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1.
Can J Physiol Pharmacol ; 83(6): 477-82, 2005 Jun.
Article in English | MEDLINE | ID: mdl-16049547

ABSTRACT

We have previously shown that in vivo lipogenesis is markedly reduced in liver, carcass, and in 4 different depots of adipose tissue of rats adapted to a high protein, carbohydrate-free (HP) diet. In the present work, we investigate the activity of enzymes involved in lipogenesis in the epididymal adipose tissue (EPI) of rats adapted to an HP diet before and 12 h after a balanced diet was introduced. Rats fed an HP diet for 15 days showed a 60% reduction of EPI fatty acid synthesis in vivo that was accompanied by 45%-55% decreases in the activities of pyruvate dehydrogenase complex, ATP-citrate lyase, acetyl-CoA carboxylase, glucose-6-phosphate dehydrogenase, and malic enzyme. Reversion to a balanced diet for 12 h resulted in a normalization of in vivo EPI lipogenesis, and in a restoration of acetyl-CoA carboxylase activity to levels that did not differ significantly from control values. The activities of ATP-citrate lyase and pyruvate dehydrogenase complex increased to about 75%-86% of control values, but the activities of glucose-6-phosphate dehydrogenase and malic enzyme remained unchanged 12 h after diet reversion. The data indicate that in rats, the adjustment of adipose tissue lipogenic activity is an important component of the metabolic adaptation to different nutritional conditions.


Subject(s)
Adipose Tissue/enzymology , Diet , Dietary Carbohydrates/administration & dosage , Dietary Proteins/administration & dosage , Fatty Acids/biosynthesis , Adaptation, Physiological , Adipose Tissue/metabolism , Animals , Epididymis/enzymology , Epididymis/metabolism , Insulin/blood , Male , Rats , Rats, Wistar
2.
Metabolism ; 52(8): 1072-7, 2003 Aug.
Article in English | MEDLINE | ID: mdl-12898476

ABSTRACT

To investigate the effects of prolonged dietary sodium restriction on lipid metabolism, male rats weighing 35 to 40 g (just weaned) were fed either a low-salt (LSD) or a normal salt diet (NSD) and used in metabolic experiments after 1, 2, or 3 months of diet consumption. After 2 and 3 months on the diet, LSD rats showed increased amounts of lipid in carcass and retroperitoneal tissue. In both LSD and NSD, extending the feeding period from 2 to 3 months resulted in a marked reduction in the in vivo rates of adipose tissue fatty acid synthesis that was accompanied by increases in liver lipogenesis and in the activity of adipose tissue lipoprotein lipase (LPL). However, these increases were more marked in LSD rats. Thus, in vivo rates of liver fatty synthesis and LPL activity in LSD rats, which were already higher (by about 35% and 20%, respectively) than in controls after 2 months, attained levels 50% higher than those in NSD animals after another month on the diet. Brown adipose tissue (BAT) thermogenic capacity, estimated after 2 and 3 months by the tissue temperature response to norepinephrine (NE) injection and by guanosine diphosphate (GDP) binding to BAT mitochondria, did not change in controls, but was significantly reduced in LSD rats. This raises the possibility that a decrease in overall energy expenditure, together with an LPL-induced increased uptake of preformed fatty acids from the circulation, may account for the excessive lipid accumulation in LSD rats. Taken together, the data indicate that prolonged dietary sodium restriction exacerbates normal, age-related changes in white and BAT metabolism.


Subject(s)
Adipose Tissue/physiology , Aging/physiology , Diet, Sodium-Restricted/adverse effects , Lipids/biosynthesis , Liver/metabolism , Adipose Tissue, Brown/enzymology , Adipose Tissue, Brown/metabolism , Animals , Body Temperature Regulation/physiology , Body Weight/physiology , Eating/physiology , Fatty Acids/biosynthesis , Glycerol/metabolism , Guanosine Diphosphate/metabolism , Lipoprotein Lipase/biosynthesis , Liver/growth & development , Male , Mitochondria/metabolism , Norepinephrine/pharmacology , Rats , Rats, Wistar , Triglycerides/biosynthesis , Vasoconstrictor Agents/pharmacology
3.
Am J Physiol Regul Integr Comp Physiol ; 285(1): R177-82, 2003 Jul.
Article in English | MEDLINE | ID: mdl-12793997

