메뉴 건너뛰기




Volumn 106, Issue 2, 2000, Pages 281-287

Congenital sucrase-isomaltase deficiency arising from cleavage and secretion of a mutant form of the enzyme

Author keywords

[No Author keywords available]

Indexed keywords

SUCRASE ISOMALTASE;

EID: 0033929748     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI9677     Document Type: Article
Times cited : (41)

References (32)
  • 1
    • 84989990014 scopus 로고
    • Genetic aspects of intestinal sucrase-isomaltase deficiency
    • Kerry, K.R., and Townley, R.R.W. 1965. Genetic aspects of intestinal sucrase-isomaltase deficiency. Aust. Paediatr. J. 1:223-235.
    • (1965) Aust. Paediatr. J. , vol.1 , pp. 223-235
    • Kerry, K.R.1    Townley, R.R.W.2
  • 2
    • 0021995494 scopus 로고
    • Transport to cell surface of intestinal sucrase-isomaltase is blocked in the Golgi apparatus in a patient with congenital sucrase-isomaltase deficiency
    • Hauri, H.P., Roth, J., Sterchi, E.E., and Lentze, M.J. 1985. Transport to cell surface of intestinal sucrase-isomaltase is blocked in the Golgi apparatus in a patient with congenital sucrase-isomaltase deficiency. Proc. Natl. Acad. Sci. USA. 82:4423-4427.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4423-4427
    • Hauri, H.P.1    Roth, J.2    Sterchi, E.E.3    Lentze, M.J.4
  • 3
    • 0023118653 scopus 로고
    • A study of the molecular pathology of sucrase-isomaltase deficiency. a defect in the intracellular processing of the enzyme
    • Lloyd, M.L., and Olsen, W.A. 1987. A study of the molecular pathology of sucrase-isomaltase deficiency. A defect in the intracellular processing of the enzyme. N. Engl. J. Med. 316:438-442.
    • (1987) N. Engl. J. Med. , vol.316 , pp. 438-442
    • Lloyd, M.L.1    Olsen, W.A.2
  • 4
    • 0023783489 scopus 로고
    • Sucrase-isomaltase deficiency in humans. Different mutations disrupt intracellular transport, processing, and function of an intestinal brush border enzyme
    • Naim, H.Y., et al. 1988. Sucrase-isomaltase deficiency in humans. Different mutations disrupt intracellular transport, processing, and function of an intestinal brush border enzyme. J. Clin. Invest. 82:667-679.
    • (1988) J. Clin. Invest. , vol.82 , pp. 667-679
    • Naim, H.Y.1
  • 5
    • 0026042569 scopus 로고
    • Naturally occurring mutations in intestinal sucrase-isomaltase provide evidence for the existence of an intracellular sorting signal in the isomaltase subunit
    • Fransen, J.A., Hauri, H.P., Ginsel, L.A., and Naim, H.Y. 1991. Naturally occurring mutations in intestinal sucrase-isomaltase provide evidence for the existence of an intracellular sorting signal in the isomaltase subunit. J. Cell Biol. 115:45-57.
    • (1991) J. Cell Biol. , vol.115 , pp. 45-57
    • Fransen, J.A.1    Hauri, H.P.2    Ginsel, L.A.3    Naim, H.Y.4
  • 6
    • 0022504432 scopus 로고
    • The sucrase-isomaltase complex: Primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein
    • Hunziker, W., Spiess, M., Semenza, G., and Lodish, H.F. 1986. The sucrase-isomaltase complex: primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein. Cell. 46:227-234.
    • (1986) Cell , vol.46 , pp. 227-234
    • Hunziker, W.1    Spiess, M.2    Semenza, G.3    Lodish, H.F.4
  • 7
    • 0018729680 scopus 로고
    • Biogenesis of intestinal plasma membrane: Posttranslational route and cleavage of sucrase-isomaltase
    • Hauri, H.P., Quaroni, A., and Isselbacher, K.J. 1979. Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase. Proc. Natl. Acad. Sci. USA. 76:5183-5186.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5183-5186
    • Hauri, H.P.1    Quaroni, A.2    Isselbacher, K.J.3
  • 8
    • 0023923020 scopus 로고
    • Biosynthesis of the human sucrase-isomaltase complex. Differential O-glycosylation of the sucrase subunit correlates with its position within the enzyme complex
    • Naim, H.Y., Sterchi, E.E., and Lentze, M.J. 1988. Biosynthesis of the human sucrase-isomaltase complex. Differential O-glycosylation of the sucrase subunit correlates with its position within the enzyme complex. J. Biol. Chem. 263:7242-7253.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7242-7253
    • Naim, H.Y.1    Sterchi, E.E.2    Lentze, M.J.3
  • 9
    • 0034008665 scopus 로고    scopus 로고
    • Structural determinants required for apical sorting of an intestinal brush-border membrane protein
    • Jacob, R., Alfalah, M., Grunberg, J., Obendorf, M., and Naim, H.Y. 2000. Structural determinants required for apical sorting of an intestinal brush-border membrane protein. J. Biol. Chem. 275:6566-6572.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6566-6572
    • Jacob, R.1    Alfalah, M.2    Grunberg, J.3    Obendorf, M.4    Naim, H.Y.5
  • 10
