D-pinitol attenuates the impaired activities of hepatic key enzymes in carbohydrate metabolism of streptozotocin-induced diabetic rats

General Physiology and Biophysics

Volumn 28, Issue 3, 2009, Pages 233-241

  Sivakumar, Selvaraj ^a   Subramanian, Sorimuthu P ^a  

^a UNIVERSITY OF MADRAS   (India)

Author keywords

D pinitol; Diabetes mellitus; Insulin; Liver; Streptozotocin

Indexed keywords

CARBOHYDRATE; DEXTRO PINITOL; FRUCTOSE BISPHOSPHATASE; GLICLAZIDE; GLUCOSE; GLUCOSE 6 PHOSPHATASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLYCOGEN; GLYCOGEN PHOSPHORYLASE; GLYCOGEN SYNTHASE; GLYCOSYLATED HEMOGLOBIN; HEXOKINASE; INSULIN; LACTATE DEHYDROGENASE; LIVER ENZYME; NATURAL PRODUCT; PYRUVATE KINASE; STREPTOZOCIN; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CARBOHYDRATE METABOLISM; CONTROLLED STUDY; ENZYME ACTIVITY; GLUCONEOGENESIS; GLUCOSE BLOOD LEVEL; GLYCOGEN LIVER LEVEL; GLYCOGEN METABOLISM; HUMAN; HYPERGLYCEMIA; INSULIN BLOOD LEVEL; MALE; NONHUMAN; RAT; SOYBEAN; STREPTOZOCIN DIABETES;

ANIMALS; BODY WEIGHT; CARBOHYDRATE METABOLISM; DIABETES MELLITUS, EXPERIMENTAL; GLICLAZIDE; GLUCOSE TOLERANCE TEST; GLYCOGEN; GLYCOGEN PHOSPHORYLASE; GLYCOGEN SYNTHASE; HYPOGLYCEMIC AGENTS; INOSITOL; LIVER; MALE; RATS; RATS, WISTAR;

GLYCINE MAX; RATTUS;

EID: 72949093626     PISSN: 02315882     EISSN: None     Source Type: Journal    
DOI: 10.4149/gpb_2009_03_233     Document Type: Article

References (51)