ABSTRACT

Brown adipose tissue (BAT) glyceroneogenesis was evaluated in rats either fasted for 48 h or with streptozotocin-diabetes induced 3 days previously or adapted for 20 days to a high-protein, carbohydrate-free (HP) diet, conditions in which BAT glucose utilization is reduced. The three treatments induced an increase in BAT glyceroneogenic activity, evidenced by increased rates of incorporation of [1-14C]pyruvate into triacylglycerol (TAG)-glycerol in vitro and a marked, threefold increase in the activity of BAT phosphoenolpyruvate carboxykinase (PEPCK). BAT glycerokinase activity was not significantly affected by fasting or diabetes. After unilateral BAT denervation of rats fed either the HP or a balanced diet, glyceroneogenesis activity increased in denervated pads, evidenced by increased rates of nonglucose carbon incorporation into TAG-glycerol in vivo (difference between 3H2O and [14C]glucose incorporations) and of [1-14C]pyruvate in vitro. PEPCK activity was not significantly affected by denervation. The data suggest that BAT glyceroneogenesis is not under sympathetic control but is sensitive to hormonal/metabolic factors. In situations of reduced glucose use there is an increase in BAT glyceroneogenesis that may compensate the decreased generation of glycerol-3-phosphate from the hexose.


Subject(s)
Adipose Tissue, Brown/enzymology , Glycerol Kinase/metabolism , Glycerol/metabolism , Phosphoenolpyruvate Carboxykinase (GTP)/metabolism , Triglycerides/metabolism , Adipose Tissue, Brown/innervation , Animal Feed , Animals , Carbon Radioisotopes , Denervation , Diabetes Mellitus, Experimental/metabolism , Dietary Carbohydrates/pharmacology , Fasting/physiology , Male , Pyruvic Acid/pharmacokinetics , Rats , Rats, Wistar
4.
Br Poult Sci ; 44(1): 149-54, 2003 Mar.
Article in English | MEDLINE | ID: mdl-12737238

ABSTRACT

1. The role of beta2-agonist and of cAMP in chick skeletal muscle proteolytic pathways and protein synthesis was investigated using an in vitro preparation that maintains tissue glycogen stores and metabolic activity for several hours. 2. In extensor digitorum longus (EDL) muscle total proteolysis decreased by 15 to 20% in the presence of equimolar concentrations of epinephrine, clenbuterol, a selective hbetaagonist, or dibutyryl-cAMP. Rates of protein synthesis were not altered by clenbuterol or dibutyryl-cAMP. 3. The decrease in the rate of total protein degradation induced by 10(-5)M clenbuterol was paralleled by a 44% reduction in Ca2+-dependent proteolysis, which was prevented by 10(-5)M ICI 118.551, a selective fbeta2antagonist. 4. No change was observed in the activity of the lysosomal, ATP-dependent, and ATP-independent proteolytic systems. Ca2+-dependent proteolytic activity was also reduced by 58% in the presence of 10(-4)M dibutyryl-cAMP or isobutylmethylxanthine. 5. The data suggest that catecholamines exert an inhibitory control of Ca2+-dependent proteolysis in chick skeletal muscle, probably mediated by fbeta2adrenoceptors, with the participation of a cAMP-dependent pathway.


Subject(s)
Adrenergic beta-Agonists/pharmacology , Epinephrine/pharmacology , Muscle Proteins/metabolism , Muscle, Skeletal/metabolism , Receptors, Adrenergic, beta-2/physiology , Adrenergic beta-Antagonists/pharmacology , Animals , Bucladesine/pharmacology , Chickens , Clenbuterol/pharmacology , Kinetics , Muscle Proteins/drug effects , Propanolamines/pharmacology , Receptors, Adrenergic, beta-2/drug effects
5.
Am J Physiol Regul Integr Comp Physiol ; 284(6): R1536-41, 2003 Jun.
Article in English | MEDLINE | ID: mdl-12736183

ABSTRACT

The effect of cold exposure (4 degrees C) or prolonged norepinephrine infusion on the activity and mRNA levels of glycerokinase (GyK) was investigated in rat interscapular brown adipose tissue (BAT). Cold exposure for 12 and 24 h induced increases of 30% and 100%, respectively, in the activity of BAT GyK, which was paralleled by twofold and fourfold increase in enzyme mRNA levels. BAT hemidenervation resulted in reductions of 50% and 30% in GyK activity and in mRNA levels, respectively, in denervated pads from rats kept at 25 degrees C, and suppressed in these pads the cold-induced increases in both GyK activity and mRNA levels. The increase in GyK activity induced by cold exposure was not affected by phenoxybenzamine, but was markedly inhibited by previous administration of propranolol or actinomycin D. BAT GyK activity did not change significantly after 6 h of continuous subcutaneous infusion of norepinephrine (20 microg/h), but increased twofold and fourfold after 12 and 24 h, with no further increase after 72 h of infusion. Norepinephrine infusion also activated mRNA production, but the effect was comparatively smaller than that on enzyme activity. beta-Adrenergic agonists also stimulated GyK activity with the following relative magnitude of response: CL316243 (beta(3)) > isoproterenol (non-selective) > dobutamine (beta(1)). In vitro rates of incorporation of glycerol into glyceride-glycerol were increased in BAT from rats exposed to cold. The data suggest that in conditions of a sustained increase in BAT sympathetic flow there is a stimulation of GyK gene expression at the pretranslational level, with increased enzyme activity, mediated by beta-adrenoreceptors, mainly beta(3).


