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Volumn 6, Issue 9, 2011, Pages

Characterization of the biosynthesis, processing and kinetic mechanism of action of the enzyme deficient in mucopolysaccharidosis IIIC

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; LIPID; DETERGENT; HGSNAT PROTEIN, HUMAN;

EID: 80053037444     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0024951     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 0018222893 scopus 로고
    • A new biochemical subtype of the Sanfilippo syndrome: characterization of the storage material in cultured fibroblasts of Sanfilippo C patients
    • Kresse H, Von Figura K, Klein U, (1978) A new biochemical subtype of the Sanfilippo syndrome: characterization of the storage material in cultured fibroblasts of Sanfilippo C patients. Euro J Biochem 92: 333-339.
    • (1978) Euro J Biochem , vol.92 , pp. 333-339
    • Kresse, H.1    von Figura, K.2    Klein, U.3
  • 2
    • 0000869162 scopus 로고    scopus 로고
    • The Mucopolysaccharides
    • In: Scriver CR, Beaudet AL, Sly WS, Valle D, editors, New York, McGraw-Hill,8 Ed
    • Neufeld EF, Muenzer J, (2001) The Mucopolysaccharides. In: Scriver CR, Beaudet AL, Sly WS, Valle D, editors. The Metabolic and Molecular Bases of Inherited Disease. 8 ed New York McGraw-Hill pp. 3421-3452.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3421-3452
    • Neufeld, E.F.1    Muenzer, J.2
  • 3
    • 0018214687 scopus 로고
    • Sanfilippo syndrome type C: deficiency of acetyl-CoA:alpha-glucosaminide N-acetyltransferase in skin fibroblasts
    • Klein U, Kresse H, von Figura K, (1978) Sanfilippo syndrome type C: deficiency of acetyl-CoA:alpha-glucosaminide N-acetyltransferase in skin fibroblasts. Proc Natl Acad Sci U S A 75: 5185-5189.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 5185-5189
    • Klein, U.1    Kresse, H.2    von Figura, K.3
  • 4
    • 33749024739 scopus 로고    scopus 로고
    • Identification of the gene encoding the enzyme deficient in MPS IIIC (Sanfilippo type C)
    • Fan X, Zhang H, Zhang S, Bagshaw RD, Tropak MB, et al. (2006) Identification of the gene encoding the enzyme deficient in MPS IIIC (Sanfilippo type C). Am J Hum Genet 79: 738-744.
    • (2006) Am J Hum Genet , vol.79 , pp. 738-744
    • Fan, X.1    Zhang, H.2    Zhang, S.3    Bagshaw, R.D.4    Tropak, M.B.5
  • 5
    • 33751117228 scopus 로고    scopus 로고
    • Mutations in TMEM76* cause mucopolysaccharidosis IIIC (Sanfilippo C syndrome)
    • Hrebicek M, Mrazova L, Seyrantepe V, Durand S, Roslin NM, et al. (2006) Mutations in TMEM76* cause mucopolysaccharidosis IIIC (Sanfilippo C syndrome). Am J Hum Genet 79: 807-819.
    • (2006) Am J Hum Genet , vol.79 , pp. 807-819
    • Hrebicek, M.1    Mrazova, L.2    Seyrantepe, V.3    Durand, S.4    Roslin, N.M.5
  • 6
    • 77954116878 scopus 로고    scopus 로고
    • Functional analysis of the HGSNAT gene in patients with mucopolysaccharidosis IIIC (Sanfilippo C Syndrome)
    • Fedele AO, Hopwood JJ, (2010) Functional analysis of the HGSNAT gene in patients with mucopolysaccharidosis IIIC (Sanfilippo C Syndrome). Hum Mutat 31: E1574-1586.
    • (2010) Hum Mutat , vol.31 , pp. 1574-1586
    • Fedele, A.O.1    Hopwood, J.J.2
  • 7
    • 80052618375 scopus 로고    scopus 로고
    • Molecular analysis of Sanfilippo syndrome type C in Spain: seven novel HGSNAT mutations and characterization of the mutant alleles
    • in press
    • Canals I, Elalaoui SC, Pineda M, Delgadillo V, Szlago M, et al. (2010) Molecular analysis of Sanfilippo syndrome type C in Spain: seven novel HGSNAT mutations and characterization of the mutant alleles. Clinical Genetics in press.