1. Adisakwattana S., Roengsamran S., Hsu W. H., Yibchok-Anun S. (2005): Mechanisms of antihyperglycemic effect of p-methoxycinnamic acid in normal and streptozotocin-induced diabetic rats. Life Sci. 78, 406-412; doi:10.1016/j.lfs.2005.04.073 (Pubitemid 41597550)
2. Bailey C. J. (2000): Potential new treatments for type 2 diabetes. Trends Pharmacol. Sci. 21, 259-265; doi:10.1016/S0165-6147(00)01506-1516
3. Bates S. H., Jones R. B., Bailey C. J. (2000): Insulin-like effect of pinitol. Br. J. Pharmacol. 130, 1944-1948; doi:10.1038/sj.bjp.0703523
4. Brandstrup N., Kirk J. E., Bruni C. (1957): The hexokinase and phosphoglucoisomerase activities of aortic and pulmonary artery tissue in individuals of various ages. J. Gerontol. 12, 166-171
5. Chen R., Meseck M., McEvoy R. C., Woo S. L. (2000): Glucose-stimulated and self-limiting insulin production by glucose 6-phosphatase promoter driven insulin expression in hepatoma cells. Gene Ther. 7, 1802-1809; doi:10.1038/sj.gt.3301306
6. Cornblath M., Randle P. J., Parmeggiani A., Morgan H. E. (1963): Regulation of glycogenosis in muscle. Effects of glucagon and anoxia on lactate production, glycogen content, and Phosphorylase activity in the perfused isolated rat heart. J. Biol. Chem. 238, 1592-1597
7. Drabkin D. L., Austin H. J. (1932): Spectrophotometric studies. I. Spectrophotometric constants for common hemoglobin derivatives in human, dog and rabbit blood. J. Biol. Chem. 98, 719-733
8. Ells H. A., Kirkman H. N. (1961): A colorimetric method for assay of erythrocytic glucose-6-phosphate dehydrogenase. Proc. Soc. Exp. Biol. Med. 106, 607-609
9. Ferrannini E., Lanfranchi A., Rohner-Jeanrenaud F., Manfredini G., Van de Werve G. (1990): Influence of long-term diabetes on liver glycogen metabolism in the rat. Metabolism 39, 1082-1088; doi:10.1016/0026-0495(90)90170-H (Pubitemid 20351268)
10. Fonseca V. (2003): Clinical significance of targeting postprandial and fasting hyperglycemia in managing type 2 diabetes mellitus. Curr. Med. Res. Opin. 19, 635-641 ; doi:10.1185/030079903125002351
11. Gancedo J. M., Gancedo C. (1971): Fructose-1,6-diphosphatase, phosphofructokinase and glucose-6-phosphate dehydrogenase from fermenting and non fermenting yeasts. Arch. Mikrobiol. 76, 132-138; doi:10.1007/BF00411787
12. Gupta D., Raju J., Prakash J., Baquer N. Z. (1999): Change in the lipid profile, lipogenic and related enzymes in the livers of experimental diabetic rats: effect of insulin and vanadate. Diabetes Res. Clin. Pract. 46, 1-7; doi:10.1016/S0168-8227(99)00067-74
13. Haller M. J., Stalvey M. S., Silverstein J. H. (2004): Predictors of control of diabetes: monitoring may be the key. J. Pediatr. 144, 660-661; doi:10.1016/j.jpeds.2003.12.042
14. Huizinga M. M., Rothman R. L. (2006): Addressing the diabetes pandemic: a comprehensive approach. Indian J. Med. Res. 124, 481-484
15. Joy K. L., Kuttan R. (1999): Anti-diabetic activity of Picrorrhiza kurroa extract. J. Ethnopharmacol. 67, 143-148; doi:10.1016/S0378-8741(98)00243-248
16. Kim J. L., Kim J. C., Kang M. J., Lee M. S., Kim J. J., Cha I. J. (2005): Effects of pinitol isolated from soybeans on glycaemic control and cardiovascular risk factors in Korean patients with type II diabetes mellitus: a randomized controlled study. Eur. J. Clin. Nutr. 59, 456-458; doi:10.1038/sj.ejcn.I602081
17. King J. (1959): A routine method for the estimation of lactic dehydrogenase activity. J. Med. Lab. Technol. 16, 265-272
18. Koide H., Oda T. (1959): Pathological occurrence of glucose-6-phosphatase in serum in liver diseases. Clin. Chim. Acta 4, 554-561; doi:10.1016/0009- 8981(59)90165-2
19. Kumar P. A., Haseeb A., Suryanarayana P., Ehtesham N. Z., Reddy G. B. (2005): Elevated expression of alphaA- and alphaB-crystallins in streptozotocin-induced diabetic rat. Arch. Biochem. Biophys. 444, 77-83; doi:10.1016/j.abb.2005.09.021
20. Kuo T. M., Lowell C. A., Nelsen T. C. (1997): Occurrence of pinitol in developing soybean seed tissues. Phytochemistry 45, 29-35; doi:10.1016/S0031 -9422(96)00795-799
21. Laakso M., Malkki M., Deeb S. S. (1995): Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes 44, 330-334; doi:10.2337/diabetes.44.3.330
22. Lee J. S., Lee C. M., Jeong Y. L, Jung I. D., Kim B. H., Seong E. Y, Kim J. I., Choi I. W., Chung H. Y., Park Y. M. (2007): D-pinitol regulates Thl/Th2 balance via suppressing Th2 immune response in ovalbumin-induced asthma. FEBS Lett. 581, 57-64; doi:10.1016/j.febslet.2006.11.077
23. Leloir L. E., Goldemberg S. H. (1962): Glycogen synthetase from rat liver. In: Methods in Enzymology. (Eds. S. P. Colowick and N. O. Kaplan), pp. 145-147, New York Academic Press; doi:10.1016/S0076-6879(62)05196-4
24. Lemieux G., Aranda M. R., Fournel P., Lemieux C. (1984): Renal enzymes during experimental diabetes mellitus in the rat. Role of insulin, carbohydrate metabolism, and ketoacidosis. Can. J. Physiol. Pharmacol. 62, 70-75
25. Massillon D., Barzilai N., Chen W, Hu M., Rossetti L. (1996): Glucose regulates in vivo gIucose-6-phosphatase gene expression in the liver of diabetic rats. J. Biol. Chem. 271, 9871-9874; doi:10.1074/jbc.271.17.9871
