Effects of Adrenalectomy, Adrenalectomy–Ovariectomy, and Cortisol and Estrogen Therapies Upon Enzyme Activities in Lactating Rat Mammary Glands

1972 ◽  
Vol 50 (4) ◽  
pp. 366-376 ◽  
Author(s):  
G. O. Korsrud ◽  
R. L. Baldwin
Keyword(s):  
Pyruvate Kinase ◽  
Enzyme Activities ◽  
Secretory Cell ◽  
Succinic Dehydrogenase ◽  
Mammary Glands ◽  
Pentose Phosphate ◽  
Phosphogluconate Dehydrogenase ◽  
Udpglucose Pyrophosphorylase ◽  
Cleavage Enzyme ◽  
Glucose 6 Phosphate Dehydrogenase

The effects of adrenalectomy and adrenalectomy–ovariectomy on the 5th day of lactation followed by cortisol and estrogen therapies on enzyme activities in rat mammary glands were investigated. This stage of lactation was selected because mammary secretory cell proliferation is essentially complete at this time thereby enabling study of the effects of cortisol and estrogen on enzyme levels in a nonproliferating secretory cell population. Eighteen enzymes were selected for study on the bases of their respective roles in milk biosynthesis and carbohydrate and energy metabolism and/or on the basis of previous studies indicating that their activities increase during midlactation or are regulated, in part, by steroid hormones. After adrenalectomy on the 5th day of lactation, cortisol therapy was required for normal increases in the activities of succinic dehydrogenase, citrate cleavage enzyme, malic enzyme, UDPglucose pyrophosphorylase, UDPglucose 4-epimerase, and glucose-6-phosphate dehydrogenase. The activities of UDPglucose pyrophosphorylase and glucose-6-phosphate dehydrogenase were higher than normal in cortisol-treated animals. Cortisol therapy during the last 2 days of the experiment increased the activity of UDPglucose pyrophosphorylase and possibly citrate cleavage enzyme. The activities of α-glycerolphosphate dehydrogenase, phosphoglucomutase, 6-phosphogluconate dehydrogenase, pentose phosphate metabolizing ability, hexokinase, phosphofructokinase, fructose-1,6-diphosphate aldolase, pyruvate kinase, lactic dehydrogenase, aspartate aminotransferase, isocitrate dehydrogenase, and extramitochondrial malate dehydrogenase were not notably affected by adrenalectomy or cortisol therapy. The activities of 6-phosphogluconate dehydrogenase, pentose phosphate metabolizing ability, phosphofructokinase, and pyruvate kinase may have increased after the 5th day of lactation in adrenalectomized as well as in normal animals. Combining ovariectomy with adrenalectomy reduced pup weight gains more than adrenalectomy alone, but did not further decrease significantly the activities of any of the enzymes measured. Ovariectomy had no effect when cortisol was administered. Cortisol therapy completely reversed adverse effects of estrogen given to adrenalectomized–ovariectomized animals. On the bases of these and previous data, it was concluded that cortisol regulates the rates of synthesis of several mammary gland enzymes during midlactation.

Estimations of Rates of Synthesis and Degradation of Several Rat Mammary Gland Enzymes from Changes in Enzyme Activities

1972 ◽  
Vol 50 (4) ◽  
pp. 386-391 ◽  
Author(s):  
G. O. Korsrud ◽  
R. L. Baldwin
Keyword(s):  
Fatty Acid ◽  
Malic Enzyme ◽  
Fatty Acid Synthetase ◽  
Mammary Glands ◽  
Phosphogluconate Dehydrogenase ◽  
Udpglucose Pyrophosphorylase ◽  
Cleavage Enzyme ◽  
Rat Mammary Gland ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Synthesis And Degradation

Based upon rates of decrease in the activities of citrate cleavage enzyme (EC 4.1.3.7), malic enzyme (EC 1.1.1.40), fatty acid synthetase, UDPglucose pyrophosphorylase (EC 2.7.7.9), UDPglucose 4-epimerase (EC 5.1.3.3), and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) in rat mammary glands after adrenalectomy–ovariectomy on the 11th day of lactation, the half-lives of the enzymes were estimated to be 28, 31, 28, 50, 20, and 24 h, respectively. The half-life estimates for UDPglucose pyrophosphorylase and glucose-6-phosphate dehydrogenase compared favorably with previous estimates of 35 and 20 h, respectively, obtained in rats 5 days postpartum utilizing specific immunological techniques. In a second experiment, increases in the activities of enzymes in adrenalectomized, lactating rats after initiation of cortisol therapy were investigated. Rats were adrenalectomized on the 5th day of lactation and cortisol therapy was started 5 days later. The estimated half-lives for citrate cleavage enzyme, malic enzyme, fatty acid synthetase, UDPglucose pyrophosphorylase, UDPglucose 4-epimerase, the A protein of the lactose synthetase complex, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase (EC 1.1.1.44), and hexokinase (EC 2.7.1.1) were, respectively, 84, 60, 92, 76, 170, 102, 79, 88, and 81 h.

