메뉴 건너뛰기




Volumn 24, Issue 3, 2013, Pages 606-612

Methylation of histone H3 at lysine 4 and expression of the maltase-glucoamylase gene are reduced by dietary resistant starch

Author keywords

Chromatin; Maltase glucoamylase; Methylated histone H3 at K4; Resistant starch; Small intestine

Indexed keywords

ALPHA GLUCOSIDASE; HISTONE H3; LYSINE; STARCH;

EID: 84875508401     PISSN: 09552863     EISSN: 18734847     Source Type: Journal    
DOI: 10.1016/j.jnutbio.2012.03.006     Document Type: Article
Times cited : (6)

References (34)
  • 1
    • 0026571574 scopus 로고
    • Starch digestion and absorption in nonruminants
    • Gray G.M. Starch digestion and absorption in nonruminants. J Nutr 1992, 122(1):172-177.
    • (1992) J Nutr , vol.122 , Issue.1 , pp. 172-177
    • Gray, G.M.1
  • 2
    • 0037417990 scopus 로고    scopus 로고
    • The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch digestion activities
    • Nichols B.L., Avery S., Sen P., Swallow D.M., Hahn D., Sterchi E. The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch digestion activities. Proc Natl Acad Sci USA 2003, 100(3):1432-1437.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.3 , pp. 1432-1437
    • Nichols, B.L.1    Avery, S.2    Sen, P.3    Swallow, D.M.4    Hahn, D.5    Sterchi, E.6
  • 3
    • 0032579520 scopus 로고    scopus 로고
    • Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.
    • Nichols B.L., Eldering J., Avery S., Hahn D., Quaroni A., Sterchi E. Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase. JBiol Chem 1998, 273(5):3076-3081.
    • (1998) JBiol Chem , vol.273 , Issue.5 , pp. 3076-3081
    • Nichols, B.L.1    Eldering, J.2    Avery, S.3    Hahn, D.4    Quaroni, A.5    Sterchi, E.6
  • 4
    • 34447125036 scopus 로고    scopus 로고
    • Contribution of mucosal maltase-glucoamylase activities to mouse small intestinal starch alpha-glucogenesis
    • Quezada-Calvillo R., Robayo-Torres C.C., Opekun A.R., Sen P., Ao Z., Hamaker B.R., et al. Contribution of mucosal maltase-glucoamylase activities to mouse small intestinal starch alpha-glucogenesis. J Nutr 2007, 137(7):1725-1733.
    • (2007) J Nutr , vol.137 , Issue.7 , pp. 1725-1733
    • Quezada-Calvillo, R.1    Robayo-Torres, C.C.2    Opekun, A.R.3    Sen, P.4    Ao, Z.5    Hamaker, B.R.6
  • 5
    • 79951743624 scopus 로고    scopus 로고
    • The regulation of jejunal induction of the maltase-glucoamylase gene by a high starch/low fat-diet in mice
    • Mochizuki K., Honma K., Shimada M., Goda T. The regulation of jejunal induction of the maltase-glucoamylase gene by a high starch/low fat-diet in mice. Mol Nutr Food Res 2010, 54(10):1445-1451.
    • (2010) Mol Nutr Food Res , vol.54 , Issue.10 , pp. 1445-1451
    • Mochizuki, K.1    Honma, K.2    Shimada, M.3    Goda, T.4
  • 6
    • 0027972277 scopus 로고
    • Effect of high-amylose starch on carbohydrate digestive capability and lipogenesis in epididymal adipose tissue and liver of rats
    • Goda T., Urakawa T., Watanabe M., Takase S. Effect of high-amylose starch on carbohydrate digestive capability and lipogenesis in epididymal adipose tissue and liver of rats. J Nutr Biochem 1994, 5(5):256-260.
    • (1994) J Nutr Biochem , vol.5 , Issue.5 , pp. 256-260
    • Goda, T.1    Urakawa, T.2    Watanabe, M.3    Takase, S.4
  • 7
    • 0019991032 scopus 로고
    • Effect of sucrose and Acarbose feeding on the development of streptozotocin-induced diabetes in the rat
    • Goda T., Yamada K., Sugiyama M., Moriuchi S., Hosoya N. Effect of sucrose and Acarbose feeding on the development of streptozotocin-induced diabetes in the rat. J Nutr Sci Vitaminol (Tokyo) 1982, 28(1):41-56.
