Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B.

Peters, C; Schmidt, Bernhard; Rommerskirch, W; Rupp, Katharina; Zühlsdorf, M; Vingron, Martin; Meyer, H. E.; Pohlmann, R; Figura, Kurt Von

doi:10.1016/s0021-9258(19)39778-9

Cited by 119 publications

(11 citation statements)

References 36 publications

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“…On longer exposure, the endogenous transcripts of the ASB gene, 4.8, 2.5 and 1.8 kb in size (see Fig. 3 of Peters et al, 1990), are visible in the RNA of uninfected 5343 fibroblasts (results not shown).…”

Section: Resultsmentioning

confidence: 94%

“…4, lane 6). NH4Cl is known to induce secretion of precursors of lysosomal enzymes (Hasilik & Neufeld, -1980;Myerowitz & Neufeld, 1981) including those of ASB Peters et al, 1990;Taylor et al, 1990). During a 16 h chase the 64 kDa precursor disappeared and a 47 kDa and a 12.5 kDa polypeptide accumulated in the cell extract (Fig.…”

Section: Resultsmentioning

confidence: 97%

“…A retroviral vector, XT-ASB (Fig. 1 [preceded by a DNA fragment encoding the first 29 amino acids of the signal peptide of lysosomal acid phosphatase (Peters et al, 1990)] into the retroviral expression vector pXT I (Boulter & Wagner, 1987). The details of construction are given in the Materials and methods section.…”

Section: Resultsmentioning

confidence: 99%

“…Production of recombinant retrovirus XT-ASB The 1903 bp XhoI-Sall DNA fragment of plasmid pCA7 encoding the first 29 amino acids of the signal peptide of lysosomal acid phosphatase and amino acids 37-533 of ASB (Peters et al, 1990) was ligated into the XhoI site of the retroviral expression vector pXTl (Boulter & Wagner, 1987). The orientation of the insert in the resulting plasmid pXT-ASB was checked by digestion with the restriction enzymes SstI and XhoI + Sall; plasmid pXT-ASB was amplified in Escherichia coli strain HB1O1 in the presence of ampicillin (200 jug/ml).…”

Section: Cell Lines and Vectorsmentioning

confidence: 99%

“…MPS VI appears to be an appropriate model for gene therapy approaches of lysosomal storage diseases, since ASB cDNAs have been isolated recently (Peters et al, 1990;Schuchman et al, 1990). Furthermore, a feline model of the disease has been described (Jezyk et al, 1977), and a successful allogenic bonemarrow transplantation in an affected cat resulting in encouraging improvements of the symptoms has been reported (Gasper et al, 1984).…”

Section: Introductionmentioning

confidence: 99%

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Restoration of arylsulphatase B activity in human mucopolysaccharidosis-type-VI fibroblasts by retroviral-vector-mediated gene transfer

Peters

Rommerskirch

Modaressi

et al. 1991

Biochemical Journal

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The Maroteaux-Lamy syndrome (mucopolysaccharidosis type VI; MPS VI) is a lysosomal storage disease caused by deficiency of the enzyme arylsulphatase B (ASB). A human ASB cDNA has been subcloned into the retroviral vector pXT1 containing the bacterial neomycin-resistance gene and an internal thymidine kinase promoter for transcription of the inserted gene. Replication defective retrovirus was generated by transfecting the construct into the amphotropic packaging cell line PA317. Human MPS VI fibroblasts infected with recombinant retrovirus integrated the provirus into their genome and expressed retrovirus-encoded ASB mRNAs. In infected fibroblasts the level of ASB was up to 36-fold higher than in normal fibroblasts. Biosynthesis and processing of ASB in infected MPS VI fibroblasts was accomplished as in normal fibroblasts, and mature, enzymically active, ASB accumulated in dense lysosomes, indicating that the ASB deficiency in MPS VI fibroblasts was corrected by the retroviral gene transfer.

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Section: Resultsmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 99%

Section: Cell Lines and Vectorsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Restoration of arylsulphatase B activity in human mucopolysaccharidosis-type-VI fibroblasts by retroviral-vector-mediated gene transfer

Peters

Rommerskirch

Modaressi

et al. 1991

Biochemical Journal

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Arylsulfatase exists as non-enzymatic cell surface protein in sea urchin embryos

et al. 1998

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The physiological role of arylsulfatase (Ars) and its function during development have yet to be satisfactorily defined in any species, though the proteins are widely distributed and the genes have been cloned from various organisms. Here we report the dual location of two types of Ars in sea urchin embryos. The majority of sea urchin Ars does not exhibit enzyme activity and is extracellularly distributed in aboral ectoderm cells (nonenzymatic Ars). Only a small portion has enzyme activity and is localized in lysosomal vesicles (enzymatic Ars). The elution pattern of Ars proteins processed by DEAE‐cellulose or analytical gel‐column chromatography reveals that although the molecular radius of enzymatic Ars differs from that of nonenzymatic Ars, they have the same charge. Furthermore, sedimentation analysis shows that purified Ars of sea urchin embryos is soluble in the absence of divalent cations but becomes insoluble in the presence of Ca2+ or Mg2+. Taken together, the present results suggest that nonenzymatic Ars is a new member of the cell surface component or extracellular matrix. It is possible that this cell surface Ars plays an important role in morphogenesis of sea urchin embryos. J. Exp. Zool. 280:220–230, 1998. © 1998 Wiley‐Liss, Inc.

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Two novel frameshift mutations causing premature stop codons in a patient with the severe form of Maroteaux-Lamy syndrome

Isbrandt¹,

Hopwood²,

Figura³

et al. 1996

Hum. Mutat.

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Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B.

Cited by 119 publications

References 36 publications

Restoration of arylsulphatase B activity in human mucopolysaccharidosis-type-VI fibroblasts by retroviral-vector-mediated gene transfer

Restoration of arylsulphatase B activity in human mucopolysaccharidosis-type-VI fibroblasts by retroviral-vector-mediated gene transfer

Arylsulfatase exists as non-enzymatic cell surface protein in sea urchin embryos

Two novel frameshift mutations causing premature stop codons in a patient with the severe form of Maroteaux-Lamy syndrome

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