Subject(s)
Adipose Tissue, Brown/enzymology , Adipose Tissue, Brown/innervation , Gene Expression Regulation, Enzymologic , Glycerol Kinase/metabolism , Sympathetic Nervous System/physiology , Adipose Tissue, Brown/drug effects , Adrenergic Agents/pharmacology , Animals , Cold Temperature , Fatty Acids/metabolism , Glycerides/metabolism , Glycerol/metabolism , Male , Norepinephrine/pharmacology , RNA, Messenger/genetics , RNA, Messenger/metabolism , Rats , Rats, Wistar , Sympathectomy , Sympathetic Nervous System/drug effects , Sympathomimetics/pharmacology , Time Factors
6.
Metabolism ; 51(11): 1501-5, 2002 Nov.
Article in English | MEDLINE | ID: mdl-12404205

ABSTRACT

In vivo rates of glucose uptake, insulin-responsive glucose transporter (GLUT4) content, and activities of glycolytic enzymes were determined in brown adipose tissue (BAT) from rats adapted to a high-protein, carbohydrate-free (HP) diet. Adaptation to the HP diet resulted in marked decreases in BAT glucose uptake and in GLUT4 content. Replacement of the HP diet by a balanced control diet for 24 hours restored BAT glucose uptake to levels above those in rats fed the control diet, with no changes in GLUT4 levels in 4 of 5 animals examined. BAT denervation of rats fed the control diet induced a 50% reduction in glucose uptake, but did not significantly affect the already markedly reduced BAT hexose uptake in HP diet-fed rats. It is suggested that the pronounced decrease in BAT glucose uptake in these animals is due to the combined effects of the HP diet-induced reductions in plasma insulin levels and in BAT sympathetic activity. Adaptation to the HP diet was accompanied by decreased activities of hexokinase, phosphofructo-1-kinase, and pyruvate kinase (PK). The activity of BAT PK in HP diet-fed rats was reduced to about 50% of controls, and approached normal levels 24 hours after diet reversion. BAT denervation induced a small (15%) decrease in BAT PK activity in control rats, but did not affect the activity of the enzyme in HP diet-adapted rats. Also, denervation did not interfere with the restoration of PK activity induced by diet substitution. Treatment with anti-insulin serum resulted in an almost 50% reduction in PK activity in both innervated and denervated BAT from rats fed the control diet, but caused a much smaller ( thick approximate 20%) decrease in BAT from HP diet-fed rats. Furthermore, anti-insulin serum administration completely suppressed the restoration of BAT PK activity induced by diet reversion. These data suggest that, differently from glucose uptake, BAT PK activity is predominantly controlled by hormonal/metabolic factors.


Subject(s)
Adipose Tissue, Brown/metabolism , Dietary Proteins/administration & dosage , Glucose/metabolism , Insulin/deficiency , Monosaccharide Transport Proteins/metabolism , Muscle Proteins , Pyruvate Kinase/metabolism , Adipose Tissue, Brown/enzymology , Animals , Blotting, Western , Glucose Transporter Type 4 , Glycolysis , Insulin/immunology , Male , Rats , Rats, Wistar
7.
Metabolism ; 51(3): 343-9, 2002 Mar.
Article in English | MEDLINE | ID: mdl-11887171

ABSTRACT

The effect of denervation or acute insulin deficiency on brown adipose tissue lipogenesis was investigated in rats adapted to a high-protein diet before and after diet reversion to a balanced diet. Denervation of rats fed the balanced diet induced a 50% reduction in in vivo rates of brown adipose tissue fatty acid synthesis, with decreased activities of acetyl-CoA carboxylase and adenosine triphosphate (ATP)-citrate lyase. The markedly (80%) reduced fatty acid synthesis and enzyme activities in brown adipose tissue from rats adapted to the high-protein diet were not affected by denervation. Replacement of the high-protein diet by the balanced diet for 24 hours restored fatty acid synthesis to normal levels, but recovery of enzyme activities was only partial. Lipogenesis restoration and partial recovery of enzyme activities were impaired in denervated tissue from high-protein diet-fed rats. In all experimental conditions, the activities of acetyl-CoA carboxylase and ATP-citrate lyase showed a better correlation with brown adipose tissue lipogenesis than the generators of H(+), glucose-6-P dehydrogenase, and malic enzyme. Anti-insulin serum administration during the 12- to 24-hour period after diet reversion completely blocked lipogenesis recovery in innervated and denervated tissues and drastically reduced brown adipose tissue lipogenesis of concomitantly injected rats fed the balanced diet. The data suggest that efficient and rapid adjustments of brown adipose tissue lipogenesis require sympathetic activation, and that this tissue can maintain significant, albeit reduced, rates of lipogenesis in the absence of sympathetic activation, but not in the absence of insulin.


