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ARSB  -  arylsulfatase B

Homo sapiens

Synonyms: ASB, Arylsulfatase B, G4S, MPS6, N-acetylgalactosamine-4-sulfatase
 
 
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Disease relevance of ARSB

 

High impact information on ARSB

 

Chemical compound and disease context of ARSB

 

Biological context of ARSB

 

Anatomical context of ARSB

 

Associations of ARSB with chemical compounds

 

Other interactions of ARSB

  • Sequence analysis of two mouse clones showed high degrees of homology with the human ARSA and ARSB sequences, respectively, and likely represent the murine homologues of these enzymes [24].
  • The same pattern was observed in RNA from fibroblasts of three Maroteaux-Lamy patients who were deficient in ASB activity, as well as in RNA from fibroblasts of three patients with multiple sulfatase deficiency, in which all known sulfatases were markedly diminished [18].
  • To identify the molecular defect in a patient with the intermediate form of the disease, arylsulfatase B mRNA from his fibroblasts was reverse-transcribed, amplified by the polymerase chain reaction, and subcloned [11].
  • The reaction was made specific for arylsulfatase A by inhibiting arylsulfatase C activity with low pH and arylsulfatase B activity with pyrophosphate [25].
  • The presence of the extra cysteine residue at position 451 in the feline enzyme may explain why feline ARSB is a homodimer and the human enzyme is a monomer [26].
 

Analytical, diagnostic and therapeutic context of ARSB

  • Each individual exon of the ARSB gene was amplified by PCR and subsequently sequenced [2].
  • MPS VI has been described in man, cats and rats, and several mutations in the ASB gene have been identified in human patients and the animal models [27].
  • The purified arylsulfatase B migrated as a single polypeptide of 58 kDa on non-reducing SDS-PAGE, indicating that the three chains are linked by disulfide bonds [28].
  • To facilitate comparative structure/function studies of the human and feline enzymes and to initiate somatic gene therapy trials in the MPS VI cats, a full-length feline ARSB cDNA was reconstructed from a 1440-bp partial cDNA and an ARSB fragment amplified from feline first-strand cDNA by the polymerase chain reaction [26].
  • Arylsulfatase B was separated from arylsulfatase A in extracts of human lung tissue by anion exchange chromatography and further purified by gel filtration and cation exchange chromatography [5].