    • (2010) Clinical Genetics
    • Canals, I.1    Elalaoui, S.C.2    Pineda, M.3    Delgadillo, V.4    Szlago, M.5
  • 8
    • 29344470512 scopus 로고    scopus 로고
    • An acetylated 120-kDa lysosomal transmembrane protein is absent from mucopolysaccharidosis IIIC fibroblasts: a candidate molecule for MPS IIIC
    • Ausseil J, Landry K, Seyrantepe V, Trudel S, Mazur A, et al. (2006) An acetylated 120-kDa lysosomal transmembrane protein is absent from mucopolysaccharidosis IIIC fibroblasts: a candidate molecule for MPS IIIC. Mol Genet Metab 87: 22-31.
    • (2006) Mol Genet Metab , vol.87 , pp. 22-31
    • Ausseil, J.1    Landry, K.2    Seyrantepe, V.3    Trudel, S.4    Mazur, A.5
  • 9
    • 0022195520 scopus 로고
    • Acteyl Coenzyme A: alpha-Glucosaminide NAceyltransferase: Evidence for a transmembrane acetylation mechanism
    • Bame KJ, Rome LH, (1985) Acteyl Coenzyme A: alpha-Glucosaminide NAceyltransferase: Evidence for a transmembrane acetylation mechanism. J Biol Chem 260: 11293-11299.
    • (1985) J Biol Chem , vol.260 , pp. 11293-11299
    • Bame, K.J.1    Rome, L.H.2
  • 10
    • 34748843178 scopus 로고    scopus 로고
    • Lending a helping hand, screening chemical libraries for compounds that enhance ß-hexosaminidase A activity in GM2 Gangliosidosis cells
    • Tropak MB, Mahuran D, (2007) Lending a helping hand, screening chemical libraries for compounds that enhance ß-hexosaminidase A activity in GM2 Gangliosidosis cells. FEBS J 274: 4951-4961.
    • (2007) FEBS J , vol.274 , pp. 4951-4961
    • Tropak, M.B.1    Mahuran, D.2
  • 12
    • 0022468494 scopus 로고
    • Genetic evidence for transmembrane acetylation by lysosomes
    • Bame KJ, Rome LH, (1986) Genetic evidence for transmembrane acetylation by lysosomes. Science 233: 1087-1089.
    • (1986) Science , vol.233 , pp. 1087-1089
    • Bame, K.J.1    Rome, L.H.2
  • 13
    • 77957794731 scopus 로고    scopus 로고
    • Analysis of the Biogenesis of Heparan Sulfate Acetyl-CoA: {alpha}-Glucosaminide N-Acetyltransferase Provides Insights into the Mechanism Underlying Its Complete Deficiency in Mucopolysaccharidosis IIIC
    • Durand S, Feldhammer M, Bonneil E, Thibault P, Pshezhetsky AV, (2010) Analysis of the Biogenesis of Heparan Sulfate Acetyl-CoA: {alpha}-Glucosaminide N-Acetyltransferase Provides Insights into the Mechanism Underlying Its Complete Deficiency in Mucopolysaccharidosis IIIC. J Biol Chem 285: 31233-31242.
    • (2010) J Biol Chem , vol.285 , pp. 31233-31242
    • Durand, S.1    Feldhammer, M.2    Bonneil, E.3    Thibault, P.4    Pshezhetsky, A.V.5
  • 14
    • 0028989710 scopus 로고
    • Human acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase. Kinetic characterization and mechanistic interpretation
    • Meikle PJ, Whittle AM, Hopwood JJ, (1995) Human acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase. Kinetic characterization and mechanistic interpretation. Biochem J 308: 327-333.