Subject(s)
Adaptation, Physiological/physiology , Adipose Tissue, Brown/metabolism , Dietary Proteins/administration & dosage , Fatty Acids/biosynthesis , Insulin/physiology , Sympathetic Nervous System/physiology , Animals , Blood Glucose/analysis , Denervation , Dose-Response Relationship, Drug , Enzymes/metabolism , Glucagon/blood , Insulin/blood , Insulin/deficiency , Male , Rats , Rats, Wistar
8.
Am J Physiol Regul Integr Comp Physiol ; 282(4): R1185-90, 2002 Apr.
Article in English | MEDLINE | ID: mdl-11893624

ABSTRACT

The effect of brown adipose tissue (BAT) sympathetic hemidenervation on the activity of glycerokinase (GyK) was investigated in different physiological conditions. In rats fed a balanced diet, the activity of the enzyme was approximately 50% lower in BAT-denervated pads than in intact, innervated pads. In rats adapted to a high-protein, carbohydrate-free diet, norepinephrine turnover rates and BAT GyK activity were already reduced, and BAT denervation resulted in a further decrease in the activity of the enzyme. Cold acclimation of normally fed rats at 4 degrees C for 10 days markedly increased the activity of the enzyme. Cold exposure (4 degrees C) for 6 h was insufficient to stimulate BAT GyK, but the activity of the enzyme was already increased after 12 h of cold exposure. The cold-induced BAT GyK stimulation was completely blocked in BAT-denervated pads. The data indicate that an adequate sympathetic flow to BAT is required for the maintenance of normal levels of GyK activity and for the enzyme response to situations, such as cold exposure, which markedly increase BAT sympathetic flow.


Subject(s)
Adipose Tissue, Brown/enzymology , Adipose Tissue, Brown/innervation , Glycerol Kinase/metabolism , Sympathetic Nervous System/physiology , Acclimatization/physiology , Animals , Cold Temperature , Dietary Carbohydrates , Dietary Proteins/pharmacology , Male , Rats , Rats, Wistar , Sympathectomy
9.
Metabolism ; 50(12): 1493-8, 2001 Dec.
Article in English | MEDLINE | ID: mdl-11735100

ABSTRACT

The effect of cold acclimation on brown adipose tissue (BAT) fatty acid synthesis was investigated in rats adapted to a high-protein, carbohydrate-free diet. At an ambient temperature (25 degrees C), rates of fatty acid synthesis in BAT from rats adapted to the high-protein diet were reduced to 27% of rats fed the balanced diet and increased markedly after cold acclimation (10 days at 4 degrees C), although the increase was smaller than in control rats. BAT weight increase induced by cold acclimation was smaller in rats fed the high-protein diet (30%) than in controls (100%). When expressed per whole tissue, maximal activities of BAT glucose-6-phosphate dehydrogenase, malic enzyme, adenosine triphosphate (ATP)-citrate lyase, and acetyl-coenzyme A carboxylase were markedly reduced in high-protein diet-adapted rats at 25 degrees C and increased after cold acclimation in BAT from the 2 groups. However, when expressed per milligram protein, only acetyl-coenzyme A carboxylase showed an increase in both controls and in rats fed the high-protein diet. G6P-dehydrogenase, malic enzyme, and ATP-citrate lyase increased (per milligram protein) only in rats adapted to the high-protein diet and actually decreased in BAT from cold-acclimated control rats. Initial (before activation) pyruvate dehydrogenase (PDH) complex activity was lower in BAT from rats fed the high-protein diet at 25 degrees C and increased in cold-acclimated rats from the 2 groups. Circulating levels of insulin decreased in the 2 groups after cold acclimation. The data suggest that the cold acclimation-induced increase in BAT lipogenesis in rats adapted to the high-protein diet was due to a restoration of sympathetic activity, which induced both BAT hyperplasia and activation of adipocyte free fatty acid (FFA) synthesis, with an important participation of acetyl-coenzyme A carboxylase and pyruvate dehydrogenase.


Subject(s)
Acclimatization , Adipose Tissue, Brown/metabolism , Cold Temperature , Dietary Carbohydrates/administration & dosage , Dietary Proteins/administration & dosage , Fatty Acids/biosynthesis , ATP Citrate (pro-S)-Lyase/metabolism , Acetyl-CoA Carboxylase/metabolism , Adaptation, Physiological , Adipose Tissue, Brown/anatomy & histology , Animals , Body Temperature , Glucosephosphate Dehydrogenase/metabolism , Malate Dehydrogenase/metabolism , Male , Organ Size , Pyruvate Dehydrogenase Complex/metabolism , Rats , Rats, Wistar
10.
Mol Cell Biochem ; 225(1-): 35-41, 2001 Sep.
Article in English | MEDLINE | ID: mdl-11716362

