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  • 1
    Electronic Resource
    Electronic Resource
    Low arylsulphatase A activity and choreoathetotic syndrome in three siblings: differentiation of pseudodeficiency from metachromatic leukodystrophy (1991)
    Springer
    European journal of pediatrics 150 (1991), S. 287-290 
    Details
    ISSN: 1432-1076
    Keywords: Arylsulphatase A ; Metachromatic leukodystrophy ; Arylsulphatase A pseudodeficiency
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We report on a family with a sibship of three children for whom the diagnosis of “an unusual form of metachromatic leukodystrophy (MLD)” had been suggested earlier. The patients had choreiform movements and dystomic posturing accompanied by dysarthria since childhood. The availability of the polymerase chain reaction enabled us to show that the three siblings have a pseudodeficiency genotype (ASAp/ASAp). There was no abnormal sulphatiduria, and we propose that the neurological disease and low arylsulphatase A activity are unrelated to one another in this family. A diagnosis of MLD carries very serious implications, and we recommend that gene amplification by polymerase chain reaction and hybridization with allele-specific oligonucleotide probes should be used to corroborate the diagnosis, especially when there is no abnormal sulphatiduria and when metachromatic material cannot be demonstrated in a sural nerve biopsy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01955534
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  • 2
    Electronic Resource
    Electronic Resource
    Primary cultures of rat hepatocytes synthesize fibronectin
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 90 (1979), S. 1348-1354 
    Details
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0006-291X(79)91184-7
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  • 3
    Electronic Resource
    Electronic Resource
    Structure of the Mouse Arylsulfatase A Gene and cDNA
    Amsterdam : Elsevier
    Genomics 19 (1994), S. 249-256 
    Details
    ISSN: 0888-7543
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1006/geno.1994.1055
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  • 4
    Electronic Resource
    Electronic Resource
    Sulfatide is expressed in neurons and astrocytes and accumulates at degradation deficiency (2003)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 85 (2003), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Sulfatide expression was explored in adult rat gray matter, using the Sulf I antibody and immunohistochemistry. To further explore sulfatide metabolism an arylsulfatase enzyme deficient mice model were used, resembling metachromatic leukodystrophy (MLD) characterized by lysosomal sulfatide storage. Analyses showed sulfatide staining in subpopulations of neurons and astrocytes, and in particular the neurons showed more staining in the ASA-deficient mice, indicating a higher turnover of sulfatide. These results demonstrate sulfatide expression beyond myelin and oligodendrocyte progenitors, and the intracellular localized sulfatide in neurons and astrocytes indicate other roles than in myelin. The accumulation of sulfatide in neurons might be part of the pathological process in MLD and explain known symptoms unlikely to be related to the well-established white matter disturbances.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.85.s2.22_4.x
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  • 5
    Electronic Resource
    Electronic Resource
    Biosynthesis of acid α-glucosidase in late-onset forms of glycogenosis type II (Pompe's disease)
    Amsterdam : Elsevier
    FEBS Letters 150 (1982), S. 69-76 
    Details
    ISSN: 0014-5793
    Keywords: Acid α-glucosidase ; Glycogenosis type II ; Lysosomal enzyme synthesis ; Lysosomal α-glucosidase ; Pompe's disease
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(82)81306-9
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  • 6
    Electronic Resource
    Electronic Resource
    Advances in the molecular genetics of metachromatic leukodystrophy (1990)
    Springer
    Journal of inherited metabolic disease 13 (1990), S. 560-571 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Metachromatic leukodystrophy is a lysosomal storage disorder caused by the deficiency of arylsulphatase A (EC 3.1.6.1). This results in the intralysosomal storage of cerebroside sulphate, which leads to a progressive demyelination of the nervous system. The patients usually die within a few years from the onset of symptoms. Clinically, there are different forms of the disease and the molecular basis for this heterogeneity is unknown. The gene for arylsulphatase A has recently been cloned and provides a necessary tool for the exact description of the molecular defects occurring in the different forms of metachromatic leukodystrophy. Metachromatic leukodystrophy can also be caused by the deficiency of an arylsulphatase A activator protein (sphingolipid activator protein B). The cDNA for the precursor of this protein has been isolated and a mutant cDNA of one patient has been analysed. A substantial arylsulphatase A deficiency can also occur in healthy individuals, a phenotype termed pseudodeficiency. Two concurrent mutations have been identified in this low arylsulphatase A activity allele. This permitted the development of a rapid assay which allows the detection of the pseudodeficiency allele. Bone marrow transplantation has been tried in several metachromatic leukodystrophy patients and there is evidence that this treatment might slow or even halt the progression of the disease. A final conclusion as to whether bone marrow transplantation is a suitable therapy for metachromatic leukodystrophy cannot be drawn yet.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01799513
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  • 7
    Electronic Resource
    Electronic Resource
    Molecular genetics of metachromatic leukodystrophy (1994)
    Springer