    • (1995) Biochem J , vol.308 , pp. 327-333
    • Meikle, P.J.1    Whittle, A.M.2    Hopwood, J.J.3
  • 16
    • 77949322837 scopus 로고    scopus 로고
    • Protein misfolding as an underlying molecular defect in mucopolysaccharidosis III type C
    • Feldhammer M, Durand S, Pshezhetsky AV, (2009) Protein misfolding as an underlying molecular defect in mucopolysaccharidosis III type C. PLoS One 4: e7434.
    • (2009) PLoS One , vol.4
    • Feldhammer, M.1    Durand, S.2    Pshezhetsky, A.V.3
  • 17
    • 0025924830 scopus 로고
    • The human GM2 activator protein. A substrate specific cofactor of ß-hexosaminidase A
    • Meier EM, Schwarzmann G, Fürst W, Sandhoff K, (1991) The human GM2 activator protein. A substrate specific cofactor of ß-hexosaminidase A. J Biol Chem 266: 1879-1887.
    • (1991) J Biol Chem , vol.266 , pp. 1879-1887
    • Meier, E.M.1    Schwarzmann, G.2    Fürst, W.3    Sandhoff, K.4
  • 18
    • 77949886783 scopus 로고    scopus 로고
    • A sensitive fluorescence-based assay for monitoring GM2 ganglioside hydrolysis in live patient cells and their lysates
    • Tropak MB, Bukovac SW, Rigat BA, Yonekawa S, Wakarchuk W, et al. (2010) A sensitive fluorescence-based assay for monitoring GM2 ganglioside hydrolysis in live patient cells and their lysates. Glycobiology 20: 356-365.
    • (2010) Glycobiology , vol.20 , pp. 356-365
    • Tropak, M.B.1    Bukovac, S.W.2    Rigat, B.A.3    Yonekawa, S.4    Wakarchuk, W.5
  • 19
    • 0019151902 scopus 로고
    • The subunit and polypeptide structure of hexosaminidase from human placenta
    • Mahuran DJ, Lowden JA, (1980) The subunit and polypeptide structure of hexosaminidase from human placenta. Can J Biochem 58: 287-294.
    • (1980) Can J Biochem , vol.58 , pp. 287-294
    • Mahuran, D.J.1    Lowden, J.A.2
  • 20
    • 0032409906 scopus 로고    scopus 로고
    • Application of magnetic chromatography to the isolation of lysosomes from fibroblasts of patients with lysosomal storage disorders
    • Diettrich O, Mills K, Johnson AW, Hasilik A, Winchester BG, (1998) Application of magnetic chromatography to the isolation of lysosomes from fibroblasts of patients with lysosomal storage disorders. FEBS Lett 441: 369-372.
    • (1998) FEBS Lett , vol.441 , pp. 369-372
    • Diettrich, O.1    Mills, K.2    Johnson, A.W.3    Hasilik, A.4    Winchester, B.G.5
  • 21
    • 69949119548 scopus 로고    scopus 로고
    • Identification and characterization of ambroxol as an enzyme-enhancement agent for gaucher disease
    • Maegawa GHB, Tropak MB, Buttner JD, Rigat BA, Fuller M, et al. (2009) Identification and characterization of ambroxol as an enzyme-enhancement agent for gaucher disease. J Biol Chem 284: 23502-23516.
    • (2009) J Biol Chem , vol.284 , pp. 23502-23516
    • Maegawa, G.H.B.1    Tropak, M.B.2    Buttner, J.D.3    Rigat, B.A.4    Fuller, M.5
  • 22
    • 43249114793 scopus 로고    scopus 로고
    • Molecular consequences of the pathogenic mutation in feline GM1 gangliosidosis
    • Martin DR, Rigat BA, Foureman P, Varadarajan GS, Hwang M, et al. (2008) Molecular consequences of the pathogenic mutation in feline GM1 gangliosidosis. Mol Genet Metab 94: 212-221.