ABSTRACT

The activity of ATP, ubiquitin (Ub)-dependent proteases partially purified from skeletal muscle (psoas) from alloxan diabetic rabbits was determined at different periods of insulin deficiency. Two days after alloxan injection, no change was observed in the activity of ATP, Ub-dependent proteases, but this activity increased 3 and 5 days after diabetes induction, attaining 181% of control values on the 5th day. However, after this early rise, the activity of muscle ATP, Ub-dependent proteases decreased, returning to values that did not differ significantly from controls 7 and 10 days after alloxan injection. After 15 days, the activity of these proteases was 57% lower than in muscle from control rabbits. Both the initial increase and the subsequent fall in the activity of the enzymes were prevented by insulin treatment of alloxan diabetic rabbits. The data suggest that Ub-proteasome-dependent proteolysis have an important role in the control of muscle protein degradation and may be regulated by insulin.


Subject(s)
Cysteine Endopeptidases/metabolism , Diabetes Mellitus, Experimental/metabolism , Multienzyme Complexes/metabolism , Muscle Proteins/metabolism , Ubiquitins/metabolism , Animals , Blood Glucose/analysis , Fatty Acids/blood , Insulin/pharmacology , Male , Muscle, Skeletal/metabolism , Proteasome Endopeptidase Complex , Rabbits , Time Factors
11.
Metabolism ; 50(10): 1208-12, 2001 Oct.
Article in English | MEDLINE | ID: mdl-11586495

ABSTRACT

Rates of glucose uptake by epididymal and retroperitoneal adipose tissue in vivo, as well as rates of hexose uptake and glycolytic flux in isolated adipocytes, were determined in rats adapted to a high-protein, carbohydrate-free (HP) diet and in control rats fed a balanced (N) diet. Adaptation to the HP diet induced a significant reduction in rates of glucose uptake, estimated with 2-deoxy-[1-(3)H]-glucose, both by adipose tissue (epididymal and retroperitoneal) in vivo and by isolated adipocytes. Twelve hours after replacement of the HP diet with the balanced diet, rates of adipose tissue uptake in vivo in HP-adapted rats returned to levels that did not differ significantly from those in N-fed rats. The rate of flux in the glycolytic pathway, estimated with (3)H[5]-glucose, was also significantly reduced in adipocytes from HP-fed rats. In agreement with the above findings, the activities of hexokinase (HK), phosphofructo-1-kinase (PFK-1), and pyruvate kinase (PK) were markedly reduced in adipose tissue from HP-adapted rats. The activity of pyruvate kinase was partially reverted by diet replacement for 12 hours. The low-plasma insulin and high-glucagon levels in HP-fed rats may have played an important role in the reduction of adipose tissue glucose utilization in these animals.


Subject(s)
Adipose Tissue/metabolism , Carbohydrates/administration & dosage , Glucose/metabolism , Proteins/administration & dosage , Adipose Tissue/cytology , Animals , Carbon Radioisotopes , Epididymis , Glucagon/blood , Glycolysis , Hexokinase/metabolism , Insulin/blood , Male , Phosphofructokinase-1/metabolism , Pyruvate Kinase/metabolism , Rats , Rats, Wistar , Tritium
12.
Am J Physiol Endocrinol Metab ; 281(3): E449-54, 2001 Sep.
Article in English | MEDLINE | ID: mdl-11500299

ABSTRACT

Overall proteolysis and the activity of skeletal muscle proteolytic systems were investigated in rats 1, 2, or 4 days after adrenodemedullation. Adrenodemedullation reduced plasma epinephrine by 95% and norepinephrine by 35% but did not affect muscle norepinephrine content. In soleus and extensor digitorum longus (EDL) muscles, rates of overall proteolysis increased by 15-20% by 2 days after surgery but returned to normal levels after 4 days. The rise in rates of protein degradation was accompanied by an increased activity of Ca(2+)-dependent proteolysis in both muscles, with no significant change in the activity of lysosomal and ATP-dependent proteolytic systems. In vitro rates of Ca(2+)-dependent proteolysis in soleus and EDL from normal rats decreased by ~35% in the presence of either 10(-5) M clenbuterol, a beta(2)-adrenergic agonist, or epinephrine or norepinephrine. In the presence of dibutyryl cAMP, proteolysis was reduced by 62% in soleus and 34% in EDL. The data suggest that catecholamines secreted by the adrenal medulla exert an inhibitory control of Ca(2+)-dependent proteolysis in rat skeletal muscle, mediated by beta(2)-adrenoceptors, with the participation of a cAMP-dependent pathway.


