메뉴 건너뛰기




Volumn 36, Issue 3, 2011, Pages 325-337

Effects of spaced feeding on gene expression of hepatic transaminase and gluconeogenic enzymes in rats

Author keywords

Alanine aminotransferase; Aspartate aminotransferase; Gluconeogenesis; Liver; Rats

Indexed keywords

ACYL COENZYME A DEHYDROGENASE; ALANINE AMINOTRANSFERASE; AMINOTRANSFERASE; ASPARTATE AMINOTRANSFERASE; BETA ACTIN; CARNITINE PALMITOYLTRANSFERASE; FRUCTOSE 1,6 BISPHOSPHATE; GLUCOSE; GLUCOSE 6 PHOSPHATASE; MESSENGER RNA; PYRUVATE KINASE;

EID: 79958074212     PISSN: 03881350     EISSN: 18803989     Source Type: Journal    
DOI: 10.2131/jts.36.325     Document Type: Article
Times cited : (18)

References (34)
  • 2
    • 0025128458 scopus 로고
    • Fenofibrate. A review of its pharmacodynamic and pharmacokinetic properties and therapeutic use in dyslipidaemia
    • Balfour, J.A., McTavish, D. and Heel, R.C. (1990): Fenofibrate. A review of its pharmacodynamic and pharmacokinetic properties and therapeutic use in dyslipidaemia. Drugs, 40, 260-290.
    • (1990) Drugs , vol.40 , pp. 260-290
    • Balfour, J.A.1    McTavish, D.2    Heel, R.C.3
  • 3
    • 0023623394 scopus 로고
    • Comparative toxicity and safety profile of fenofibrate and other fibric acid derivatives
    • Blane, G.F. (1987): Comparative toxicity and safety profile of fenofibrate and other fibric acid derivatives. Am. J. Med., 83, 26-36.
    • (1987) Am. J. Med , vol.83 , pp. 26-36
    • Blane, G.F.1
  • 5
    • 0027465715 scopus 로고
    • Effects of moderate dietary restriction and age on blood parameters and metabolic enzymes in Lobund-Wistar rats
    • Chen, L.H., Huang, T.L. and Synder, D.L. (1993): Effects of moderate dietary restriction and age on blood parameters and metabolic enzymes in Lobund-Wistar rats. Arch. Gerontol. Geriatr., 16, 69-80.
    • (1993) Arch. Gerontol. Geriatr , vol.16 , pp. 69-80
    • Chen, L.H.1    Huang, T.L.2    Synder, D.L.3
  • 6
    • 0016686118 scopus 로고
    • Metabolic implications of the distribution of the alanine aminotransferase isoenzymes
    • DeRosa, G. and Swick, R.W. (1975): Metabolic implications of the distribution of the alanine aminotransferase isoenzymes. J. Biol. Chem., 250, 7961-7967.
    • (1975) J. Biol. Chem , vol.250 , pp. 7961-7967
    • Derosa, G.1    Swick, R.W.2
  • 7
    • 0032877056 scopus 로고    scopus 로고
    • Calories and aging alter gene expression for gluconeogenic, glycolytic, and nitrogen-metabolizing enzymes
    • Dhahbi, J.M., Mote, P.L., Wingo, J., Tillman, J.B., Walford, R.L. and Spindler, S.R. (1999): Calories and aging alter gene expression for gluconeogenic, glycolytic, and nitrogen-metabolizing enzymes. Am. J. Physiol., 277, E352-360.
    • (1999) Am. J. Physiol , vol.277
    • Dhahbi, J.M.1    Mote, P.L.2    Wingo, J.3    Tillman, J.B.4    Walford, R.L.5    Spindler, S.R.6
  • 8
    • 0015578098 scopus 로고
    • The glucose-alanine cycle
    • Felig, P. (1973): The glucose-alanine cycle. Metabolism, 22, 179-207.
    • (1973) Metabolism , vol.22 , pp. 179-207
    • Felig, P.1
  • 9
    • 0017264344 scopus 로고
    • Alanine and glutamine synthesis and release from skeletal muscle. II. The precursor role of amino acids in alanine and glutamine synthesis
    • Garber, A.J., Karl, I.E. and Kipnis, D.M. (1976): Alanine and glutamine synthesis and release from skeletal muscle. II. The precursor role of amino acids in alanine and glutamine synthesis. J. Biol. Chem., 251, 836-843.