    • (2008) Mol Genet Metab , vol.94 , pp. 212-221
    • Martin, D.R.1    Rigat, B.A.2    Foureman, P.3    Varadarajan, G.S.4    Hwang, M.5
  • 23
    • 66349117008 scopus 로고    scopus 로고
    • Sanfilippo syndrome type C: mutation spectrum in the heparan sulfate acetyl-CoA: alpha-glucosaminide N-acetyltransferase (HGSNAT) gene
    • Feldhammer M, Durand S, Mrazova L, Boucher RM, Laframboise R, et al. (2009) Sanfilippo syndrome type C: mutation spectrum in the heparan sulfate acetyl-CoA: alpha-glucosaminide N-acetyltransferase (HGSNAT) gene. Hum Mutat 30: 918-925.
    • (2009) Hum Mutat , vol.30 , pp. 918-925
    • Feldhammer, M.1    Durand, S.2    Mrazova, L.3    Boucher, R.M.4    Laframboise, R.5
  • 24
    • 0028347851 scopus 로고
    • Prenatal diagnosis of Sanfilippo disease type C using a simple fluorometric enzyme assay
    • He W, Voznyi Ya V, Huijmans JG, Geilen GC, Karpova EA, et al. (1994) Prenatal diagnosis of Sanfilippo disease type C using a simple fluorometric enzyme assay. Prenat Diagn 14: 17-22.
    • (1994) Prenat Diagn , vol.14 , pp. 17-22
    • He, W.1    Voznyi, Y.V.2    Huijmans, J.G.3    Geilen, G.C.4    Karpova, E.A.5
  • 25
    • 0037136040 scopus 로고    scopus 로고
    • Stability of the lactose permease in detergent solutions
    • Engel CK, Chen L, Prive GG, (2002) Stability of the lactose permease in detergent solutions. Biochim Biophys Acta 1564: 47-56.
    • (2002) Biochim Biophys Acta , vol.1564 , pp. 47-56
    • Engel, C.K.1    Chen, L.2    Prive, G.G.3
  • 29
    • 33847032037 scopus 로고    scopus 로고
    • High-throughput screening for novel human lysosomal beta-N-acetyl hexosaminidase inhibitors acting as pharmacological chaperones
    • Tropak MB, Blanchard J, Withers SG, Brown E, Mahuran D, (2006) High-throughput screening for novel human lysosomal beta-N-acetyl hexosaminidase inhibitors acting as pharmacological chaperones. Chem Biol 14: 153-164.
    • (2006) Chem Biol , vol.14 , pp. 153-164
    • Tropak, M.B.1    Blanchard, J.2    Withers, S.G.3    Brown, E.4    Mahuran, D.5
  • 30
    • 0018903866 scopus 로고
    • Biosynthesis of lysosomal enzymes in fibroblasts: synthesis as precursors of higher molecular weight
    • Hasilik A, Neufeld EF, (1980) Biosynthesis of lysosomal enzymes in fibroblasts: synthesis as precursors of higher molecular weight. J Biol Chem 255: 4937-4945.
    • (1980) J Biol Chem , vol.255 , pp. 4937-4945
    • Hasilik, A.1    Neufeld, E.F.2
  • 31
    • 33846374117 scopus 로고    scopus 로고
    • Catalytic mechanism of a MYST family histone acetyltransferase
    • Berndsen CE, Albaugh BN, Tan S, Denu JM, (2007) Catalytic mechanism of a MYST family histone acetyltransferase. Biochemistry 46: 623-629.
    • (2007) Biochemistry , vol.46 , pp. 623-629
    • Berndsen, C.E.1    Albaugh, B.N.2    Tan, S.3    Denu, J.M.4
  • 32
    • 34250622878 scopus 로고    scopus 로고
    • Mutational analysis of the HGSNAT gene in Italian patients with mucopolysaccharidosis IIIC (Sanfilippo C syndrome)
    • Fedele AO, Filocamo M, Di Rocco M, Sersale G, Lubke T, et al. (2007) Mutational analysis of the HGSNAT gene in Italian patients with mucopolysaccharidosis IIIC (Sanfilippo C syndrome). Hum Mutat 28: 523.