Subject(s)
Calcium/pharmacology , Catecholamines/pharmacology , Cyclic AMP/physiology , Muscle Proteins/metabolism , Muscle, Skeletal/drug effects , Receptors, Adrenergic, beta-2/physiology , Adrenal Medulla/physiology , Adrenal Medulla/surgery , Adrenergic beta-2 Receptor Agonists , Animals , Bucladesine/pharmacology , Catecholamines/physiology , Clenbuterol/pharmacology , Endopeptidases/metabolism , Epinephrine/analysis , Epinephrine/blood , Lysosomes/enzymology , Male , Muscle, Skeletal/chemistry , Muscle, Skeletal/metabolism , Norepinephrine/analysis , Norepinephrine/blood , Rats , Rats, Wistar , Receptors, Adrenergic, beta-2/drug effects
13.
Physiol Behav ; 72(1-2): 175-9, 2001 Jan.
Article in English | MEDLINE | ID: mdl-11239995

ABSTRACT

The physiological significance of central cholinergic neurons was investigated by verifying the effect of previous intracerebroventricular administration of atropine on the hyperglycemia induced by 2-deoxyglucose (2-DG) or by immobilization stress in unrestrained, nonanesthetized rats. Intravenous 2-DG induced a marked increase in plasma glucose that was not affected by atropine injected intracerebroventricularly 30 min before. However, the hyperglycemia induced by intracerebroventricular 2-DG was significantly reduced by previous intracerebroventricular injection of atropine. Immobilization induced a rapid increase of plasma glucose levels that was reduced by about 50% by intracerebroventricular injection of atropine. The increase in plasma lactate induced by intravenous 2-DG, or immobilization, was not significantly affected by previous intracerebroventricular injection of atropine. The data suggest that central cholinergic neurons participate in the complex neural events responsible for the hyperglycemic response to neurocytoglucopenia and to stressful situations.


Subject(s)
Atropine/pharmacology , Hyperglycemia/prevention & control , Muscarinic Antagonists/pharmacology , Stress, Psychological/psychology , Animals , Antimetabolites , Blood Glucose/metabolism , Deoxyglucose , Hyperglycemia/chemically induced , Immobilization , Injections, Intraventricular , Lactic Acid/blood , Male , Rats , Rats, Wistar
14.
J Comp Physiol B ; 170(5-6): 373-7, 2000 Sep.
Article in English | MEDLINE | ID: mdl-11083519

ABSTRACT

The activity of cytoplasmic and mitochondrial phosphoenolpyruvate carboxykinase (PEPCK) in kidney and liver, and in vivo gluconeogenic activity, were determined during different phases of prolonged fasting in quails. The fasting-induced changes in the activity of kidney cytoplasmic PEPCK were positively correlated with the changes in gluconeogenesis. Both activities increased at the initial phase (I) of fasting to levels 65% to 100% higher than fed values, and decreased during the protein-sparing period (phase II), although remaining higher than in fed birds. At the catabolic final phase (III) both kidney cytoplasmic PEPCK activity and gluconeogenesis increased markedly, attaining levels 115% to 150% higher than fed values. The activity of liver cytoplasmic PEPCK, present in appreciable amounts in quails, did not change during phases I and II of fasting, but increased to levels 60% higher than fed values at the final phase (III). Plasma glucose levels at phase III did not differ significantly from those at phases I and II. In both kidney and liver the activity of the mitochondrial PEPCK was not significantly affected by fasting. The data suggest that the kidney cytoplasmic PEPCK is the main enzyme responsible for gluconeogenesis adjustments during food deprivation in quails, and that this function is complemented at the final phase by enzyme present in liver cytosol.


Subject(s)
Fasting/physiology , Gluconeogenesis/physiology , Kidney/enzymology , Liver/enzymology , Phosphoenolpyruvate Carboxykinase (GTP)/metabolism , Animals , Bicarbonates/pharmacokinetics , Blood Glucose , Carbon Radioisotopes , Coturnix , Cytosol/enzymology , L-Lactate Dehydrogenase/metabolism , Male , Mitochondria/enzymology
15.
Am J Physiol Endocrinol Metab ; 279(3): E663-8, 2000 Sep.
Article in English | MEDLINE | ID: mdl-10950836

ABSTRACT

The role of adrenoceptor subtypes and of cAMP on rat skeletal muscle proteolysis was investigated using a preparation that maintains tissue glycogen stores and metabolic activity for several hours. In both soleus and extensor digitorum longus (EDL) muscles, proteolysis decreased by 15-20% in the presence of equimolar concentrations of epinephrine, isoproterenol, a nonselective beta-agonist, or clenbuterol, a selective beta(2)-agonist. Norepinephrine also reduced proteolysis but less markedly than epinephrine. No change in proteolysis was observed when muscles were incubated with phenylephrine, a nonselective alpha-agonist. The decrease in the rate of protein degradation induced by 10(-4) M epinephrine was prevented by 10(-5) M propranolol, a nonselective beta-antagonist, and by 10(-5) M ICI 118.551, a selective beta(2)-antagonist. The antiproteolytic effect of epinephrine was not inhibited by prazosin or yohimbine (selective alpha(1)-and alpha(2)-antagonists, respectively) or by atenolol, a selective beta(1)-antagonist. Dibutyryl cAMP and isobutylmethylxanthine reduced proteolysis in both soleus and EDL muscles. The data suggest that catecholamines exert an inhibitory control of skeletal muscle proteolysis, probably mediated by beta(2)-adrenoceptors, with the participation of a cAMP-dependent pathway.