    • (1982) J Nutr Sci Vitaminol (Tokyo) , vol.28 , Issue.1 , pp. 41-56
    • Goda, T.1    Yamada, K.2    Sugiyama, M.3    Moriuchi, S.4    Hosoya, N.5
  • 8
    • 64049105770 scopus 로고    scopus 로고
    • Mucosal maltase-glucoamylase plays a crucial role in starch digestion and prandial glucose homeostasis of mice
    • Nichols B.L., Quezada-Calvillo R., Robayo-Torres C.C., Ao Z., Hamaker B.R., Butte N.F., et al. Mucosal maltase-glucoamylase plays a crucial role in starch digestion and prandial glucose homeostasis of mice. J Nutr 2009, 139(4):684-690.
    • (2009) J Nutr , vol.139 , Issue.4 , pp. 684-690
    • Nichols, B.L.1    Quezada-Calvillo, R.2    Robayo-Torres, C.C.3    Ao, Z.4    Hamaker, B.R.5    Butte, N.F.6
  • 9
    • 0037116638 scopus 로고    scopus 로고
    • Oral antihyperglycemic therapy for type 2 diabetes: scientific review
    • Inzucchi S.E. Oral antihyperglycemic therapy for type 2 diabetes: scientific review. JAMA 2002, 287(3):360-372.
    • (2002) JAMA , vol.287 , Issue.3 , pp. 360-372
    • Inzucchi, S.E.1
  • 10
    • 0038185186 scopus 로고    scopus 로고
    • Is there a role for alpha-glucosidase inhibitors in the prevention of type 2 diabetes mellitus?
    • Scheen A.J. Is there a role for alpha-glucosidase inhibitors in the prevention of type 2 diabetes mellitus?. Drugs 2003, 63(10):933-951.
    • (2003) Drugs , vol.63 , Issue.10 , pp. 933-951
    • Scheen, A.J.1
  • 11
    • 0035943624 scopus 로고    scopus 로고
    • Sucrase-isomaltase gene transcription requires the hepatocyte nuclear factor-1 (HNF-1) regulatory element and is regulated by the ratio of HNF-1 alpha to HNF-1 beta
    • Boudreau F., Zhu Y., Traber P.G. Sucrase-isomaltase gene transcription requires the hepatocyte nuclear factor-1 (HNF-1) regulatory element and is regulated by the ratio of HNF-1 alpha to HNF-1 beta. J Biol Chem 2001, 276(34):32122-32128.
    • (2001) J Biol Chem , vol.276 , Issue.34 , pp. 32122-32128
    • Boudreau, F.1    Zhu, Y.2    Traber, P.G.3
  • 13
    • 2642570305 scopus 로고    scopus 로고
    • The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote
    • Schubeler D., MacAlpine D.M., Scalzo D., Wirbelauer C., Kooperberg C., van Leeuwen F., et al. The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. Genes Dev 2004, 18(11):1263-1271.
    • (2004) Genes Dev , vol.18 , Issue.11 , pp. 1263-1271
    • Schubeler, D.1    MacAlpine, D.M.2    Scalzo, D.3    Wirbelauer, C.4    Kooperberg, C.5    van Leeuwen, F.6
  • 14
    • 3543008920 scopus 로고    scopus 로고
    • High-resolution genome-wide mapping of histone modifications
    • Roh T.Y., Ngau W.C., Cui K., Landsman D., Zhao K. High-resolution genome-wide mapping of histone modifications. Nat Biotechnol 2004, 22(8):1013-1016.
    • (2004) Nat Biotechnol , vol.22 , Issue.8 , pp. 1013-1016
    • Roh, T.Y.1    Ngau, W.C.2    Cui, K.3    Landsman, D.4    Zhao, K.5
  • 15
    • 14644406272 scopus 로고    scopus 로고
    • Active chromatin domains are defined by acetylation islands revealed by genome-wide mapping
    • Roh T.Y., Cuddapah S., Zhao K. Active chromatin domains are defined by acetylation islands revealed by genome-wide mapping. Genes Dev 2005, 19(5):542-552.
    • (2005) Genes Dev , vol.19 , Issue.5 , pp. 542-552
    • Roh, T.Y.1    Cuddapah, S.2    Zhao, K.3
  • 16
    • 69949127823 scopus 로고    scopus 로고
    • Feeding rats dietary resistant starch shifts the peak of SGLT1 gene expression and histone H3 acetylation on the gene from the upper jejunum toward the ileum
    • Shimada M., Mochizuki K., Goda T. Feeding rats dietary resistant starch shifts the peak of SGLT1 gene expression and histone H3 acetylation on the gene from the upper jejunum toward the ileum. J Agric Food Chem 2009, 57(17):8049-8055.