    • (1976) J. Biol. Chem , vol.251 , pp. 836-843
    • Garber, A.J.1    Karl, I.E.2    Kipnis, D.M.3
  • 10
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall, A.G., Bardawill, C.J. and David, M.M. (1949): Determination of serum proteins by means of the biuret reaction. J. Biol. Chem., 177, 751-766.
    • (1949) J. Biol. Chem , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 11
    • 21844459973 scopus 로고    scopus 로고
    • 2-Hydroxypropyl-beta-cyclodextrin (HP-beta-CD): A toxicology review
    • Gould, S. and Scott, R.C. (2005): 2-Hydroxypropyl-beta-cyclodextrin (HP-beta-CD): a toxicology review. Food Chem. Toxicol., 43, 1451-1459.
    • (2005) Food Chem. Toxicol , vol.43 , pp. 1451-1459
    • Gould, S.1    Scott, R.C.2
  • 12
    • 0015233550 scopus 로고
    • Aspartate aminotransferase in fat tissues: Changes with growth and hormones
    • Herzfeld, A. and Greengard, O. (1971): Aspartate aminotransferase in fat tissues: changes with growth and hormones. Biochim. Biophys. Acta, 237, 88-98.
    • (1971) Biochim. Biophys. Acta , vol.237 , pp. 88-98
    • Herzfeld, A.1    Greengard, O.2
  • 14
    • 0024005281 scopus 로고
    • Rat cytosolic aspartate aminotransferase: Regulation of its mRNA and contribution to gluconeogenesis
    • Horio, Y., Tanaka, T., Taketoshi, M., Uno, T. and Wada, H. (1988): Rat cytosolic aspartate aminotransferase: regulation of its mRNA and contribution to gluconeogenesis. J. Biochem., 103, 805-808.
    • (1988) J. Biochem , vol.103 , pp. 805-808
    • Horio, Y.1    Tanaka, T.2    Taketoshi, M.3    Uno, T.4    Wada, H.5
  • 15
    • 2342627291 scopus 로고    scopus 로고
    • Murine alanine aminotransferase: CDNA cloning, functional expression, and differential gene regulation in mouse fatty liver
    • Jadaho, S.B., Yang, R.Z., Lin, Q., Hu, H., Anania, F.A., Shuldiner, A.R. and Gong, D.W. (2004): Murine alanine aminotransferase: cDNA cloning, functional expression, and differential gene regulation in mouse fatty liver. Hepatology, 39, 1297-1302.
    • (2004) Hepatology , vol.39 , pp. 1297-1302
    • Jadaho, S.B.1    Yang, R.Z.2    Lin, Q.3    Hu, H.4    Anania, F.A.5    Shuldiner, A.R.6    Gong, D.W.7
  • 17
    • 0014737905 scopus 로고
    • Correlation between triglycerides and glutamic-pyruvic transaminase in men on high-fat diets
    • Katchman, B.J. and Zipf, R.E. (1970): Correlation between triglycerides and glutamic-pyruvic transaminase in men on high-fat diets. Clin. Chem., 16, 118-123.
    • (1970) Clin. Chem , vol.16 , pp. 118-123
    • Katchman, B.J.1    Zipf, R.E.2
  • 18
    • 68549106059 scopus 로고    scopus 로고
    • Effects of fenofibrate on plasma and hepatic transaminase activities and hepatic transaminase gene expression in rats
    • Kobayashi, A., Suzuki, Y., Kuno, H., Sugai, S., Sakakibara, H. and Shimoi, K. (2009): Effects of fenofibrate on plasma and hepatic transaminase activities and hepatic transaminase gene expression in rats. J. Toxicol. Sci., 34, 377-387.
    • (2009) J. Toxicol. Sci , vol.34 , pp. 377-387
    • Kobayashi, A.1    Suzuki, Y.2    Kuno, H.3    Sugai, S.4    Sakakibara, H.5    Shimoi, K.6
  • 19
    • 77958053630 scopus 로고    scopus 로고
    • Relationships between plasma and tissue transaminase activities in rats maintained under different feeding conditions
