Molecular and biochemical characterisation of a novel sulphatase gene: Arylsulfatase G (ARSG) View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2002-12

AUTHORS

Paola Ferrante, Silvia Messali, Germana Meroni, Andrea Ballabio

ABSTRACT

Molecular analysis has provided important insights into the biochemistry and genetics of the sulphatase family of enzymes. Through bioinformatic searches of the EST database, we have identified a novel gene consisting of 11 exons and encoding a 525 aa protein that shares a high degree of sequence similarity with all sulphatases and in particular with arylsulphatases, hence the tentative name Arylsulfatase G (ARSG). The highest homology is shared with Arylsulfatase A, a lysosomal sulphatase which is mutated in metachromatic leukodistrophy, particularly in the amino-terminal region. The 10 amino acids that form the catalytic site are strongly conserved. The murine homologue of Arylsulfatase G gene product shows 87% identity with the human protein. To test the function of this novel gene we transfected the full-length cDNA in Cos7 cells, and detected an Arylsulfatase G precursor protein of 62 kDa. After glycosylation the precursor is maturated in a 70 kDa form, which localises to the endoplasmic reticulum. Northern blot analysis of Arylsulfatase G revealed a ubiquitous expression pattern. We tested the sulphatase activity towards two different artificial substrates 4-methylumbelliferyl (4-MU) sulphate and p-nitrocatechol sulphate, but no arylsulphatase activity was detectable. Further studies are needed to characterise the function of Arylsulfatase G, possibly revealing a novel metabolic pathway. More... »

PAGES

5200887

References to SciGraph publications

  • 1988-12. Metabolism of3H-dehydroepiandrosterone sulphate by subjects with steroid sulphatase deficiency in JOURNAL OF INHERITED METABOLIC DISEASE
  • 1970. Enzymological Aspects of Steroid Conjugation in CHEMICAL AND BIOLOGICAL ASPECTS OF STEROID CONJUGATION
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    http://scigraph.springernature.com/pub.10.1038/sj.ejhg.5200887

    DOI

    http://dx.doi.org/10.1038/sj.ejhg.5200887

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/12461688


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