    Journal of inherited metabolic disease 17 (1994), S. 500-509 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Metachromatic leukodystrophy is a lysosomal storage disorder caused by the deficiency of arylsulphatase A. The disease is characterized by a progressive demyelination that causes a variety of neurological symptoms. Patients die within a few years after the age of onset. Clinically the disease is heterogeneous and according to the age of onset three different forms can be distinguished. The gene of arylsulphatase A has been cloned and several mutations causing metachromatic leukodystrophy have been characterized. The distribution of these alleles among patients with different clinical forms of the disease has revealed a genotype-phenotype correlation. A major determinant of the clinical phenotype is the residual enzyme activity that it associated with a particular genotype. Homozygosity for alleles that do not allow the synthesis of arylsulphatase A polypeptides causes the most severe form of disease, whereas homozygosity for alleles that encode arylsulphatase A with low residual enzyme activity is found in the mild late-onset forms of disease. A substantial arylsulphatase A deficiency can also be found in healthy individuals at high frequency. This phenomenon has been termed pseudodeficiency. It is often difficult to distinguish whether an arylsulphatase A deficiency is due to metachromatic leukodystrophy or harmless pseudodeficiency. The characterization of the mutations causing pseudodeficiency has allowed the detection of the pseudodeficiency allele in the DNA of probands and has thus improved the diagnosis and genetic counselling for metachromatic leukodystrophy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00711364
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  • 8
    Electronic Resource
    Electronic Resource
    Localization of receptors for endocytosis of lysosomal enzymes on different brain cells (1998)
    Springer
    Journal of inherited metabolic disease 21 (1998), S. 313-317 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005305213832
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  • 9
    Electronic Resource
    Electronic Resource
    Metachromatic leukodystrophy: Molecular genetics and an animal model (1998)
    Springer
    Journal of inherited metabolic disease 21 (1998), S. 564-574 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Metachromatic leukodystrophy (MLD) is a lysosomal storage disorder caused by the deficiency of arylsulphatase A (ASA; EC 3.1.6.8). Deficiency of this enzyme causes intralysosomal storage of the sphingolipid cerebroside sulphate. This lipid is abundant in myelin and it may thus not be surprising that storage mainly affects oligodendrocytes. Patients suffer from a progressive demyelination causing various neurological symptoms. The disease is fatal and treatment is not available. The human ASA gene has been cloned and more than 40 mutations have been analysed that cause metachromatic leukodystrophy. Few of these alleles are frequent among patients, whereas most mutant alleles have only been found in single families. Since MLD has only been described in humans and no naturally occurring animal model has been described, ASA-deficient mice have been generated by homologous recombination. The ASA knockout mice are unable to degrade sulphatide and store the lipid intralysosomally. The pattern of lipid storage in neuronal and nonneuronal tissues resembles that described for patients. In the nervous system, lipid storage is found in oligodendrocytes, astrocytes and some neurons. Animals display an astrogliosis and a decreased average axonal diameter. Purkinje cells and Bergmann glia of the cerebellum are morphologically aberrant. Demyelination is seen in the acoustic ganglion and occurs between the ages of 6 and 12 months. The animals are deaf at this age and display various neuromotor abnormalities. However, compared to humans the mice have a surprisingly mild phenotype, since they have a normal life span and do not develop widespread demyelination. ASA-deficient mice have been transplanted with bone marrow, which was transduced with a retroviral vector expressing arylsulphatase A. The majority of transplanted animals display sustained expression of arylsulphatase A from the retroviral construct up to 5 months after transplantation. However, preliminary data suggest that this therapeutic approach does not reduce storage material.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005471106088
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  • 10
    Electronic Resource
    Electronic Resource
    Immunological characterization of human acid phosphatase gene products (1985)
    Springer
    Biochemical genetics 23 (1985), S. 309-319 
    Details
    ISSN: 1573-4927
    Keywords: human acid phosphatases ; isozymes ; tartrate inhibition ; human tissues ; antiphosphatase monospecific antibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The immunological cross-reactivity of heterogeneous acid phosphatase isozymes from different human tissues has been studied using monospecific antisera prepared against four homogeneous acid phosphatases. The enzyme characterized as tartrate-inhibitable, prostatic acid phosphatase is also found to be present in leukocytes, kidney, spleen, and placenta. The tartrate-inhibitable (liver) lysosomal enzyme is also found in kidney, fibroblasts, brain, placenta, and spleen, but it is not detectable in erythrocytes and prostate. In several tissues, 10–20% of the tartrate-inhibitable enzyme is not precipitated by any of the antisera used; an exceptionally high amount (54%) of such an enzyme is present in human brain. Antiserum against a low molecular weight tartrate-resistant liver enzyme (14 kDa) does not cross-react with the erythrocyte enzyme. (10–20 kDa). All other tissues except placenta, prostate, and fibroblast cells show a cross-reactivity with the 14-kDa acid phosphatase antiserum. Thus, the low molecular weight human liver acid phosphatase is distinct from the erythrocyte enzyme, and there are also at least three different tartrate-inhibitable acid phosphatases in human tissues. Chromosomal assignments have been made for only two of the (at least) five acid phosphatases that are present in adult human tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504327
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