    • (2009) J Agric Food Chem , vol.57 , Issue.17 , pp. 8049-8055
    • Shimada, M.1    Mochizuki, K.2    Goda, T.3
  • 17
    • 1642564551 scopus 로고    scopus 로고
    • Selective recognition of acetylated histones by bromodomain proteins visualized in living cells
    • Kanno T., Kanno Y., Siegel R.M., Jang M.K., Lenardo M.J., Ozato K. Selective recognition of acetylated histones by bromodomain proteins visualized in living cells. Mol Cell 2004, 13(1):33-43.
    • (2004) Mol Cell , vol.13 , Issue.1 , pp. 33-43
    • Kanno, T.1    Kanno, Y.2    Siegel, R.M.3    Jang, M.K.4    Lenardo, M.J.5    Ozato, K.6
  • 18
    • 23744514308 scopus 로고    scopus 로고
    • The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription
    • Jang M.K., Mochizuki K., Zhou M., Jeong H.S., Brady J.N., Ozato K. The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription. Mol Cell 2005, 19(4):523-534.
    • (2005) Mol Cell , vol.19 , Issue.4 , pp. 523-534
    • Jang, M.K.1    Mochizuki, K.2    Zhou, M.3    Jeong, H.S.4    Brady, J.N.5    Ozato, K.6
  • 19
    • 7044250740 scopus 로고    scopus 로고
    • Lysine acetylation and the bromodomain: a new partnership for signaling
    • Yang X.J. Lysine acetylation and the bromodomain: a new partnership for signaling. Bioessays 2004, 26(10):1076-1087.
    • (2004) Bioessays , vol.26 , Issue.10 , pp. 1076-1087
    • Yang, X.J.1
  • 20
    • 0035694922 scopus 로고    scopus 로고
    • Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase
    • Wang H., Cao R., Xia L., Erdjument-Bromage H., Borchers C., Tempst P., et al. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol Cell 2001, 8(6):1207-1217.
    • (2001) Mol Cell , vol.8 , Issue.6 , pp. 1207-1217
    • Wang, H.1    Cao, R.2    Xia, L.3    Erdjument-Bromage, H.4    Borchers, C.5    Tempst, P.6
  • 21
    • 33745198218 scopus 로고    scopus 로고
    • Histone H3 lysine 4 dimethylation signals the transcriptional competence of the adiponectin promoter in preadipocytes
    • Musri M.M., Corominola H., Casamitjana R., Gomis R., Parrizas M. Histone H3 lysine 4 dimethylation signals the transcriptional competence of the adiponectin promoter in preadipocytes. J Biol Chem 2006, 281(25):17180-17188.
    • (2006) J Biol Chem , vol.281 , Issue.25 , pp. 17180-17188
    • Musri, M.M.1    Corominola, H.2    Casamitjana, R.3    Gomis, R.4    Parrizas, M.5
  • 22
    • 33751116960 scopus 로고    scopus 로고
    • Histone H3 Lys 4 methylation: caught in a bind?
    • Sims R.J., Reinberg D. Histone H3 Lys 4 methylation: caught in a bind?. Genes Dev 2006, 20(20):2779-2786.
    • (2006) Genes Dev , vol.20 , Issue.20 , pp. 2779-2786
    • Sims, R.J.1    Reinberg, D.2
  • 23
    • 33745839365 scopus 로고    scopus 로고
    • A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling
    • Wysocka J., Swigut T., Xiao H., Milne T.A., Kwon S.Y., Landry J., et al. A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling. Nature 2006, 442(7098):86-90.
    • (2006) Nature , vol.442 , Issue.7098 , pp. 86-90
    • Wysocka, J.1    Swigut, T.2    Xiao, H.3    Milne, T.A.4    Kwon, S.Y.5    Landry, J.6
  • 24
    • 0034785146 scopus 로고    scopus 로고
    • Heat moisture treatment of high amylose cornstarch increases its resistant starch content but not its physiologic effects in rats
    • Kishida T., Nogami H., Himeno S., Ebihara K. Heat moisture treatment of high amylose cornstarch increases its resistant starch content but not its physiologic effects in rats. J Nutr 2001, 131(10):2716-2721.
    • (2001) J Nutr , vol.131 , Issue.10 , pp. 2716-2721
