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1.
Indian J Biochem Biophys ; 2007 Dec; 44(6): 477-80
Article in English | IMSEAR | ID: sea-26549

ABSTRACT

The modulation of glucose-metabolizing enzymes activities play a vital role in the depletion of energy metabolism and leads to inhibition of cancer growth. In the present study, the effect of Gynandropsis gynandra L. extract on aflatoxin B1 (AFB1)-induced hepatocellular carcinoma (HCC) was studied on glucose-metabolizing enzymes in rats. A significant increase (p < 0.001) in the activities of the key glycolytic enzymes viz., hexokinase and phosphoglucoisomerase, with a significant decrease (p < 0.001) in the gluconeogenic enzymes glucose-6-phosphatase and fructose-1,6-bisphosphatase were observed in HCC-bearing rats, when compared with the control. Administration of G. gynandra extract caused a significant decrease in the activities of glycolytic enzymes and an increase in the gluconeogenic enzymes activities to near normal values. Thus, findings suggest the G. gynandra extract has a definite modulating role on the key enzymes of glucose metabolism in HCC. The modulatory effect may be due to the phytoactive constituents present in the extract of G. gynandra.


Subject(s)
Aflatoxin B1/toxicity , Animals , Carcinoma, Hepatocellular/chemically induced , Fructose-Bisphosphatase/metabolism , Gluconeogenesis , Glucose/metabolism , Glucose-6-Phosphatase/metabolism , Glucose-6-Phosphate Isomerase/metabolism , Glycolysis , Hexokinase/metabolism , Liver Neoplasms/chemically induced , Male , Plant Extracts/toxicity , Rats , Rats, Wistar
2.
Indian J Exp Biol ; 2001 Sep; 39(9): 925-8
Article in English | IMSEAR | ID: sea-62488

ABSTRACT

Aavirai Kudineer (AK) is an herbal decoction of seven botanical drugs, cited in the Gunapadam; a Tamil Siddha medical text. The anti-diabetic efficacy of this formulation was evaluated using alloxan-induced diabetic and normal rats. Glucose tolerance was observed within 1 hr in AK-treated rats (10 ml/kg body ) as compared to control. A significant decrease in the severe hyperglycemia characteristic of alloxan diabetes was noted after 15 days of AK treatment. Further AK treatment reversed the elevated urea, creatinine, cholesterol and decreased protein values to near normal levels. Assay of glycogen content and chief carbohydrate-metabolizing enzymes, viz. hexokinase, glucose-6-phosphatase and fructose 1,6 diphosphatase in the liver of diabetic and AK-treated diabetic rats clearly ascertains the hypoglycemic efficacy of this formulation. The mode of action of this herbal formulation remains to be elucidated.


Subject(s)
Animals , Blood Glucose/metabolism , Cholesterol/blood , Creatinine/blood , Diabetes Mellitus, Experimental/blood , Fructose-Bisphosphatase/metabolism , Glucose-6-Phosphatase/metabolism , Glycogen/metabolism , Hexokinase/metabolism , Hypoglycemic Agents/therapeutic use , Male , Phytotherapy , Plant Preparations/therapeutic use , Plants, Medicinal , Rats , Rats, Wistar , Urea/blood
3.
Braz. j. med. biol. res ; 34(8): 1055-1064, Aug. 2001. ilus, tab
Article in English | LILACS | ID: lil-290143

ABSTRACT

The effects of short-term burst (5 min at 1.8 m/s) swimming and long-term cruiser (60 min at 1.2 m/s) swimming on maximal enzyme activities and enzyme distribution between free and bound states were assessed for nine glycolytic and associated enzymes in tissues of horse mackerel, Trachurus mediterraneus ponticus. The effects of exercise were greatest in white muscle. The activities of phosphofructokinase (PFK), pyruvate kinase (PK), fructose-1,6-bisphosphatase (FBPase), and phosphoglucomutase (PGM) all decreased to 47, 37, 37 and 67 percent, respectively, during 60-min exercise and all enzymes except phosphoglucoisomerase (PGI) and PGM showed a change in the extent of binding to subcellular particulate fractions during exercise. In red muscle, exercise affected the activities of PGI, FBPase, PFK, and lactate dehydrogenase (LDH) and altered percent binding of only PK and LDH. In liver, exercise increased the PK activity 2.3-fold and reduced PGI 1.7-fold only after 5 min of exercise but altered the percent binding of seven enzymes. Fewer effects were seen in brain, with changes in the activities of aldolase and PGM and in percent binding of hexokinase, PFK and PK. Changes in enzyme activities and in binding interactions with subcellular particulate matter appear to support the altered demands of tissue energy metabolism during exercise


Subject(s)
Animals , Enzymes/metabolism , Fishes/physiology , Glycolysis/physiology , Muscle, Skeletal/enzymology , Physical Exertion/physiology , Brain/enzymology , Enzymes/analysis , Fructose-Bisphosphatase/metabolism , Liver/enzymology , Phosphofructokinase-1/metabolism , Phosphoglucomutase/metabolism , Swimming
4.
Indian J Exp Biol ; 1999 Feb; 37(2): 196-9
Article in English | IMSEAR | ID: sea-56616

ABSTRACT

The effects of insulin, sodium orthovanadate and a hypoglycemic plant material, Trigonella foenum graecum (fenugreek) seed powder were studied on the activities of glucose-6-phosphatase and fructose-1,6-bisphosphatase in diabetic liver and kidney. The significantly increased activities of the two enzymes during diabetes in liver and kidney were found to be lowered to almost control values by the use of the antidiabetic compounds. Diabetic liver exhibited a much greater increase in the activities of the two enzymes than diabetic kidney. The highest percentage of reversal to normal values was seen using the combination of vanadate and Trigonella seed powder. The lowered rate of growth of the animals as well as the increased blood sugar were reversed almost to the control levels by the Trigonella seed powder and vanadate treatment. The inclusion of the Trigonella seed powder overcame the toxicity of vanadium encountered when it was given alone as insulin mimetic agent. Much lower levels of vanadate were needed when it was given in combination with Trigonella seed powder. Their combined effects were better at restoring the above parameters than those induced by insulin administration.