scholarly journals Antioxidant SMe1EC2 modulates pentose phosphate pathway and glutathione-dependent enzyme activities in tissues of aged diabetic rats

2017 ◽  
Vol 10 (4) ◽  
pp. 148-154 ◽  
Author(s):  
Nuray Nuriye Ulusu ◽  
Müslüm Gök ◽  
Arzu Ayşe Sayin Şakul ◽  
Nuray Ari ◽  
Milan Stefek ◽  
...  
Keyword(s):  
Pentose Phosphate Pathway ◽  
Enzyme Activities ◽  
Body Weight Loss ◽  
Diabetic Rats ◽  
Pentose Phosphate ◽  
Aged Rats ◽  
Glutathione S Transferase ◽  
Phosphogluconate Dehydrogenase ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
And Control

Abstract The pentose phosphate pathway and glutathione-associated metabolism are the main antioxidant cellular defense systems. This study investigated the effects of the powerful antioxidant SMe1EC2 (2-ethoxycarbonyl-8-methoxy-2,3,4,4a,5,9b-hexahydro-1H-pyrido[4,3-b] indolinium dichloride) on pentose phosphate pathway (PPP) and glutathione-dependent enzyme activities in aged diabetic and aged matched control rats. Diabetes was induced by streptozotocin injection in rats aged 13-15 months. Diabetic and control rats were divided into two subgroups, one untreated and one treated with SMe1EC2 (10 mg/kg/day, orally) for 4 months. SMe1EC2 ameliorated body weight loss, but not hyperglycemia of aged diabetic rats. Diabetes resulted in decreased glucose-6-phosphate dehydrogenase (G6PD), 6-phosphogluconate dehydrogenase (6PGD) and glutathione-S-transferase (GST), yet in unchanged glutathione reductase (GR) in the liver of aged diabetic rats. In the liver of the aged control rats, SMe1EC2 did not affect G6PDH, 6PGDH and GR, but it inhibited GST. SMe1EC2 also failed to affect diabetes-induced decline in 6PGDH, it ameliorated G6PDH but produced further decline in GST in the liver of aged diabetic rats. In the kidney of aged rats, G6PDH and GST were found to be comparable among the groups, but diabetes up-regulated 6PGDH and GR; these alterations were prevented by SMe1EC2. In the heart of aged diabetic rats, while GST remained unchanged, the recorded increase in G6PD, 6PGD, GR was prevented by SMe1EC2. Furthermore, an unchanged GR and remarkable increases in G6PD, 6PGD and GST were found in the lung of the aged diabetic group. These alterations were completely prevented by SMe1EC2. The results suggest that in aged rats SMe1EC2 can ameliorate the response of the kidney, heart and lung but not that of the liver against diabetes-induced glucotoxicity by interfering with the activity of redox network enzymes.

II. Lokalisation von Enzymen des reduktiven und dem oxydativen Pentosephosphat-Zyklus in den Chloroplasten und Permeabilität der Chloroplasten-Membran gegenüber Metaboliten

1967 ◽  
Vol 22 (11) ◽  
pp. 1200-1215 ◽  
Author(s):  
U. Heber ◽  
U. W. Hallier ◽  
M. A. Hudson ◽  
B. von der Groeben ◽  
R. Ernst ◽  
...  
Keyword(s):  
Pentose Phosphate Pathway ◽  
Enzyme Activities ◽  
Intracellular Localization ◽  
Pentose Phosphate ◽  
Oxidative Pentose Phosphate Pathway ◽  
Amino Acid Synthesis ◽  
Phosphogluconate Dehydrogenase ◽  
Chloroplast Membrane ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Isolated Chloroplasts