    • (2007) Hum Mutat , vol.28 , pp. 523
    • Fedele, A.O.1    Filocamo, M.2    Di Rocco, M.3    Sersale, G.4    Lubke, T.5
  • 33
    • 74549200267 scopus 로고    scopus 로고
    • Role of the signal peptide in the synthesis and processing of the glucagon-like peptide-1 receptor
    • Huang Y, Wilkinson GF, Willars GB, (2010) Role of the signal peptide in the synthesis and processing of the glucagon-like peptide-1 receptor. Brit J Pharmaco 159: 237-251.
    • (2010) Brit J Pharmaco , vol.159 , pp. 237-251
    • Huang, Y.1    Wilkinson, G.F.2    Willars, G.B.3
  • 34
    • 0026584007 scopus 로고
    • The early and late processing of lysosomal enzymes: proteolysis and compartmentation
    • Hasilik A, (1992) The early and late processing of lysosomal enzymes: proteolysis and compartmentation. Experientia 48: 130-151.
    • (1992) Experientia , vol.48 , pp. 130-151
    • Hasilik, A.1
  • 35
    • 0023929842 scopus 로고
    • Proteolytic processing of the alpha chain of the lysosomal enzyme ß-hexosaminidase, in normal human fibroblasts
    • Little LE, Lau MML, Quon DVK, Fowler AV, Neufeld EF, (1988) Proteolytic processing of the alpha chain of the lysosomal enzyme ß-hexosaminidase, in normal human fibroblasts. J Biol Chem 263: 4288-4292.
    • (1988) J Biol Chem , vol.263 , pp. 4288-4292
    • Little, L.E.1    Lau, M.M.L.2    Quon, D.V.K.3    Fowler, A.V.4    Neufeld, E.F.5
  • 36
    • 0024550289 scopus 로고
    • Proteolytic processing of the ß-subunit of the lysosomal enzyme, ß-hexosaminidase, in normal human fibroblasts
    • Quon DVK, Proia RL, Fowler AV, Bleibaum J, Neufeld EF, (1989) Proteolytic processing of the ß-subunit of the lysosomal enzyme, ß-hexosaminidase, in normal human fibroblasts. J Biol Chem 264: 3380-3384.
    • (1989) J Biol Chem , vol.264 , pp. 3380-3384
    • Quon, D.V.K.1    Proia, R.L.2    Fowler, A.V.3    Bleibaum, J.4    Neufeld, E.F.5
  • 37
    • 0025263882 scopus 로고
    • Characterization of human placental ß-hexosaminidase I2: Proteolytic processing intermediates of hexosaminidase A
    • Mahuran DJ, (1991) Characterization of human placental ß-hexosaminidase I2: Proteolytic processing intermediates of hexosaminidase A. J Biol Chem 265: 6794-6799.
    • (1991) J Biol Chem , vol.265 , pp. 6794-6799
    • Mahuran, D.J.1
  • 38
    • 33744798282 scopus 로고    scopus 로고
    • Crystallographic Structure of Human beta-Hexosaminidase A: Interpretation of Tay-Sachs Mutations and Loss of G(M2) Ganglioside Hydrolysis
    • Lemieux MJ, Mark BL, Cherney MM, Withers SG, Mahuran DJ, et al. (2006) Crystallographic Structure of Human beta-Hexosaminidase A: Interpretation of Tay-Sachs Mutations and Loss of G(M2) Ganglioside Hydrolysis. J Mol Biol 359: 913-929.
    • (2006) J Mol Biol , vol.359 , pp. 913-929
    • Lemieux, M.J.1    Mark, B.L.2    Cherney, M.M.3    Withers, S.G.4    Mahuran, D.J.5
  • 39
    • 0344837327 scopus 로고    scopus 로고
    • Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease
    • Mark BL, Mahuran DJ, Cherney MM, Zhao D, Knapp S, et al. (2003) Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease. J Mol Biol 327: 1093-1109.
    • (2003) J Mol Biol , vol.327 , pp. 1093-1109
    • Mark, B.L.1    Mahuran, D.J.2    Cherney, M.M.3    Zhao, D.4    Knapp, S.5
  • 40
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak M, (1986) Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44: 283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 41
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino JS, Traub LM, (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 72: 395-447.
    • (2003) Annu Rev Biochem , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2


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