Subject(s)
Animals , Diabetes Mellitus, Experimental/drug therapy , Female , Fructose-Bisphosphatase/metabolism , Gluconeogenesis/drug effects , Glucose-6-Phosphatase/metabolism , Hypoglycemic Agents/pharmacology , Insulin/pharmacology , Kidney/enzymology , Liver/enzymology , Plant Extracts/pharmacology , Plants, Medicinal , Rats , Rats, Wistar , Trigonella , Vanadates/pharmacology
5.
Indian J Biochem Biophys ; 1993 Oct; 30(5): 270-6
Article in English | IMSEAR | ID: sea-28243

ABSTRACT

Rate of net CO2 exchange and activities of the key enzymes of fru-2,6-P2, sucrose and starch synthesis and levels of certain intermediates of Calvin cycle were determined in Brassica pods at different stages of their development. The rate of net CO2 exchange, activities of FBPase, UDPG-pyrophosphorylase and SPS, and the contents of 3-PGA, DHAP, RuBP and UDPG increased up to day 21 after anthesis followed by a continuous decrease thereafter. However the content of fru-6-P started decreasing only after 28 days of anthesis. Changes in the levels of fru-2,6-P2 were closely associated with the changes in F6P 2-kinase activity rather than with F2,6-P2ase activity. Similarly, activities of ADPG-pyrophosphorylase and ADPG-starch synthetase closely followed the pattern of starch accumulation in pod tissues. These observations suggest that during the early phase of pod development (up to 21 days after anthesis), which is also the active phase for pod photosynthesis, carbon is mainly utilised for sucrose synthesis and that during the later phase of pod development (from day 21 to 42 after anthesis), there is shift in metabolic path of carbon from sucrose to starch.


Subject(s)
Brassica/enzymology , Carbon Dioxide/metabolism , Fructose-Bisphosphatase/metabolism , Oxidation-Reduction , Photosynthesis , Starch/biosynthesis , Sucrose/biosynthesis , Time Factors , UTP-Glucose-1-Phosphate Uridylyltransferase/metabolism
6.
Acta cient. venez ; 41(5/6): 311-6, 1990. ilus
Article in Spanish | LILACS | ID: lil-105366

ABSTRACT

As compared to the liver, intestinal mucosa shows a high rate of aerobic glycolysis. This difference has been attributed to the higher activity of the intestinal phosphofructokinase (PFK) isoenzyme. The regulatory properties of rat small intestine and liver PFK were investigated. At pH 8, where PFK activity can be evaluated free of allosteric influences, the specific activity of the liver isoenzyme was 25%higher that of the intestinal one, At pH 7, the mucosal PFK was activated to 80%of its maximal activity at pH 8, while the liver enzyme showed only a 40%activation. The apparent Kms for Fructose-6-P were 0.47 and 1.03 mM for the mucosal and hepatic isoenzymes, respectively. At 2 mM Fructose-6-P, the optimal ATP concentration for both isoenzymes was 1 mM Hogher ATP concentrations strongly anhibited both enzymes, but below 3 mM, PFK activity was larger in the mucosal homogenate. In addition, the intestinal PFK was more sensitive to activation by Fructose-2,6-bisphosphate and 6-phosphogluconate, particulary at low Fructose-6-p concentrations, and by AMP below 0.3 mM. These studies suggest that, under physiological conditions, the intestinal isoenzyme is more active than its liver counterpart. This may acccunt for the high rate of aerobic glycolysis observed in the intestinal mucosa


Subject(s)
Rats , Animals , Male , Fructose-Bisphosphatase/metabolism , Intestinal Mucosa/metabolism , Liver/metabolism , Phosphofructokinase-1/metabolism , Fructosediphosphates/metabolism , Glycolysis , Hexosediphosphates/metabolism , Lactates/metabolism , Rats, Inbred Strains
10.
Indian J Physiol Pharmacol ; 1984 Jul-Sep; 28(3): 195-200
Article in English | IMSEAR | ID: sea-107255

ABSTRACT

Neutral fructose 1, 6 bisphosphatase activity increases till 7 days, after which, a decline is observed postnatally upto 30 days. Alkaline fructose 1, 6 bisphosphatase follows the same pattern. The optimum activity of fructose 1, 6 bisphosphatase in mouse liver at pH 6.5 and 9.0 of all the periods, suggests the presence of both neutral and alkaline enzyme during the developmental period studied. On the basis of similarity observed in optimum pH, the same properties of enzyme at all the developmental stages studied, could not be ruled out.


Subject(s)
Aging , Animals , Body Weight , Fructose-Bisphosphatase/metabolism , Liver/enzymology , Mice , Organ Size , Proteins/metabolism
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