    • 0033519624 scopus 로고    scopus 로고
    • O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts
    • Alfalah, M., et al. 1999. O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts. Curr. Biol. 9:593-596.
    • (1999) Curr. Biol. , vol.9 , pp. 593-596
    • Alfalah, M.1
  • 11
    • 0030062178 scopus 로고    scopus 로고
    • Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment
    • Ouwendijk, J., et al. 1996. Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment. J. Clin. Invest. 97:633-641.
    • (1996) J. Clin. Invest. , vol.97 , pp. 633-641
    • Ouwendijk, J.1
  • 12
    • 0023088808 scopus 로고
    • Biosynthesis and maturation of lactase-phlorizin hydrolase in the human small intestinal epithelial cells
    • Naim, H.Y., Sterchi, E.E., and Lentze, M.J. 1987. Biosynthesis and maturation of lactase-phlorizin hydrolase in the human small intestinal epithelial cells. Biochem. J. 241:427-434.
    • (1987) Biochem. J. , vol.241 , pp. 427-434
    • Naim, H.Y.1    Sterchi, E.E.2    Lentze, M.J.3
  • 13
    • 0031003841 scopus 로고    scopus 로고
    • A mutation in a highly conserved region in brush-border sucrase-isomaltase and lysosomal alpha-glucosidase results in Golgi retention
    • Moolenaar, C.E., et al. 1997. A mutation in a highly conserved region in brush-border sucrase-isomaltase and lysosomal alpha-glucosidase results in Golgi retention. J. Cell Sci. 110:557-567.
    • (1997) J. Cell Sci. , vol.110 , pp. 557-567
    • Moolenaar, C.E.1
  • 14
    • 0033583312 scopus 로고    scopus 로고
    • Hierarchy of sorting signals in chimeras of intestinal lactase-phlorizin hydrolase and the influenza virus hemagglutinin
    • Jacob, R., et al. 1999. Hierarchy of sorting signals in chimeras of intestinal lactase-phlorizin hydrolase and the influenza virus hemagglutinin. J. Biol. Chem. 274:8061-8067.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8061-8067
    • Jacob, R.1
  • 15
    • 0025823166 scopus 로고
    • Expression of a full-length cDNa coding for human intestinal lactase-phlorizin hydrolase reveals an uncleaved, enzymatically active, and transport-competent protein
    • Naim, H.Y., Lacey, S.W., Sambrook, J.F., and Gething, M.J. 1991. Expression of a full-length cDNA coding for human intestinal lactase-phlorizin hydrolase reveals an uncleaved, enzymatically active, and transport-competent protein. J. Biol. Chem. 266:12313-12320.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12313-12320
    • Naim, H.Y.1    Lacey, S.W.2    Sambrook, J.F.3    Gething, M.J.4
  • 16
    • 0022181709 scopus 로고
    • Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells
    • Hauri, H.P., Sterchi, E.E., Bienz, D., Fransen, J.A., and Marxer, A. 1985. Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells. J. Cell Biol. 101:838-851.
    • (1985) J. Cell Biol. , vol.101 , pp. 838-851
    • Hauri, H.P.1    Sterchi, E.E.2    Bienz, D.3    Fransen, J.A.4    Marxer, A.5
  • 17
    • 0014235959 scopus 로고
    • Assay of intestinal disaccharidases
    • Dahlqvist, A. 1968. Assay of intestinal disaccharidases. Anal. Biochem. 22:99-107.
    • (1968) Anal. Biochem. , vol.22 , pp. 99-107
    • Dahlqvist, A.1
  • 18
    • 0029044647 scopus 로고
    • Ultrastructural, immunocytochemical and stereological investigation of hepatocytes in a patient with the mutation of the ornithine transcarbamylase gene
    • Zimmer, K.P., et al. 1995. Ultrastructural, immunocytochemical and stereological investigation of hepatocytes in a patient with the mutation of the ornithine transcarbamylase gene. Eur. J. Cell Biol. 67:73-83.
    • (1995) Eur. J. Cell Biol. , vol.67 , pp. 73-83
    • Zimmer, K.P.1
  • 19
    • 0023277698 scopus 로고
    • The posttranslational processing of sucrase-isomaltase in HT-29 cells is a function of their state of enterocytic differentiation
    • Trugnan, G., Rousset, M., Chantret, I., Barbat, A., and Zweibaum, A. 1987. The posttranslational processing of sucrase-isomaltase in HT-29 cells is a function of their state of enterocytic differentiation. J. Cell Biol. 104:1199-1205.
    • (1987) J. Cell Biol. , vol.104 , pp. 1199-1205
    • Trugnan, G.1    Rousset, M.2    Chantret, I.3    Barbat, A.4    Zweibaum, A.5
  • 20
    • 0023552339 scopus 로고
    • Identification of an endosomal antigen specific to absorptive cells of suckling rat ileum
    • Wilson, J.M., Whitney, J.A., and Neutra, M.R. 1987. Identification of an endosomal antigen specific to absorptive cells of suckling rat ileum. J. Cell Biol. 105:691-703.
    • (1987) J. Cell Biol. , vol.105 , pp. 691-703
    • Wilson, J.M.1    Whitney, J.A.2    Neutra, M.R.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0026674130 scopus 로고
    • Sequence of the complete cDNa and the 5′ structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase
