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Decreasing Activity and Altered Protein Processing of Human Iduronate-2-sulfatase Mutations Demonstrated by Expression in COS7 Cells

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References

  • Arnold K, Bordoli L, Kopp J, Schwede T (2006) The Swiss-model workspace: a web-based environment for protein structure homology modeling. Bioinformatics 22:195–201

    Article  PubMed  CAS  Google Scholar 

  • Bach G, Eisenberg F Jr, Cantz M, Neufeld EF (1973) The defect in the Hunter syndrome: deficiency of sulfoiduronate sulfatase. Proc Natl Acad Sci USA 70:2134–2138

    Article  PubMed  CAS  Google Scholar 

  • Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM (1997) Structure of a human lysosomal sulfatase. Structure 5:277–289

    Article  PubMed  CAS  Google Scholar 

  • Flomen RH, Green EP, Green PM, Bentley DR, Giannelli F (1993) Determination of the organisation of coding sequences within the iduronate sulphate sulphatase (IDS) gene. Hum Mol Genet 2:5–10

    Article  PubMed  CAS  Google Scholar 

  • Froissart R, Millat G, Mathieu M, Bozon D, Maire I (1995) Processing of iduronate 2-sulphatase in human fibroblasts. Biochem J 309(Pt 2):425–430

    PubMed  CAS  Google Scholar 

  • Froissart R, Da Silva IM, Maire I (2007) Mucopolysaccharidosis type II: an update on mutation spectrum. Acta Paediatr Suppl 96:71–77

    Article  PubMed  Google Scholar 

  • Ghosh D (2007) Human sulfatases: a structural perspective to catalysis. Cell Mol Life Sci 64:2013–2022

    Article  PubMed  CAS  Google Scholar 

  • Goldenfum SL, Young E, Michelakakis H, Tsagarakis S, Winchester B (1996) Mutation analysis in 20 patients with Hunter disease. Hum Mutat 7:76–78

    Article  PubMed  CAS  Google Scholar 

  • Guex N, Peitsch MC (1997) Swiss-Model and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714–2723

    Article  PubMed  CAS  Google Scholar 

  • Hernandez-Guzman FG, Higashiyama T, Osawa Y, Ghosh D (2001) Purification, characterization and crystallization of human placental estrone/dehydroepiandrosterone sulfatase, a membrane-bound enzyme of the endoplasmic reticulum. J Steroid Biochem Mol Biol 78:441–450

    Article  PubMed  CAS  Google Scholar 

  • Hernandez-Guzman FG, Higashiyama T, Pangborn W, Osawa Y, Ghosh D (2003) Structure of human estrone sulfatase suggests functional roles of membrane association. J Biol Chem 278:22989–22997

    Article  PubMed  CAS  Google Scholar 

  • Kato T, Kato Z, Kuratsubo I, Tanaka N, Ishigami T, Kajihara J, Sukegawa-Hayasaka K, Orii K, Isogai K, Fukao T, Shimozawa N, Orii T, Kondo N, Suzuki Y (2005) Mutational and structural analysis of Japanese patients with mucopolysaccharidosis type II. J Hum Genet 50:395–402

    Article  PubMed  CAS  Google Scholar 

  • Keeratichamroen S, Cairns JR, Wattanasirichaigoon D, Wasant P, Ngiwsara L, Suwannarat P, Pangkanon S, Kuptanon J, Tanpaiboon P, Rujirawat T, Liammongkolkul S, Svasti J (2008) Molecular analysis of the iduronate-2-sulfatase gene in Thai patients with Hunter syndrome. J Inherit Metab Dis 31(Suppl 2):S303–S311

    Article  PubMed  Google Scholar 

  • Kim CH, Hwang HZ, Song SM, Paik KH, Kwon EK, Moon KB, Yoon JH, Han CK, Jin DK (2003) Mutational spectrum of the iduronate 2 sulfatase gene in 25 unrelated Korean Hunter syndrome patients: identification of 13 novel mutations. Hum Mutat 21:449–450

    Article  PubMed  CAS  Google Scholar 

  • Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W (1998) Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. Biochemistry 37:3654–3664

    Article  PubMed  CAS  Google Scholar 

  • Millat G, Froissart R, Maire I, Bozon D (1997a) Characterization of iduronate sulphatase mutants affecting N-glycosylation sites and the cysteine-84 residue. Biochem J 326(1):243–247

    PubMed  CAS  Google Scholar 

  • Millat G, Froissart R, Maire I, Bozon D (1997b) IDS transfer from overexpressing cells to IDS-deficient cells. Exp Cell Res 230:362–367

    Article  PubMed  CAS  Google Scholar 

  • Neufeld EF, Muenzer J (2001) The mucopolysaccharidoses. In: Scriver CR, Beaudet AL, Sly WS, Valle D (eds) The metabolic and molecular bases of inherited disease, 8th edn. McGraw-Hill, New York, pp 3421–3452

    Google Scholar 

  • Parkinson-Lawrence E, Turner C, Hopwood J, Brooks D (2005) Analysis of normal and mutant iduronate-2-sulphatase conformation. Biochem J 386:395–400