    • Kobayashi, A., Oshida, S., Yamazaki, Y., Maekawa, T., Kuno, H., Sugai, S., Sakakibara, H. and Shimoi, K. (2010): Relationships between plasma and tissue transaminase activities in rats maintained under different feeding conditions. J. Toxicol. Sci., 35, 639-652.
    • (2010) J. Toxicol. Sci , vol.35 , pp. 639-652
    • Kobayashi, A.1    Oshida, S.2    Yamazaki, Y.3    Maekawa, T.4    Kuno, H.5    Sugai, S.6    Sakakibara, H.7    Shimoi, K.8
  • 20
    • 57049154152 scopus 로고    scopus 로고
    • Studies of the toxicological potential of capsinoids: VII. A 13-week toxicity study of dihydrocapsiate in rats
    • Kodama, T., Watanabe, E., Tsubuku, S., Otabe, A., Mochizuki, M., Masuyama, T. and Bernard, B.K. (2008): Studies of the toxicological potential of capsinoids: VII. A 13-week toxicity study of dihydrocapsiate in rats. Int. J. Toxicol., 27, Suppl. 3, 79-100.
    • (2008) Int. J. Toxicol , vol.27 , Issue.SUPPL. 3 , pp. 79-100
    • Kodama, T.1    Watanabe, E.2    Tsubuku, S.3    Otabe, A.4    Mochizuki, M.5    Masuyama, T.6    Bernard, B.K.7
  • 21
    • 0037303077 scopus 로고    scopus 로고
    • Free fatty acids increase basal hepatic glucose production and induce hepatic insulin resistance at different sites
    • Lam, T.K., van de Werve, G. and Giacca, A. (2003): Free fatty acids increase basal hepatic glucose production and induce hepatic insulin resistance at different sites. Am. J. Physiol. Endocrinol. Metab., 284, E281-290.
    • (2003) Am. J. Physiol. Endocrinol. Metab , vol.284
    • Lam, T.K.1    van de Werve, G.2    Giacca, A.3
  • 22
    • 54449085416 scopus 로고    scopus 로고
    • From the Cover: Physiological significance of a peripheral tissue circadian clock
    • Lamia, K.A., Storch, K.F. and Weitz, C.J. (2008): From the Cover: Physiological significance of a peripheral tissue circadian clock. Proc. Natl. Acad. Sci. USA, 105, 15172-15177.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15172-15177
    • Lamia, K.A.1    Storch, K.F.2    Weitz, C.J.3
  • 23
    • 0019444610 scopus 로고
    • Isolation and purification of aspartate aminotransferase isoenzymes from human liver by chromatography and isoelectric focusing
    • Leung, F.Y. and Henderson, A.R. (1981): Isolation and purification of aspartate aminotransferase isoenzymes from human liver by chromatography and isoelectric focusing. Clin. Chem., 27, 232-238.
    • (1981) Clin. Chem , vol.27 , pp. 232-238
    • Leung, F.Y.1    Henderson, A.R.2
  • 24
    • 0014353509 scopus 로고
    • In vivo and in vitro studies of gluconeogenesis in meal-fed and nibbling rats
    • Leveille, G.A. and Chakrabarty, K. (1968): In vivo and in vitro studies of gluconeogenesis in meal-fed and nibbling rats. J. Nutr., 96, 397-402.
    • (1968) J. Nutr , vol.96 , pp. 397-402
    • Leveille, G.A.1    Chakrabarty, K.2
  • 25
    • 0023874804 scopus 로고
    • In vivo regulation of glycolytic and gluconeogenic enzyme gene expression in newborn rat liver
    • Lyonnet, S., Coupé, C., Girard, J., Kahn, A. and Munnich, A. (1988): In vivo regulation of glycolytic and gluconeogenic enzyme gene expression in newborn rat liver. J. Clin. Invest., 81, 1682-1689.
    • (1988) J. Clin. Invest , vol.81 , pp. 1682-1689
    • Lyonnet, S.1    Coupé, C.2    Girard, J.3    Kahn, A.4    Munnich, A.5
  • 27
    • 34547118377 scopus 로고    scopus 로고