26. Morales M. A., Jabbagy A. J., Terenizi H. R. (1973): Mutations affecting accumulation of Neurospora glycogen. News Lett. 20, 24-25
27. Narayanan C. R., Joshi D. D., Mujumdar A. M., Dhekne V. V. (1987): Pinitol a new anti-diabetic compound from the leaves of Bougainvillea spectabilis. Curr. Sci. 56, 139-141
28. Nayak S. S., Pattabiraman T. N. (1981): A new colorimetric method for the estimation of glycosylated hemoglobin. Clin. Chim. Acta 109, 267-274; doi:10.1016/0009-8981(81)90312-90320
29. Nordlie R. C, Foster J. D., Lange A. J. ( 1999): Regulation of glucose production by the liver. Annu. Rev. Nutr. 19, 379-406; doi:10.1146/annurev.nutr. l9.1.379
30. O'Doherty R. M., Lehman D. L., Télémaque-Potts S., Newgard C. B. (1999): Metabolic impact of glucokinase overexpression in liver: lowering of blood glucose in fed rats is accompanied by hyperlipidemia. Diabetes 48, 2022-2027; doi:10.2337/diabetes.48.10.2022
31. Pepato M. T., Migliorini R. H., Goldberg A. L., Kettelhut I. C. (1996): Role of different proteolytic pathways in degradation of muscle protein from streptozotocin-diabetic rats. Am. J. Physiol. 271, E340-347
32. Phillips D. V., Dougherty D. E., Smith A. E. (1982): Cyclitols in soybean. J. Agric. Food Chem. 30, 456-458; doi:10.1021/jf00111a011
33. Pilkis S. J., Claus T. H. (1991): Hepatic gluconeogenesis/glycolysis: regulation and structure/function relationships of substrate cycle enzymes. Annu. Rev. Nutr. 11, 465-515; doi:10.1146/annurev.nu.l 1.070191.002341
34. Pogson C. L., Denton R. M. (1967): Effect of alloxan diabetes, starvation and refeeding on glycolytic kinase activities in rat epididymal adipose tissue. Nature 216, 156-157; doi:10.1038/216156a0
35. Pulido N., Suarez A., Casanova B., Romero R., Rodriguez E., Rovira A. (1997): Gliclazide treatment of streptozotocin diabetic rats restores GLUT4 protein content and basal glucose uptake in skeletal muscle. Metabolism 46, 10-13; doi:10.1016/S0026-0495(97)90310-3 (Pubitemid 127675843)
36. Rakieten N., Rakieten M. L., Nadkarni M. R. (1963): Studies on the diabetogenic action of streptozotocin (NSC-37917). Cancer Chemother. Rep. 29, 91-98
37. Roden M., Bernroider E. (2003): Hepatic glucose metabolism in humans-its role in health and disease. Best Pract. Res. Clin. Endocrinol. Metab. 17, 365-383; doi:10.1016/S1521-690X(03)00031-39
38. Roesler W. J., Khandelwal R. L. (1986): Quantitation of glycogen synthase and Phosphorylase protein in mouse liver: correlation between enzymatic protein and enzyme activity. Arch. Biochem. Biophys. 244, 397-407; doi:10.1016/0003- 9861(86)90130-X
39. Sasaki T., Matsy S., Sonae A. (1972): Effect of acetic acid concentration on the colour reaction in the O-toluidine boric acid method for blood glucose estimation. Rinsh. Kagaku 1, 346-353 (in Japanese)
40. Schein P. S., Cooney D. A., McMenamin M. G., Anderson T. (1973): Streptozotocin diabetes-further studies on the mechanism of depression of nicotinamide adenine dinucleotide concentrations in mouse pancreatic islets and liver. Biochem. Pharmacol. 22, 2625-2631 ; doi:10.1016/0006-2952(73)90071-3 S 4357891,4356190
41. Sen S., Kar M., Roy A., Chakraborti A. S. (2005): Effect of nonenzymatic glycation on functional and structural properties of hemoglobin. Biophys. Chem. 113, 289-298; doi:10.1016/j.bpc.2004.05.005
42. Singh R. K., Pandey B. L., Tripathi M., Pandey V. B. (2001): Anti-in-flammatory effect of (+)-pinitol. Fitoterapia 72, 168-170; doi:10.1016/S0367-326X(00)00267-7
43. Szkudelski T. (2001): The mechanism of alloxan and streptozotocin action in B cells of the rat pancreas. Physiol. Res. 50, 537-546
44. Taylor R., Agius L. (1988): The biochemistry of diabetes. Biochem. J. 250, 625-640
45. Wang H., Chu W., Das S. K., Ren Q., Hasstedt S. J., Elbein S. C. (2002): Liver pyruvate kinase polymorphisms are associated with type 2 diabetes in northern European Caucasians. Diabetes 51, 2861-2865; doi:10.2337/diabetes.51.9. 2861
46. West I. C. (2002): Glucose-6-phosphate dehydrogenase: a candidate gene for diabetes. Diabet. Med. 19, 172-174; doi:10.1046/j.1464-5491.2002.690-1.x
47. Whitton P. D., Hems D. A. (1975): Glycogen synthesis in the perfused liver of streptozotocin-diabetic rats. Biochem. J. 150, 153-165
48. Wild S., Roglic G., Green A., Sicree R., King H. (2004): Global prevalence of diabetes: estimates for the year 2000 and projections for 2030. Diabetes Care 27, 1047-1053; doi:10.2337/diacare.27.5.1047
49. Williamson D. H., Lund P., Krebs H. A. (1967): The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem. J. 103, 514-527
50. Xu Y., Osborne B. W., Stanton R. C. (2005): Diabetes causes inhibition of glucose-6-phosphate dehydrogenase via activation of PKA, which contributes to oxidative stress in rat kidney cortex. Am. J. Physiol. 289, F1040-1047
51. Yamamoto H., Uchigata Y., Okamoto H. (1981): Streptozotocin and alloxan induce DNA strand breaks and poly (ADP-ribose) synthetase in pancreatic islets. Nature 294, 284-286; doi:10.1038/294284a0