that changes in adipose-tissue lipoprotein lipase activity that occur with changes in nutritional status in vivo result from the combined effects of changes in plasma insulin and glucocorticoid concentrations.

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