1. The interrelationship of metabolic activities in chloroplasts and cytoplasm of leaf cells of spinach, sugar beet and Elodea has been investigated. Different methods have been adopted to study the intracellular localization of enzymes and the flow of phosphorylated intermediates across the chloroplast membrane. The flow of substrates was investigated by determining the rates of the conversion of substrates added to aqueously isolated chloroplasts, prior to and after destruction of the outer chloroplast membrane. The observed differences yielded information as to whether a substrate could traverse the chloroplast membrane.Two methods mere used to investigate the localization of enzymes :a) The percentage distribution of photosynthetic and respiratory enzymes in chloroplasts and cytoplasm was calculated from data on enzyme activities in non-aqueous cell fractions.b) Low levels of enzymes in chloroplasts in the presence of high cytoplasmatic levels were detected by assaying enzyme activities in preparations of aqueously isolated chloroplasts prior to and after ultrasonic destruction of the outer chloroplast membrane.2. If chloroplasts are isolated in aqueous sucrose buffer, their outer membranes act as an efficient barrier against the penetration of NADP, RuDP, GAP and, in some but not all experiments, of FMP and GMP. PGA, DHAP and, probably to a lesser extent, aspartate, ɑ-ketoglutarate, oxaloacetate and FDP can traverse this membrane. Chloroplast membranes are significantly altered when isolated in NaCI-buffer systems and do not correspond to the in vivo situation.3. The conversion of Ri-5-P to RuDP occurs exclusively or nearly exclusively in the chloroplasts indicating that phosphoribulokinase and/or ribosephosphate isomerase are located only there.4. The conversion of Ri-5-P to GAP and SuMP, which is catalyzed by the enzymes ribosephosphate isomerase, xylulosephosphate epimerase and transketolase, proceeds likewise only or at least predominantly in the chloroplasts and not, or only to a small extent, in the cytoplasm.5. The major parts of glucose-6-phosphate dehydrogenase and of 6-phosphogluconate dehydrogenase reside in the cytoplasm. However, a small, but significant, level of these enzymes is to be found also in the chloroplasts. Hexokinase and transaldolase are also present there. Pyruvate kinase and phosphofructokinase appear to be absent from chloroplasts.6. Since, with the presence of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, hexokinase, transaldolase and enzymes of the Calvin cycle, the enzymic machinery of the oxidative pentose phosphate pathway is complete in the chloroplasts, the results suggest that chloroplasts are engaged in the oxidative decomposition of carbohydrates.7. In the dark the oxidative pentose phosphate pathway requires the control of NADPH formation and the transfer of hydrogen across the chloroplast membrane.8. The available data on the intracellular localization of enzymes and on the kinetics of the distribution of labelled intermediates show that the photosynthetic carbon cycle operates exclusively within the chloroplasts. There is nothing to suggest that enzymes of chloroplasts and cytoplasm cooperate in the cyclic regeneration of the carbon acceptor molecule. However, the existence of phosphorylated transport metabolites suggests that secondary reactions of photosynthesis such as sucrose and amino acid synthesis, which proceed, at least in part, outside the chloroplasts, are directly linked with chloroplastic reactions by activated (phosphorylated) intermediates.

scholarly journals Changes in Metabolic Enzyme Activities during Thidiazuron-induced Lateral Budbreak of Apple

HortScience ◽  
1991 ◽  
Vol 26 (2) ◽  
pp. 171-173 ◽  
Author(s):  
Shiow Y. Wang ◽  
Hong J. Jiao ◽  
Miklos Faust
Keyword(s):  
Pyruvate Kinase ◽  
Isocitrate Dehydrogenase ◽  
Enzyme Activities ◽  
Tca Cycle ◽  
Tricarboxylic Acid ◽  
Pentose Phosphate ◽  
Rapid Expansion ◽  
Metabolic Enzyme ◽  
Cycle Enzyme ◽  
Glucose 6 Phosphate Dehydrogenase

The activity of glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphate gluconate dehydrogenase (6PGDH), isocitrate dehydrogenase (ICDH), pyruvate kinase (PK), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were studied in apple (Malus domestics Borkh.) buds during dormancy and thidiazuron-induced budbreak. When buds were dormant, the activity of the glycolytic enzymes GAPDH and PK and the tricarboxylic acid (TCA) cycle enzyme ICDH was low compared to that in nondormant buds. The activity of these enzymes increased during budbreak, peaked when buds were in the green tip stage just before the start of rapid expansion (at 8 days after thidiazuron treatment), and declined thereafter. The activity of pentose-phosphate cycle enzymes G6PDH and 6PGDH was higher in dormant buds than in nondormant buds. 6PGDH was about twice as high as G6PDH. During budbreak and resumption of growth, G6PDH and 6PGDH activity decreased.