Subject(s)
Catecholamines/pharmacology , Cyclic AMP/physiology , Muscle Proteins/metabolism , Muscle, Skeletal/metabolism , Receptors, Adrenergic/physiology , 1-Methyl-3-isobutylxanthine/pharmacology , Adenosine Triphosphate/metabolism , Adrenergic alpha-Agonists/pharmacology , Adrenergic alpha-Antagonists/pharmacology , Adrenergic beta-Agonists/pharmacology , Adrenergic beta-Antagonists/pharmacology , Animals , Bucladesine/pharmacology , Glycogen/metabolism , In Vitro Techniques , Male , Muscle Contraction/drug effects , Muscle, Skeletal/drug effects , Phosphocreatine/metabolism , Phosphodiesterase Inhibitors/pharmacology , Rats , Rats, Wistar , Receptors, Adrenergic/drug effects
16.
Am J Physiol ; 277(5): E883-9, 1999 11.
Article in English | MEDLINE | ID: mdl-10567016

ABSTRACT

Overall proteolysis and the activity of skeletal muscle proteolytic systems were investigated in rats submitted to guanethidine-induced adrenergic blockade for 4 days. In soleus, overall proteolysis increased by 15-20% during the first 2 days of guanethidine treatment but decreased to levels below control values after 4 days. Extensor digitorum longus (EDL) did not show the initial increase in total proteolysis, which was already reduced after 2 days of guanethidine treatment. The initial rise in the rate of protein degradation in soleus was accompanied by an increased activity of the Ca(2+)-dependent proteolytic pathway. In both soleus and EDL, the reduction in overall proteolysis was paralleled by decreased activities of the Ca(2+)-dependent and ATP-dependent proteolytic processes. No change was observed in the activity of the lysosomal proteolytic system. Overall proteolysis in soleus and EDL from nontreated rats was partially inhibited by isoproterenol, in vitro. The data suggest an acute inhibitory control of skeletal muscle proteolysis by the adrenergic system, well evident in the oxidative muscle, with an important participation of the Ca(2+)-dependent pathway.


Subject(s)
Adrenergic Agents/pharmacology , Guanethidine/pharmacology , Muscle, Skeletal/drug effects , Muscle, Skeletal/enzymology , Adenosine Triphosphate/metabolism , Adrenal Medulla/chemistry , Adrenergic beta-Agonists/pharmacology , Animals , Calcium/metabolism , Corticosterone/blood , Dopamine/analysis , Dopamine/blood , Endopeptidases/metabolism , Epinephrine/analysis , Epinephrine/blood , Insulin/blood , Isoproterenol/pharmacology , Lysosomes/enzymology , Male , Muscle, Skeletal/chemistry , Norepinephrine/analysis , Norepinephrine/blood , Rats , Rats, Wistar , Testosterone/blood
17.
Peptides ; 20(7): 823-7, 1999.
Article in English | MEDLINE | ID: mdl-10477082

ABSTRACT

Intravenous (IV) administration of angiotensin II (0.95 nmol/100 g body weight) produced a marked increase in plasma glucose of 20 h fasted rats. To investigate the possibility of a stimulation of gluconeogenesis, conscious unrestrained rats were continuously infused with [14C]bicarbonate, 60 microl/min (0.18 microCi/min), and label incorporation into circulating glucose was determined before and after angiotensin injection. The rate of 14C incorporation into blood glucose of fed rats increased significantly after angiotensin II administration, a 279% increase after 20 min (P < 0.01). In conclusion, the results of the present study show that the hyperglycemia induced by intravenous (IV) administration of angiotensin II is accompanied by an activation of gluconeogenesis, as evidenced by a rapid and marked increase in the rate of 14CO2 incorporation into circulating glucose.


Subject(s)
Angiotensin II/administration & dosage , Gluconeogenesis/drug effects , Animals , Blood Glucose/metabolism , Carbon Radioisotopes , Hyperglycemia/blood , Hyperglycemia/chemically induced , Infusions, Intravenous , Kinetics , Liver/drug effects , Liver/metabolism , Rats
18.
Am J Physiol ; 276(4): R1003-9, 1999 04.
Article in English | MEDLINE | ID: mdl-10198378