    • Chantret, I., et al. 1992. Sequence of the complete cDNA and the 5′ structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase. Biochem. J. 285:915-923.
    • (1992) Biochem. J. , vol.285 , pp. 915-923
    • Chantret, I.1
  • 23
    • 0027509615 scopus 로고
    • Transformation of the signal peptide/membrane anchor domain of a type II transmembrane protein into a cleavable signal peptide
    • Roy, P., Chatellard, C., Lemay, G., Crine, P., and Boileau, G. 1993. Transformation of the signal peptide/membrane anchor domain of a type II transmembrane protein into a cleavable signal peptide. J. Biol. Chem. 268:2699-2704.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2699-2704
    • Roy, P.1    Chatellard, C.2    Lemay, G.3    Crine, P.4    Boileau, G.5
  • 24
    • 0023685557 scopus 로고
    • Sequences beyond the cleavage site influence signal peptide function
    • Andrews, D.W., Perara, E., Lesser, C., and Lingappa, V.R. 1988. Sequences beyond the cleavage site influence signal peptide function. J. Biol. Chem. 263:15791-15798.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15791-15798
    • Andrews, D.W.1    Perara, E.2    Lesser, C.3    Lingappa, V.R.4
  • 25
    • 0024600703 scopus 로고
    • Mutations in signal sequence cleavage domain of preproparathyroid hormone alter protein translocation, signal sequence cleavage, and membrane-binding properties
    • Wiren, K.M., et al. 1989. Mutations in signal sequence cleavage domain of preproparathyroid hormone alter protein translocation, signal sequence cleavage, and membrane-binding properties. Mol. Endocrinol. 3:240-250.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 240-250
    • Wiren, K.M.1
  • 26
    • 0025723516 scopus 로고
    • Alteration of N-terminal residues of mature human lysozyme affects its secretion in yeast and translocation into canine microsomal vesicles
    • Kohara, A., Yamamoto, Y., and Kikuchi, M. 1991. Alteration of N-terminal residues of mature human lysozyme affects its secretion in yeast and translocation into canine microsomal vesicles. J. Biol. Chem. 266:20363-20368.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20363-20368
    • Kohara, A.1    Yamamoto, Y.2    Kikuchi, M.3
  • 27
    • 0028218512 scopus 로고
    • Deletion mutation in the signal anchor domain activates cleavage of the influenza virus neuraminidase, a type II transmembrane protein
    • Hogue, B.G., and Nayak, D.P. 1994. Deletion mutation in the signal anchor domain activates cleavage of the influenza virus neuraminidase, a type II transmembrane protein. J. Gen. Virol. 75:1015-1022.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1015-1022
    • Hogue, B.G.1    Nayak, D.P.2
  • 28
    • 0026787448 scopus 로고
    • Single amino acid substitutions can convert the uncleaved signal-anchor of sucrase-isomaltase to a cleaved signal sequence
    • Hegner, M., et al. 1992. Single amino acid substitutions can convert the uncleaved signal-anchor of sucrase-isomaltase to a cleaved signal sequence. J. Biol. Chem. 267:16928-16933.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16928-16933
    • Hegner, M.1
  • 29
    • 0001422048 scopus 로고    scopus 로고
    • Positional preference of proline in alpha-helices
    • Kim, M.K., and Kang, Y.K. 1999. Positional preference of proline in alpha-helices. Protien Sci. 8:1492-1499.
    • (1999) Protien Sci. , vol.8 , pp. 1492-1499
    • Kim, M.K.1    Kang, Y.K.2
  • 30
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • Cheng, S.H., et al. 1990. Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell. 63:827-834.
    • (1990) Cell , vol.63 , pp. 827-834
    • Cheng, S.H.1
  • 31
    • 0031006578 scopus 로고    scopus 로고
    • Compound missense mutations in the sodium/D-glucose cotransporter result in trafficking defects
    • Martin, M.G., et al. 1997. Compound missense mutations in the sodium/D-glucose cotransporter result in trafficking defects. Gastroenterology. 112:1206-1212.
    • (1997) Gastroenterology , vol.112 , pp. 1206-1212
    • Martin, M.G.1
  • 32
    • 0032561463 scopus 로고    scopus 로고
    • Mutation at the processing site of chicken low density lipoprotein receptor-related protein impairs efficient endoplasmic reticulum exit, but proteolytic cleavage is not essential for its endocytic functions
    • Ko, K.W., et al. 1998. Mutation at the processing site of chicken low density lipoprotein receptor-related protein impairs efficient endoplasmic reticulum exit, but proteolytic cleavage is not essential for its endocytic functions. J. Biol. Chem. 273:27779-27785.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27779-27785
    • Ko, K.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.