Lipogenic Enzymes of Rat Liver and Adipose Tissue. Dietary Variations and Effect of Polychlorinated Biphenyls

1994 ◽  
Vol 49 (9-10) ◽  
pp. 665-678 ◽  
Author(s):  
Meinrad Boll ◽  
Lutz W. D. Weber ◽  
Andreas Stampfl ◽  
Burkhard Messner
Keyword(s):  
Adipose Tissue ◽  
Polychlorinated Biphenyls ◽  
Enzyme Activities ◽  
Time Course ◽  
Fatty Acid Synthase ◽  
Lipogenic Enzymes ◽  
Brown Adipose ◽  
Cleavage Enzyme ◽  
Order Of Magnitude ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract The lipogenic enzymes fatty acid synthase (FAS; EC 2.3.1.85), citrate cleavage enzyme (CCE; EC 4.1.3.8), malic enzyme (ME; EC 1.1.1.40), glucose-6-phosphate dehydrogenase (G6PDH; EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (PGDH; EC 1.1.1.44) were investigated in liver and in brown adipose tissue (BAT) of Wistar rats under various dietary conditions and in the presence of 15 to 250 ppm (approximately 0.045-0.75 μmol/kg chow) polychlorinated biphenyls (PCBs).In response to refeeding starved animals, enzyme activities in both tissues increased to above normal levels and thereafter exhibited pronounced oscillations of their activities. The extent of increase depended on the carbohydrate and fat content of the diet. The lipogenic enzymes could be grouped in two categories according to their sensitivity to dietary carbohydrate: FAS and CCE responded faster to smaller changes in dietary composition, while ME, G6PDH and PGDH required larger changes and more time to respond.Diet-induced alterations of enzyme activities were of the same order of magnitude in liver and BAT. They were age-dependent, being more pronounced in young animals. Independent of the type of dietary manipulations, activities changed in a coordinate fashion, i.e., the changes of the activities of all 5 enzymes occurred at similar ratios to each other with an identical time course.Feeding PCB-containing diets resulted in a considerable increase of the activities of the lipogenic enzymes in liver, which was significantly greater with ME, G 6PD H and PGDH. The effect was dose-dependent but transient. In liver the response to PCB feeding was iden­tical in male and female animals, whereas in BAT lipogenic activities increased in females, but decreased in males.Refeeding starved animals with a PCB-containing diet led to an additional stimulation of the normal refeeding-induced increase of the enzyme activities in liver and BAT. This PCB-induced increase was 2-fold for FAS and CCE, but up to 15-fold for the other enzymes. All PCB-induced effects were significantly less pronounced in old than in young animals.In primary hepatocytes activities increased in hormone-free medium in the presence of PCBs. While activity was induced in insuline-and triiodothyronine-containing medium, this increase was significantly greater with PCBs present.

Selective induction and suppression of liver enzyme synthesis

1962 ◽  
Vol 202 (1) ◽  
pp. 137-144 ◽  
Author(s):  
George Weber ◽  
Gouri Banerjee ◽  
Seymour B. Bronstein
Keyword(s):  
Enzyme Activities ◽  
Lactic Dehydrogenase ◽  
Enzyme Synthesis ◽  
Direct Oxidation ◽  
Phosphohexose Isomerase ◽  
Phosphogluconate Dehydrogenase ◽  
Acid Analogue ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Oxidation Of Glucose

Two techniques were used to demonstrate selective induction of enzyme increases in mammalian tissue in vivo: a) refeeding of fasted animals, and b) administration of cortisone to adrenalectomized animals. Refeeding acted selectively as an inducer for the stimulation of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activities, and as a less effective inducer of phosphoglucomutase, phosphohexose isomerase, glucose-6-phosphatase, and lactic dehydrogenase. On the other hand, cortisone acted selectively as an inducer for increases in glucose-6-phosphatase, fructose-1, 6-diphosphatase, phosphohexose isomerase and lactic dehydrogenase, and as a less effective inducer of 6-phosphogluconate dehydrogenase. Thus, refeeding primarily stimulated enzymes mediating the direct oxidation of glucose-6-phosphate, whereas cortisone stimulated enzymes involved in gluconeogenesis. The amino acid analogue ethionine selectively inhibited the induced increase of enzyme activities and methionine reversed the ethionine inhibition. The nature of the elevations in the enzyme activities and the mechanisms of ethionine inhibition were discussed.

