Effect of biotin treatment on hepatic gene expression in streptozotocin-induced diabetic rats

Bioscience, Biotechnology and Biochemistry

Volumn 72, Issue 5, 2008, Pages 1290-1298

  Sugita, Yumi ^a   Shirakawa, Hitoshi ^a   Sugimoto, Ritsuko ^b   Furukawa, Yuji ^a   Komai, Michio ^a  

^a TOHOKU UNIVERSITY   (Japan)

^b Morioka Junior College   (Japan)

Author keywords

Biotin; Gene expression; Gluconeogenesis; Streptozotocin (STZ) diabetic rat

Indexed keywords

ALCOHOLS; BIOACTIVITY; BIOCHEMISTRY; COENZYMES; FUNCTIONS; GENE EXPRESSION; GLUCOSE; HORMONES; INSULIN; MAMMALS; METABOLISM; MICROFLUIDICS; MODULATION; PROTEINS; RATS; SUGAR (SUCROSE); TRANSCRIPTION FACTORS;

(I ,J) CONDITIONS; (MIN ,MAX ,+) FUNCTIONS; CELLULAR PROCESSES; DIABETIC RATS; ENERGY METABOLISM; GLUCOKINASE (GCK); GLUCONEOGENIC; GLUCONEOGENIC GENES; GLUCOSE-6-PHOSPHATASE (G6PASE); HEPATOCYTE NUCLEAR FACTOR (HNF); INSULIN TREATMENT; MRNA EXPRESSION; MRNA LEVELS; NOVEL FUNCTIONS; PHOSPHOENOLPYRUVATE CARBOXYKINASE (PEPCK); PROTEIN LEVELS; STEROL REGULATORY ELEMENT-BINDING PROTEIN (SREBP); STREPTOZOTOCIN (STZ);

TRANSCRIPTION;

BIOTIN; CARBOXYLYASE; GLUCOKINASE; GLUCOSE 6 PHOSPHATASE; INSULIN; LIPID; MESSENGER RNA; STREPTOZOCIN; TRANSCRIPTION FACTOR;

ANIMAL; ARTICLE; BLOOD; CARBOHYDRATE METABOLISM; CHEMICALLY INDUCED DISORDER; DRUG EFFECT; EXPERIMENTAL DIABETES MELLITUS; GENE EXPRESSION REGULATION; GENETICS; GLUCONEOGENESIS; GLUCOSE BLOOD LEVEL; GLYCOLYSIS; LIPID METABOLISM; LIVER; MALE; METABOLISM; RAT; SPRAGUE DAWLEY RAT;

ANIMALS; BIOTIN; BLOOD GLUCOSE; CARBOHYDRATE METABOLISM; CARBOXY-LYASES; DIABETES MELLITUS, EXPERIMENTAL; GENE EXPRESSION REGULATION; GLUCOKINASE; GLUCONEOGENESIS; GLUCOSE-6-PHOSPHATASE; GLYCOLYSIS; INSULIN; LIPID METABOLISM; LIPIDS; LIVER; MALE; RATS; RATS, SPRAGUE-DAWLEY; RNA, MESSENGER; STREPTOZOCIN; TRANSCRIPTION FACTORS;

MAMMALIA; RATTUS;

EID: 45749140376     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70781     Document Type: Article

References (31)

