Selective response of liver enzymes to the administration of different diets after fasting

Niemeyer, Hermann M.; Clark-Turri, Lyllian; Garcés, E; Vergara, Fernando

doi:10.1016/0003-9861(62)90147-9

Cited by 75 publications

(13 citation statements)

References 43 publications

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“…The role of exogenous amino acids does not appear to supply direct sources of the necessary building blocks of G6PDH protein, because essential and nonessential amino acids are equally effective in inducing the dehydrogenase. In fact, some enzymes, such as glucokinase (EC 2.7.1.2) and citrate-cleavage enzyme, could be induced with dietary carbohydrate alone [11,12,19,25]. Obviously, amino acids from labile protein reservers would have supplemented the exogenous essential or nonessential amino acids and replenished the amino acid pool of starved rats to a certain level.…”

Section: Activitiesmentioning

confidence: 99%

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Dual Control of Glucose 6-Phosphate Dehydrogenase Induction in Rat Liver by Dietary Glucose and Amino Acids

Taketa

Kaneshige

Kosaka

1972

Enzyme

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Inhibitory effect of actinomycin D on the induction of glucose 6-phosphate dehydrogenase in rat liver by fasting and refeeding a mixture of glucose and casein was eliminated by a prior glucose feeding, which by itself caused no induction. Refeeding casein alone failed to induce the enzyme even in glucose-prefed rats. Casein could be replaced by essential and nonessential amino acids, or by either alone; thus, no specific amino acids were involved in this enzyme induction. These results suggest that the dietary induced synthesis of glucose 6-phosphate dehydrogenase is regulated by a combination of transcriptional and posttranscriptional mechanisms; the former is dependent on dietary glucose and the latter on both glucose and amino acids.

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Section: Activitiesmentioning

confidence: 99%

“…In view of the fact that some liver enzymes can be induced by administration of either glucose [11,12,19,25] or amino acids [8,12,13,15], it is of some interest to study the role of these two classes of nutrient in the dietary induction of G6PDH.…”

Section: Introductionmentioning

confidence: 99%

Dual Control of Glucose 6-Phosphate Dehydrogenase Induction in Rat Liver by Dietary Glucose and Amino Acids

Taketa

Kaneshige

Kosaka

1972

Enzyme

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“…Induction in the starve-refeed experiment can be blocked by increasing the dietary intake of fat (9)(10)(11)(12)(13)(14)(15)(16), particularly fats containing polyunsaturated fatty acids (12,13,(15)(16)(17). The first set of studies using antibodies raised against G6PD indicated that enzyme activity was increased by an increase in the rate of synthesis of titratable enzyme protein (18)(19)(20); there was no indication of a conversion from inactive to active species to account for the increased activity observed.…”

mentioning

confidence: 99%

The in Vitro Stability of Rat Liver Glucose-6-Phosphate Dehydrogenase as a Function of Diet

Szepesi

Safir

1983

Experimental Biology and Medicine

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Rat liver glucose-6-phosphate dehydrogenase (G6PD) activity was studied in starvedrefed rats given diets containing three levels of fat (35%, high-fat; 5%, low-fat; 0%, fat-free). Elution characteristics from DEAE-cellulose, K,,, for glucose-6-phosphate, pH optimum, and molecular weight appeared to be similar. During storage or heat denaturation, stability apparently was lowest of G6PD of livers from rats refed the high-fat diet. Heat stability was enhanced by the addition of NADP, but some differences due to diet persisted. Titration of a constant amount of enzyme with heating gave inconsistent results: in two of four experiments rats refed the highfat diet had an equivalence point twice that of rats refed the fat-free diet. This difference disappeared if the antibody titration was camed out in the cold. The diet-induced instability of the G6PD, as measured in vitro, was reversible by changing the diet of the rats.

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“…De nombreuses études enzymologiques on été pratiquées sur des rats subissant des séquences de jeûne-réalimcntation [3,15,21,26] tandis que bien moins nombreux sont les travaux relatifs aux ré percussions des carences protidiques intermittentes sur l'activité des enzymes qui peuvent être impliquées dans les processus de lipogenèse [6,9,12,24] …”

unclassified

Activités enzymatiques du foie et du tissu adipeux pendant le jeûne total ou le jeûne protéique et la réalimentation équilibrée ultérieure

Jomain¹,

Loriette²,

Macaire³

1970

Ann Nutr Metab

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Activities of enzymes involved in glucose phosphorylation, glucokinase (EC 2.7.1.2.), hexokinase (EC 2.7.1.1.), glucose 6-phosphatase (EC 3.1.3.9.), and in NADPH production, glucose-6-phosphate dehydrogenase (EC 1.1.1.49), 6-phospho-gluconate dehydrogenase (EC 1.1.1.44), NADP Malate-dehydrogenase (EC 1.1.1.40), were studied in rat liver and adipose tissue during fasting-refeeding and protein depletion-repletion. Fasting induced an increased activity of glucose-6-phosphatase and a sharp decrease in all other activities in both liver and adipose tissue hexokinase, dehydrogenases of the pentose shunt and NADP-Malate dehydrogenase. These activities have long been associated with adaptative hyperlipogenesis. In our experiments adaptation was more evident in liver than adipose tissue. On the other hand, protein-depletion alone did not change glucose availability or glucose 6-phosphatase activity. Protein repletion did not induce any hyperactivity of glucokinase, adipose tissue hexokinase, nor dehydrogenases, evidencing a lack of hyper-lipogenesis.

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Selective response of liver enzymes to the administration of different diets after fasting

Cited by 75 publications

References 43 publications

Dual Control of Glucose 6-Phosphate Dehydrogenase Induction in Rat Liver by Dietary Glucose and Amino Acids

Dual Control of Glucose 6-Phosphate Dehydrogenase Induction in Rat Liver by Dietary Glucose and Amino Acids

The in Vitro Stability of Rat Liver Glucose-6-Phosphate Dehydrogenase as a Function of Diet

Activités enzymatiques du foie et du tissu adipeux pendant le jeûne total ou le jeûne protéique et la réalimentation équilibrée ultérieure

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