scholarly journals Depletion of glycogen synthetase and increase of glucose 6-phosphate dehydrogenase in livers of ethionine-treated mice

1965 ◽  
Vol 97 (1) ◽  
pp. 32-36 ◽  
Author(s):  
HG Sie ◽  
A Hablanian
Keyword(s):  
Pyruvate Kinase ◽  
Glucose Dehydrogenase ◽  
Liver Glycogen ◽  
Synthetase Activity ◽  
Phosphogluconate Dehydrogenase ◽  
Glycogen Synthetase ◽  
Glucose 6 Phosphate Dehydrogenase

1. Ethionine-treated mice showed a marked depletion in liver glycogen, a decrease of glycogen-synthetase activity, an increase in activity of glucose 6-phosphate dehydrogenase and the solubilization of phosphorylase. 2. The administration of cortisol or glucose did not alleviate these changes but the effect of ethionine was completely prevented in animals given methionine as well as ethionine. 3. The activities of the following enzymes were unchanged: hexokinase, glucokinase, glucose 6-phosphatase, phosphoglucomutase, 6-phosphogluconate dehydrogenase, UDP-glucose pyrophosphorylase, UDP-glucose dehydrogenase and pyruvate kinase.

scholarly journals Degradation of glucose-metabolizing enzymes in the rat small intestine during starvation

1973 ◽  
Vol 132 (4) ◽  
pp. 657-661 ◽  
Author(s):  
Gwyneth M. Jones ◽  
R. J. Mayer
Keyword(s):  
Small Intestine ◽  
Lactate Dehydrogenase ◽  
Pyruvate Kinase ◽  
Phosphoglycerate Kinase ◽  
Rat Small Intestine ◽  
Metabolizing Enzymes ◽  
Phosphogluconate Dehydrogenase ◽  
Degradation Rates ◽  
Glucose 6 Phosphate Dehydrogenase

1. The degradation rates and half-lives of hexokinase, 6-phosphogluconate dehydrogenase, lactate dehydrogenase, pyruvate kinase, glucose 6-phosphate dehydrogenase, phosphoglycerate kinase and aldolase were calculated from measurements of the decline in activities of these enzymes in rat small intestine during starvation. 2. The half-lives of the enzymes are: hexokinase, 5.7h; 6-phosphogluconate dehydrogenase, 7.6h; glucose 6-phosphate dehydrogenase, 6.0h; pyruvate kinase, 8.9h; lactate dehydrogenase, 8.7h; phosphoglycerate kinase, 8.7h; aldolase, 5.1h. 3. The significance of the results is discussed with respect to the regulation of enzyme concentrations in response to changes in diet.

EFFECTS OF TESTOSTERONE PROPIONATE AND CYPROTERONE ACETATE ON CARBOHYDRATE METABOLISM IN RAT MAMMARY GLANDS

1980 ◽  
Vol 84 (3) ◽  
pp. 467-471
Author(s):  
N. DESHPANDE ◽  
IRENE MITCHELL
Keyword(s):  
Carbohydrate Metabolism ◽  
Cyproterone Acetate ◽  
Testosterone Propionate ◽  
Mammary Glands ◽  
Normal Mammary Gland ◽  
Inhibitory Effects ◽  
Phosphogluconate Dehydrogenase ◽  
Normal Rat ◽  
And Function ◽  
Glucose 6 Phosphate Dehydrogenase

The effects of administration of testosterone propionate on the activities of seven of the enzymes of carbohydrate metabolism in normal rat mammary glands were investigated and the validity of the results was confirmed by simultaneous injection of the hormone and cyproterone acetate. The administration of the androgen increased the activities of phosphofructokinase (PFK), glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH) and lactate dehydrogenase (LDH) in glands from both intact and from ovariectomized and adrenalectomized animals. Administration of cyproterone acetate alone resulted in a significant reduction in the activities of PFK and G6PDH and when given together with the androgen it inhibited increases in the activities of PFK, G6PDH, 6PGDH and LDH induced by testosterone. It was concluded that these results did not explain the known inhibitory effects of the androgen on normal mammary gland growth and function.

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