ABSTRACT

Adaptation of rats to a high-protein, carbohydrate-free (HP) diet induced a marked reduction of brown adipose tissue (BAT) fatty acid (FA) synthesis from both 3H2O and [14C]glucose in vivo, with pronounced decreases in the activities of four enzymes associated with lipogenesis: glucose-6-phosphate dehydrogenase, malic enzyme, citrate lyase, and acetyl-CoA carboxylase. In both HP-adapted and control rats, in vivo incorporation of 3H2O and [14C]glucose into BAT glyceride-glycerol was much higher than into FA. It could be estimated that most of the glycerol synthetized was used to esterify preformed FA. Glycerol synthesis from nonglucose sources (glyceroneogenesis) was increased in BAT from HP rats, as evidenced by an increased capacity of tissue fragments to incorporate [1-14C]pyruvate into glycerol and by a fourfold increase in the activity of phosphoenolpyruvate carboxykinase activity, a key glyceroneogenic enzyme. The data suggest that high rates of glyceroneogenesis and of esterification of preformed FA in BAT from HP-adapted rats are essential for preservation of tissue lipid stores, necessary for heat generation when BAT is recruited in nonshivering thermogenesis.


Subject(s)
Adaptation, Physiological/physiology , Adipose Tissue, Brown/metabolism , Carbohydrates/administration & dosage , Dietary Proteins/administration & dosage , Triglycerides/biosynthesis , Animals , Carboxy-Lyases/metabolism , Diet , Enzymes/metabolism , Lipids/biosynthesis , Male , Rats , Rats, Wistar
19.
Metabolism ; 47(10): 1217-21, 1998 Oct.
Article in English | MEDLINE | ID: mdl-9781624

ABSTRACT

Triacylglycerol (TAG) synthesis from all carbon sources and from glucose carbon was evaluated in rats fed a high-protein, carbohydrate-free (HP) diet or control diet by determining simultaneously in the same animal the rate of incorporation of 3H2O and of 14C-glucose into the two TAG moieties in the carcass, liver, and retroperitoneal and epididymal adipose tissue. Incorporation rates of 3H2O into TAG-fatty acids (FAs) in the two adipose tissues and in liver were reduced in HP rats to about 20% and 50%, respectively, of the rates in control rats. In the two experimental groups, glucose was a poor precursor for FA synthesis, contributing only 22.8% of whole-body (carcass plus liver) total FA synthesis in control rats and even less (14%) in HP rats. In contrast to the reduction in FA synthesis, incorporation of 3H2O into TAG-glycerol in HP rats did not differ significantly or was even higher (in epididymal tissue) versus the control level. In all tissues of both HP and control rats, the rate of 14C-glucose incorporation into TAG-glycerol was much higher than the rate of incorporation into FA. Glyceroneogenesis, estimated by subtracting TAG-glycerol synthesis from glucose from the rate obtained with 3H2O, was significantly increased in adipose tissue from HP rats, with almost all of the glycerol formed by this route being used to esterify preformed FAs. It is suggested that the increased adipose tissue glyceroneogenesis is important for esterification of diet-derived FA and preservation of body fat stores in rats adapted to the HP diet.


Subject(s)
Dietary Carbohydrates/administration & dosage , Dietary Proteins/administration & dosage , Fatty Acids/biosynthesis , Glucose/metabolism , Triglycerides/biosynthesis , Adaptation, Physiological , Animals , Male , Rats , Rats, Wistar
20.
J Auton Nerv Syst ; 69(1): 1-5, 1998 Mar 03.
Article in English | MEDLINE | ID: mdl-9672117

ABSTRACT

Previous studies have shown that adaptation of rats to a high protein, carbohydrate-free (HP) diet results in a marked reduction in brown adipose tissue (BAT) thermogenic capacity. The present experiments were carried out to assess BAT sympathetic activity in HP diet-adapted rats. It was found that interscapular brown adipose tissue (IBAT) norepinephrine (NE) content, fractional turnover rate and calculated rate of turnover were markedly reduced in HP-fed rats. Replacement of the HP diet by a control, balanced diet for 24 h did not affect BAT NE content significantly, but restored fractional turnover rate and turnover rate values to those of control animals. Exposure to cold (4 degrees) for a short period (8 h) induced a marked increase in IBAT NE fractional turnover rate and calculated turnover rate in both HP and control rats. The cold-induced rise of turnover rate over values at ambient temperature (25 degrees C) was higher in HP rats than in controls. Rectal temperature after 8 h of cold exposure did not differ in HP and control rats. The data suggest that the decreased thermogenic capacity of rats adapted to a high protein, carbohydrate-free diet is due to a reduced sympathetic outflow to BAT, which can be rapidly reactivated by cold stimulation.


Subject(s)
Adaptation, Physiological , Adipose Tissue, Brown/innervation , Dietary Carbohydrates/administration & dosage , Dietary Proteins/administration & dosage , Sympathetic Nervous System/physiology , Adaptation, Physiological/physiology , Adipose Tissue, Brown/metabolism , Animals , Body Temperature Regulation/physiology , Cold Temperature , Dietary Proteins/pharmacology , Male , Norepinephrine/metabolism , Rats , Rats, Wistar
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