    • Kishida, T.1    Nogami, H.2    Himeno, S.3    Ebihara, K.4
  • 25
    • 36348988477 scopus 로고    scopus 로고
    • Heat-moisture treatment of high-amylose corn starch increases dietary fiber content and lowers plasma cholesterol in ovariectomized rats
    • Liu X., Ogawa H., Ando R., Nakakuki T., Kishida T., Ebihara K. Heat-moisture treatment of high-amylose corn starch increases dietary fiber content and lowers plasma cholesterol in ovariectomized rats. J Food Sci 2007, 72(9):S652-S658.
    • (2007) J Food Sci , vol.72 , Issue.9
    • Liu, X.1    Ogawa, H.2    Ando, R.3    Nakakuki, T.4    Kishida, T.5    Ebihara, K.6
  • 26
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987, 162(1):156-159.
    • (1987) Anal Biochem , vol.162 , Issue.1 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 27
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 2001, 25(4):402-408.
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 28
  • 29
    • 4444368426 scopus 로고
    • Method for Assay of Intestinal Disaccharidases
    • Dahlqvist A. Method for Assay of Intestinal Disaccharidases. Anal Biochem 1964, 7:18-25.
    • (1964) Anal Biochem , vol.7 , pp. 18-25
    • Dahlqvist, A.1
  • 30
    • 34247873186 scopus 로고    scopus 로고
    • Carbohydrate/fat ratio in the diet alters histone acetylation on the sucrase-isomaltase gene and its expression in mouse small intestine
    • Honma K., Mochizuki K., Goda T. Carbohydrate/fat ratio in the diet alters histone acetylation on the sucrase-isomaltase gene and its expression in mouse small intestine. Biochem Biophys Res Commun 2007, 357(4):1124-1129.
    • (2007) Biochem Biophys Res Commun , vol.357 , Issue.4 , pp. 1124-1129
    • Honma, K.1    Mochizuki, K.2    Goda, T.3
  • 31
    • 33646526684 scopus 로고    scopus 로고
    • Alpha-Glucosidase inhibitors prevent diet-induced increases in intestinal sugar transport in diabetic mice
    • Casirola D.M., Ferraris R.P. alpha-Glucosidase inhibitors prevent diet-induced increases in intestinal sugar transport in diabetic mice. Metabolism 2006, 55(6):832-841.
    • (2006) Metabolism , vol.55 , Issue.6 , pp. 832-841
    • Casirola, D.M.1    Ferraris, R.P.2
  • 32
    • 77953158697 scopus 로고    scopus 로고
    • Changes in mucosal alpha-glucosidase activities along the jejunal-ileal axis by an Hm-HACS diet intake are associated with decreased lipogenic enzyme activity in epididymal adipose tissue
    • Mochizuki K., Sato Y., Takase S., Goda T. Changes in mucosal alpha-glucosidase activities along the jejunal-ileal axis by an Hm-HACS diet intake are associated with decreased lipogenic enzyme activity in epididymal adipose tissue. J Agric Food Chem 2010, 58(11):6923-6927.
    • (2010) J Agric Food Chem , vol.58 , Issue.11 , pp. 6923-6927
    • Mochizuki, K.1    Sato, Y.2    Takase, S.3    Goda, T.4
  • 33
    • 0029040969 scopus 로고
    • Effect of resistant starch on fecal bulk and fermentation-dependent events in humans
    • Phillips J., Muir J.G., Birkett A., Lu Z.X., Jones G.P., O'Dea K., et al. Effect of resistant starch on fecal bulk and fermentation-dependent events in humans. Am J Clin Nutr 1995, 62(1):121-130.
    • (1995) Am J Clin Nutr , vol.62 , Issue.1 , pp. 121-130
    • Phillips, J.1    Muir, J.G.2    Birkett, A.3    Lu, Z.X.4    Jones, G.P.5    O'Dea, K.6
  • 34
    • 17144404895 scopus 로고    scopus 로고
    • Health properties of resistant starch
    • Nugent A.P. Health properties of resistant starch. Br Nutr Foundation Nutr Bull 2005, 30:27-54.
    • (2005) Br Nutr Foundation Nutr Bull , vol.30 , pp. 27-54
    • Nugent, A.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.