1. Moss, J., and Lane, M. D., The biotin-dependent enzymes. Adv. Enzymol., 35, 321-398 (1971).
2. Zempleni, J., and Mock, D. M., Biotin biochemistry and human requirements. J. Nutr. Biochem., 10, 128-138 (1999).
3. Wood, H. G., and Barden, R. E., Biotin enzymes. Annu. Rev. Biochem., 46, 385-413 (1977).
4. Wiedmann, S., Eudy, J. D., and Zempleni, J., Biotin supplementation increases expression of genes encoding interferon-γ, interleukin-1β, and 3-methylcrotonyl-CoA carboxylase, and decreases expression of the gene encoding interleukin-4 in human peripheral blood mononuclear cells. J. Nutr., 133, 716-719 (2003).
5. Báez-Saldaña, A., D́az, G., Espinoza, B., and Ortega, E., Biotin deficiency induces changes in subpopulations of spleen lymphocytes in mice. Am. J. Clin. Nutr., 67, 431-437 (1998).
6. Rodriguez-Melendez, R., Camporeale, G., Griffin, J. B., and Zempleni, J., Interleukin-2 receptor γ-dependent endocytosis depends on biotin in Jurkat cells. Am. J. Physiol. Cell Physiol., 284, C415-421 (2003).
7. Bhullar, R. P., and Dakshinamurti, K., The effect of biotin on cellular functions in HeLa cells. J. Cell. Physiol., 123, 425-430 (1985).
8. Dakshinamurti, K., and Cheah-Tan, C., Liver glucokinase of the biotin deficient rat. Can. J. Biochem., 46, 75-80 (1968).
9. Spence, J. T., and Kopudelka, A. P., Effects of biotin upon the intracellular level of cGMP and the activity of glucokinase in cultured rat hepatocytes. J. Biol. Chem., 259, 6393-6396 (1984).
10. Chauhan, J., and Dakshinamurti, K., Transcriptional regulation of the glucokinase gene by biotin in starved rats. J. Biol. Chem., 266, 10035-10038 (1991).
11. Borboni, P., Magnaterra, R., Rabini, R. A., Staffolani, R., Porzio, O., Sesti, G., Fusco, A., Mazzanti, L., Lauro, R., and Marlier, L. N., Effect of biotin on glucokinase activity, mRNA expression and insulin release in cultured beta-cells. Acta Diabetol., 33, 154-158 (1996).
12. Dakshinamurti, K., and Li, W., Transcriptional regulation of liver phosphoenolpyruvate carboxykinase by biotin in diabetic rats. Mol. Cell. Biochem., 132, 127-132 (1994).
13. Narang, M. A., Dumas, R., Ayer, L. M., and Gravel, R. A., Reduced histone biotinylation in multiple carboxylase deficiency patients: a nuclear role for holocarboxylase synthetase. Hum. Mol. Genet., 13, 15-23 (2004).
14. Chew, Y. C., Camporeale, G., Kothapalli, N., Sarath, G., and Zempleni, J., Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase. J. Nutr. Biochem., 17, 225-233 (2006).
15. Zhang, H., Osada, K., Sone, H., and Furukawa, Y., Biotin administration improves the impaired glucose tolerance of streptozotocin-induced diabetic Wistar rats. J. Nutr. Sci. Vitaminol., 43, 271-280 (1997).
16. Shirakawa, H., Ohsaki, Y., Minegishi, Y., Takumi, N., Ohinata, K., Furukawa, Y., Mizutani, T., and Komai, M., Vitamin K deficiency reduces testosterone production in the testis through down-regulation of the Cyp11a a cholesterol side chain cleavage enzyme in rats. Biochim. Biophys. Acta, 1760, 1782-1788 (2006).
17. Wang, X. L., Herzog, B., Waltner-Law, M., Hall, R. K., Shiota, M., and Granner, D. K., The synergistic effect of dexamethasone and all-trans-retinoic acid on hepatic phosphoenolpyruvate carboxykinase gene expression involves the coactivator p300. J. Biol. Chem., 279, 34191-34200 (2004).
18. Kahn, C. R., Lauris, V., Koch, S., Crettaz, M., and Granner, D. K., Acute and chronic regulation of phosphoenolpyruvate carboxykinase mRNA by insulin and glucose. Mol. Endocrinol., 3, 840-845 (1989).
19. Meyer, S., Hoppner, W., and Seitz, H. J., Transcriptional and post-transcriptional effects of glucose on liver phosphoenolpyruvate- carboxykinase gene expression. Eur. J. Biochem., 202, 985-991 (1991).
20. Beale, E. G., Forest, C., and Hammer, R. E., Regulation of cytosolic phosphoenolpyruvate carboxykinase gene expression in adipocytes. Biochimie, 85, 1207-1211 (2003).
21. Yoon, J. C., Puigderver, P., Chen, G., Donovan, J., Wu, Z., Rhee, J., Adelmant, G., Stafford, J., Lahn, C. R., Granner, D. K., Newgard, C. B., and Spiegelman, B. M., Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1. Nature, 413, 131-138 (2001).
22. Herzing, S., Long, F., Jhala, U. S., Hedrick, S., Quinn, R., Bauer, A., Rudolph, D., Schuts, G., Yoon, C., Puigserver, P., Spiegelman, B., and Montminy, M., CREB regulates hepatic gluconeogenesis through the coactivator PGC-1. Nature, 413, 179-183 (2001).
23. Puigderver, P., Rhee, J., Donovan, J., Walkey, C. J., Yoon, J. C., Oriente, F., Kitamura, Y., Altomomte, J., Dong, H., Accili, D., and Spiegelman, B. M., Insulin-regulated hepatic gluconeogenesis through FOXO1-PGC-1 interaction. Nature, 423, 550-555 (2003).
24. Scott, D. K., O'Doherty, R. M., Stafford, J. M., Newgard, C. B., and Granner, D. K., The repression of hormone-activated PEPCK gene expression by glucose is insulin-independent but requires glucose metabolism. J. Biol. Chem., 273, 24145-24151 (1998).
25. Solórzano-Vargas, R. S., Pacheco-Alvarez, D., and León-Del-Río, A., Holocarboxylase synthetase is an obligate participant in biotin-mediated regulation of its own expression and of biotin-dependent carboxylases mRNA levels in human cells. Proc. Natl. Acad. Sci. USA, 99, 5325-5330 (2002).
26. Pacheco-Alvarez, D., Solórzano-Vargas, R. S., Gravel, R. A., Cervantes-Roldán, R., Velázquez, A., and León-Del- Río, A., Paradoxical regulation of biotin utilization in brain and liver and implications for inherited multiple carboxylase deficiency. J. Biol. Chem., 279, 52312-52318 (2004).
27. Rodríguez-Meléndez, R., Cano, S., Méndez, S. T., and Velázquez, A., Biotin regulates the genetic expression of holocarboxylase synthetase and mitochondrial carboxylases in rats. J. Nutr., 131, 1909-1913 (2001).
28. Rodríguez-Meléndez, R., Pérez-Andrade, M. E., Díaz, A., Deolarte, A., Camacho-Arroyo, I., Cicerón, I., Ibarra, I., and Velázquez, A., Differential effects of biotin deficiency and replenishment on rat liver pyruvate and propionyl-CoA carboxylases and on their mRNAs. Mol. Genet. Metab., 66, 16-23 (1999).
29. Manthey, K. C., Griffin, J. B., and Zempleni, J., Biotin supply affects expression of biotin transporters, biotinylation of carboxylases and metabolism of interleukin-2 in Jurkat cells. J. Nutr., 132, 887-892 (2002).
30. Vlasova, T. I., Stratton, S. L., Wells, A. M., Mock, N. I., and Mock, D. M., Biotin deficiency reduces expression of SLC19A3, a potential biotin transporter, in leukocytes from human blood. J. Nutr., 135, 42-47 (2005).
31. Pirner, H. M., and Stolz, J., Biotin sensing in Saccharomyces cerevisiae is mediated by a conserved DNA element and requires the activity of biotin-protein ligase. J. Biol. Chem., 281, 12381-12389 (2006).