References

  1. Mucopolysaccharidosis type VI: Structural and clinical implications of mutations in N-acetylgalactosamine-4-sulfatase. Litjens, T., Hopwood, J.J. Hum. Mutat. (2001) [Pubmed]
  2. Mutational analysis of mucopolysaccharidosis type VI patients undergoing a trial of enzyme replacement therapy. Karageorgos, L., Harmatz, P., Simon, J., Pollard, A., Clements, P.R., Brooks, D.A., Hopwood, J.J. Hum. Mutat. (2004) [Pubmed]
  3. Mucopolysaccharidosis type VI: identification of three mutations in the arylsulfatase B gene of patients with the severe and mild phenotypes provides molecular evidence for genetic heterogeneity. Jin, W.D., Jackson, C.E., Desnick, R.J., Schuchman, E.H. Am. J. Hum. Genet. (1992) [Pubmed]
  4. Structure of the human arylsulfatase B gene. Modaressi, S., Rupp, K., von Figura, K., Peters, C. Biol. Chem. Hoppe-Seyler (1993) [Pubmed]
  5. Arylsulfatase B of human lung. Isolation, characterization, and interaction with slow-reacting substance of anaphylaxis. Wasserman, S.I., Austen, K.F. J. Clin. Invest. (1976) [Pubmed]
  6. Bone-marrow transplantation in the Maroteaux-Lamy syndrome (mucopolysaccharidosis type VI). Biochemical and clinical status 24 months after transplantation. Krivit, W., Pierpont, M.E., Ayaz, K., Tsai, M., Ramsay, N.K., Kersey, J.H., Weisdorf, S., Sibley, R., Snover, D., McGovern, M.M. N. Engl. J. Med. (1984) [Pubmed]
  7. Two mutations within a feline mucopolysaccharidosis type VI colony cause three different clinical phenotypes. Crawley, A.C., Yogalingam, G., Muller, V.J., Hopwood, J.J. J. Clin. Invest. (1998) [Pubmed]
  8. Enzyme replacement therapy from birth in a feline model of mucopolysaccharidosis type VI. Crawley, A.C., Niedzielski, K.H., Isaac, E.L., Davey, R.C., Byers, S., Hopwood, J.J. J. Clin. Invest. (1997) [Pubmed]
  9. Arylsulfatase B activities and glycosaminoglycan levels in retrovirally transduced mucopolysaccharidosis type VI cells. Prospects for gene therapy. Fillat, C., Simonaro, C.M., Yeyati, P.L., Abkowitz, J.L., Haskins, M.E., Schuchman, E.H. J. Clin. Invest. (1996) [Pubmed]
  10. Identification, expression, and biochemical characterization of N-acetylgalactosamine-4-sulfatase mutations and relationship with clinical phenotype in MPS-VI patients. Litjens, T., Brooks, D.A., Peters, C., Gibson, G.J., Hopwood, J.J. Am. J. Hum. Genet. (1996) [Pubmed]
  11. Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). An intermediate clinical phenotype caused by substitution of valine for glycine at position 137 of arylsulfatase B. Wicker, G., Prill, V., Brooks, D., Gibson, G., Hopwood, J., von Figura, K., Peters, C. J. Biol. Chem. (1991) [Pubmed]
  12. Measurements from normal umbilical cord blood of four lysosomal enzymatic activities: alpha-L-iduronidase (Hurler), galactocerebrosidase (globoid cell leukodystrophy), arylsulfatase A (metachromatic leukodystrophy), arylsulfatase B (Maroteaux-Lamy). deGasperi, R., Raghavan, S.S., Sosa, M.G., Kolodny, E.H., Carrier, C., Rubenstein, P., Peters, C., Wagner, J., Kurtzberg, J., Krivit, W. Bone Marrow Transplant. (2000) [Pubmed]
  13. Synthesis of pyrene derivatives of cerebroside sulfate and their use for determining arylsulfatase A activity. Marchesini, S., Viani, P., Cestaro, B., Gatt, S. Biochim. Biophys. Acta (1989) [Pubmed]
  14. Isolation of human eosinophil phospholipase D. Kater, L.A., Goetzl, E.J., Austen, K.F. J. Clin. Invest. (1976) [Pubmed]
  15. Regional localization of alpha-galactosidase (GLA) to Xpter----q22, hexosaminidase B (HEXB) to 5q13----qter, and arylsulfatase B (ARSB) to 5pter----q13. Fox, M.F., DuToit, D.L., Warnich, L., Retief, A.E. Cytogenet. Cell Genet. (1984) [Pubmed]
  16. Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome): six unique arylsulfatase B gene alleles causing variable disease phenotypes. Isbrandt, D., Arlt, G., Brooks, D.A., Hopwood, J.J., von Figura, K., Peters, C. Am. J. Hum. Genet. (1994) [Pubmed]
  17. Three-dimensional structures of sulfatases. Ghosh, D. Meth. Enzymol. (2005) [Pubmed]
  18. Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B. Peters, C., Schmidt, B., Rommerskirch, W., Rupp, K., Zühlsdorf, M., Vingron, M., Meyer, H.E., Pohlmann, R., von Figura, K. J. Biol. Chem. (1990) [Pubmed]
  19. Properties of sulfatases in cultured skin fibroblasts of multiple sulfatase deficient patients. Yutaka, T., Okada, S., Kato, T., Inui, K., Yabuuchi, H. Clin. Genet. (1981) [Pubmed]
  20. Clinical and biochemical study of 28 patients with mucopolysaccharidosis type VI. Azevedo, A.C., Schwartz, I.V., Kalakun, L., Brustolin, S., Burin, M.G., Beheregaray, A.P., Leistner, S., Giugliani, C., Rosa, M., Barrios, P., Marinho, D., Esteves, P., Valadares, E., Boy, R., Horovitz, D., Mabe, P., da Silva, L.C., de Souza, I.C., Ribeiro, M., Martins, A.M., Palhares, D., Kim, C.A., Giugliani, R. Clin. Genet. (2004) [Pubmed]
  21. Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum. Dierks, T., Lecca, M.R., Schmidt, B., von Figura, K. FEBS Lett. (1998) [Pubmed]
  22. Amino acid residues forming the active site of arylsulfatase A. Role in catalytic activity and substrate binding. Waldow, A., Schmidt, B., Dierks, T., von Bülow, R., von Figura, K. J. Biol. Chem. (1999) [Pubmed]
  23. Structure of a human lysosomal sulfatase. Bond, C.S., Clements, P.R., Ashby, S.J., Collyer, C.A., Harrop, S.J., Hopwood, J.J., Guss, J.M. Structure (1997) [Pubmed]
  24. The sulfatase gene family: cross-species PCR cloning using the MOPAC technique. Grompe, M., Pieretti, M., Caskey, C.T., Ballabio, A. Genomics (1992) [Pubmed]
  25. A specific ultrastructural stain for arylsulfatase A activity in human cultured fibroblasts. Chang, P.L., Moudgil, G. J. Histochem. Cytochem. (1984) [Pubmed]
  26. Feline arylsulfatase B (ARSB): isolation and expression of the cDNA, comparison with human ARSB, and gene localization to feline chromosome A1. Jackson, C.E., Yuhki, N., Desnick, R.J., Haskins, M.E., O'Brien, S.J., Schuchman, E.H. Genomics (1992) [Pubmed]
  27. N-acetylgalactosamine-4-sulfatase: identification of four new mutations within the conserved sulfatase region causing mucopolysaccharidosis type VI. Simonaro, C.M., Schuchman, E.H. Biochim. Biophys. Acta (1995) [Pubmed]
  28. Components and proteolytic processing sites of arylsulfatase B from human placenta. Kobayashi, T., Honke, K., Jin, T., Gasa, S., Miyazaki, T., Makita, A. Biochim. Biophys. Acta (1992) [Pubmed]
 
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