    Article  PubMed  CAS  Google Scholar 

  • Rathmann M, Bunge S, Steglich C, Schwinger E, Gal A (1995) Evidence for an iduronate-sulfatase pseudogene near the functional Hunter syndrome gene in Xq27.3-q28. Hum Genet 95:34–38

    Article  PubMed  CAS  Google Scholar 

  • Roeser D, Preusser-Kunze A, Schmidt B, Gasow K, Wittmann JG, Dierks T, von Figura K, Rudolph MG (2006) A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. Proc Natl Acad Sci USA 103:81–86

    Article  PubMed  CAS  Google Scholar 

  • Schmidt B, Selmer T, Ingendoh A, von Figura K (1995) A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell 82:271–278

    Article  PubMed  CAS  Google Scholar 

  • Schwede T, Kopp J, Guex N, Peitsch MC (2003) Swiss-model: an automated protein homology-modeling server. Nucl Acids Res 31:3381–3385

    Article  PubMed  CAS  Google Scholar 

  • Stenson PD, Mort M, Ball EV, Howells K, Phillips AD, Thomas NS, Cooper DN (2009) The human gene mutation database: 2008 update. Genome Med 1:13

    Article  PubMed  Google Scholar 

  • Sukegawa-Hayasaka K, Kato Z, Nakamura H, Tomatsu S, Fukao T, Kuwata K, Orii T, Kondo N (2006) Effect of Hunter disease (mucopolysaccharidosis type II) mutations on molecular phenotypes of iduronate-2-sulfatase: enzymatic activity, protein processing and structural analysis. J Inherit Metab Dis 29:755–761

    Article  PubMed  CAS  Google Scholar 

  • Villani GR, Daniele A, Balzano N, Di Natale P (2000) Expression of five iduronate-2-sulfatase site-directed mutations. Biochim Biophys Acta 1501:71–80

    Article  PubMed  CAS  Google Scholar 

  • Voznyi YV, Keulemans JL, van Diggelen OP (2001) A fluorimetric enzyme assay for the diagnosis of MPS II (Hunter disease). J Inherit Metab Dis 24:675–680

    Article  PubMed  CAS  Google Scholar 

  • Whitley CB, Anderson RA, Aronovich EL, Crotty PL, Anyane-Yeboa K, Russo D, Warburton D (1993) Caveat to genotype-phenotype correlation in mucopolysaccharidosis type II: discordant clinical severity of R468W and R468Q mutations of the iduronate-2-sulfatase gene. Hum Mutat 2:235–237

    Article  PubMed  CAS  Google Scholar 

  • Wilson PJ, Meaney CA, Hopwood JJ, Morris CP (1993) Sequence of the human iduronate 2-sulfatase (IDS) gene. Genomics 17:773–775

    Article  PubMed  CAS  Google Scholar 

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Acknowledgments

The authors are grateful to the families of the patients for their assistance in this investigation and to the Chulabhorn Research Institute and Chulabhorn Graduate Institute for financial support. This work was also partly supported by grants from Mahidol University to DW. DW is a recipient of the Research Career Development Award, Faculty of Medicine, Ramathibodi Hospital, Mahidol University.

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Authors and Affiliations

  1. Laboratory of Biochemistry, Chulabhorn Research Institute, Bangkok, 10210, Thailand

    Ratana Charoenwattanasatien, James R. Ketudat Cairns, Siriporn Keeratichamroen, Phannee Sawangareetrakul, Jisnuson Svasti & Voraratt Champattanachai

  2. Applied Biological Sciences, Chulabhorn Graduate Institute, Bangkok, 10210, Thailand

    Ratana Charoenwattanasatien & Jisnuson Svasti

  3. School of Biochemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand

    James R. Ketudat Cairns

  4. Division of Genetics and Metabolism, Children’s National Medical Center, Washington, DC, 20010, USA

    Pranoot Tanpaiboon

  5. Department of Pediatrics, Ramathibodi Hospital, Bangkok, 10400, Thailand

    Duangrurdee Wattanasirichaigoon

  6. Queen Sirikit National Institute of Child Health, Bangkok, 10400, Thailand

    Suthipong Pangkanon

  7. Department of Biochemistry and Center of Excellence in Protein Structure and Function, Faculty of Science, Mahidol University, Bangkok, 10400, Thailand

    Jisnuson Svasti

Authors
  1. Ratana Charoenwattanasatien
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  8. Jisnuson Svasti
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  9. Voraratt Champattanachai
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Correspondence to Voraratt Champattanachai.

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Charoenwattanasatien, R., Cairns, J.R.K., Keeratichamroen, S. et al. Decreasing Activity and Altered Protein Processing of Human Iduronate-2-sulfatase Mutations Demonstrated by Expression in COS7 Cells. Biochem Genet 50, 990–997 (2012). https://doi.org/10.1007/s10528-012-9538-9

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  • DOI: https://doi.org/10.1007/s10528-012-9538-9

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