    • A toxicologist guide to the diagnostic interpretation of hepatic biochemical parameters
    • Ramaiah, S.K. (2007): A toxicologist guide to the diagnostic interpretation of hepatic biochemical parameters. Food Chem. Toxicol., 45, 1551-1557.
    • (2007) Food Chem. Toxicol , vol.45 , pp. 1551-1557
    • Ramaiah, S.K.1
  • 28
    • 84961044389 scopus 로고
    • Glucocorticosteroids and transaminase activity. I. Increased activity of glutamicpyruvic transaminase in four conditions associated with gluconeogenesis
    • Rosen, F., Roberts, N.R. and Nichol, C.A. (1959): Glucocorticosteroids and transaminase activity. I. Increased activity of glutamicpyruvic transaminase in four conditions associated with gluconeogenesis. J. Biol. Chem., 234, 476-480.
    • (1959) J. Biol. Chem , vol.234 , pp. 476-480
    • Rosen, F.1    Roberts, N.R.2    Nichol, C.A.3
  • 29
    • 0035919479 scopus 로고    scopus 로고
    • Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors
    • Rutter, J., Reick, M., Wu, L.C. and McKnight, S.L. (2001): Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors. Science, 293, 510-514.
    • (2001) Science , vol.293 , pp. 510-514
    • Rutter, J.1    Reick, M.2    Wu, L.C.3    McKnight, S.L.4
  • 31
    • 0035910387 scopus 로고    scopus 로고
    • Entrainment of the Circadian Clock in the Liver by Feeding
    • Stokkan, K.A., Yamazaki, S., Tei, H., Sakaki, Y. and Menaker, M. (2001): Entrainment of the Circadian Clock in the Liver by Feeding. Science, 291, 490-493.
    • (2001) Science , vol.291 , pp. 490-493
    • Stokkan, K.A.1    Yamazaki, S.2    Tei, H.3    Sakaki, Y.4    Menaker, M.5
  • 32
    • 1642457239 scopus 로고    scopus 로고
    • Opposite regulation of the rat and human cytosolic aspartate aminotransferase genes by fibrates
    • Tomkiewicz, C., Muzeau, F., Edgar, A.D., Barouki, R. and Aggerbeck, M. (2004): Opposite regulation of the rat and human cytosolic aspartate aminotransferase genes by fibrates. Biochem. Pharmacol., 67, 213-225.
    • (2004) Biochem. Pharmacol , vol.67 , pp. 213-225
    • Tomkiewicz, C.1    Muzeau, F.2    Edgar, A.D.3    Barouki, R.4    Aggerbeck, M.5
  • 33
    • 45449118067 scopus 로고    scopus 로고
    • Effects of light cues on re-entrainment of the food-dominated peripheral clocks in mammals
    • Wu, T., Jin, Y., Ni, Y., Zhang, D., Kato, H. and Fu, Z. (2008): Effects of light cues on re-entrainment of the food-dominated peripheral clocks in mammals. Gene, 419, 27-34.
    • (2008) Gene , vol.419 , pp. 27-34
    • Wu, T.1    Jin, Y.2    Ni, Y.3    Zhang, D.4    Kato, H.5    Fu, Z.6
  • 34
    • 61949403067 scopus 로고    scopus 로고
    • Alanine aminotransferase isoenzymes: Molecular cloning and quantitative analysis of tissue expression in rats and serum elevation in liver toxicity
    • Yang, R.Z., Park, S., Reagan, W.J., Goldstein, R., Zhong, S., Lawton, M., Rajamohan, F., Qian, K., Liu, L. and Gong, D.W. (2009): Alanine aminotransferase isoenzymes: Molecular cloning and quantitative analysis of tissue expression in rats and serum elevation in liver toxicity. Hepatology, 49, 598-607.
    • (2009) Hepatology , vol.49 , pp. 598-607
    • Yang, R.Z.1    Park, S.2    Reagan, W.J.3    Goldstein, R.4    Zhong, S.5    Lawton, M.6    Rajamohan, F.7    Qian, K.8    Liu, L.9    Gong, D.W.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.