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  • 1
    Electronic Resource
    Electronic Resource
    Lysosulfatide (Sulfogalactosylsphingosine) Accumulation in Tissues from Patients with Metachromatic Leukodystrophy (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 55 (1990), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: We describe here a sensitive assay method for lysosulfatide (sulfogalactosylsphingosine) in human tissues using HPLC. The method involves extraction of lipids, saponification, isolation using a C18 Sep-Pak column, derivatization with o-phthalaldehyde, and detection of the fluorescent lysosulfatide using HPLC. In control subjects, a small amount of lysosulfatide was detected in the cerebral white matter (9–35 pmol/mg of protein), spinal cord (35 pmol/mg of protein), sciatic nerve (14 pmol/mg of protein), and kidney (∼2 pmol/ mg of protein) but not in the cerebral gray matter and liver. A marked accumulation of the lipid was noted in tissues from six patients with metachromatic leukodystrophy (MLD). The concentration of lysosulfatide was high in the cerebral white matter, spinal cord, and sciatic nerve (223–1,172 pmol/mg of protein). Even in the cerebral gray matter, kidney, and liver, where lysosulfatide was hardly detected in the control sample, a considerable amount (3–45 pmol/mg of protein) accumulated in MLD patients. The concentration and distribution pattern of lysosulfatide were similar to those of galactosylsphingosine (psychosine) accumulated in patients with Krabbe disease. Therefore, the accumulation of lysosulfatide may explain the demyelination in patients with MLD, as is the case with Krabbe disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1990.tb04942.x
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  • 2
    Electronic Resource
    Electronic Resource
    Mutation in GM2-Gangliosidosis B1 Variant (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 50 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Fibroblasts from a patient with GM2-gangliosidosis B1 variant contained mRNA of normal size but in reduced quantity for the β-hexosaminidase α subunit. The nucleotide sequence of a cDNA clone that included the entire protein coding sequence was completely normal except for a sinde base substitution from G to A at no. 533, resulting in a change from arginine to histidine at amino acid no. 178. The same mutation was found in two other cDNA clones. The position of the mutation is ∼90 amino acids from the N-terminus of the mature, processed enzyme. Computer analysis predicated substantial alterations in the secondary structure of the enzyme protein. These results provide new insight into functional domains of this enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb13266.x
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  • 3
    Electronic Resource
    Electronic Resource
    Accumulation of Lysosphingolipids in Tissues from Patients with GM1 and GM2 Gangliosidoses (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 59 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: By using a sensitive method, we assayed lysocom-pounds of gangliosides and asialogangliosides in tissues from four patients with GM2 gangliosidosis (one with Sand-hoff disease and three with Tay-Sachs disease) and from three patients with GM1 gangliosidosis [one with infantile type (fetus), one with late-infantile, and one with adult type]. In the brain and spinal cord of all the patients except for an adult GM 1 gangliosidosis patient, abnormal accumulation of the lipids was observed, though the concentration in the fetal tissue was low. In GM2 gangliosidosis, the amounts of lyso GM2 ganglioside accumulated in the brain were similar among the patient with Sandhoff disease and the patients with Tay-Sachs disease, whereas the concentration of asialo lyso GM2 ganglioside in the brain was higher in the former patient than in the latter patients. By comparing the sphingoid bases of neutral sphingolipids, gangliosides, and lysosphingolipids, it was suggested that lysosphingolipids in the diseased tissue are synthesized by sequential glycosylation from free sphingoid bases, but not by deacyla-tion of the sphingolipids. Because lysosphingolipids are known to be cytotoxic, the abnormally accumulated lysosphingolipids may well be the pathogenetic agent for the neuronal degeneration in gangliosidoses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb08460.x
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  • 4
    Electronic Resource
    Electronic Resource
    A Point Mutation in the Coding Sequence of the β-Hexosaminidase α Gene Results in Defective Processing of the Enzyme Protein in an Unusual GM2-Gangliosidosis Variant (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 51 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: cDNA clones were isolated from cultured fibro-blasts of a patient previously reported as having GM2-gangliosidosis due to defective processing of the precursor β-hexosaminidase α chain. Sequence analysis of a clone containing the entire protein coding sequence showed a single nucleotide substitution, from G to A, at nucleotide residue no. 1444, which resulted in a change in amino acid residue no. 482, from the normal glutamic acid to lysine. This transversion was confirmed in two other cDNAs from the same unamplified library. The results collectively indicate that the change from the strongly negative to strongly positive charge at amino acid residue no. 482 is responsible for the defective processing of the enzyme in this patient.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb01836.x
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  • 5
    Electronic Resource
    Electronic Resource
    NPC1 gene mutations in Japanese patients with Niemann-Pick disease type C (1999)
    Springer
    Human genetics 〈Berlin〉 105 (1999), S. 10-16 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Complementary and genomic DNAs isolated from the fibroblasts of 10 Japanese (7 late infantile, 2 juvenile, and 1 adult form of the disease) and one Caucasian patient with Niemann-Pick disease type C were analyzed for mutations in the NPC1 gene. Fourteen novel mutations were found including small deletions and point mutations. A one-base deletion and a point mutation caused splicing errors. The mutations were not clustered in any particular region of the gene and were found both in and out of the transmembrane domains. Three patients were homozygous, five were compound heterozygous, and the remaining three were suspected of being compound hetrozygous with an unknown error in one of their NPC1 alleles. Of the 14 mutations, the G1553A substitution that caused a splicing error of exon 9 appeared to be relatively common in Japanese patients, because two patients were homozygous and one patient was compound heterozygous for this mutation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004399900059
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  • 6
    Electronic Resource
    Electronic Resource
    Genetic analysis of control of proliferation in fibroblastic cells in culture. II. Alteration in proliferative and survival phenotypes in a set of temperature-sensitive mutants of rat 3Y1 cells after infection or transformation with simian virus 40 (1984)
    Springer
    Somatic cell and molecular genetics 10 (1984), S. 29-36 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Mutants of rat 3Y1 fibroblasts, temperature sensitive for proliferation or survival and which represent each of eight complementation groups, were examined to determine whether cells made quiescent at confluence at 33.8
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01534470
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  • 7
    Electronic Resource
    Electronic Resource
    Genetic analysis of control of proliferation in fibroblastic cells in culture. I. Isolation and characterization of mutants temperature-sensitive for proliferation or survival of untransformed diploid rat cell line 3Y1 (1984)
    Springer
    Somatic cell and molecular genetics 10 (1984), S. 17-28 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Mutants temperature sensitive for proliferation or survival were isolated from an untransformed diploid clone of fibroblastic rat cells (3Y1), according to an isolation protocol that selected for mutants defective at 38.5
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01534469
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  • 8
    Electronic Resource
    Electronic Resource
    Hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency: Identification of point mutations in Japanese patients with Lesch-Nyhan syndrome and hereditary gout and their permanent expression in an HPRT-deficient mouse cell line (1994)
    Springer
    Human genetics 〈Berlin〉 93 (1994), S. 175-181 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Two different single nucleotide transitions of hypoxanthine-guanine phosphoribosyltransferase (HPRT) were identified in a Japanese patient with Lesch-Nyhan syndrome (LNS) and a patient with hereditary gout. HPRT enzyme activities in the two patients were severely deficient, but the size and amount of mRNA were normal according to Northern analysis. Entire coding regions of HPRT cDNAs were amplified by PCR and sequenced. A G-to-A substitution at base 208 in exon 3, which predicted glycine 70 to arginine, was detected in the LNS patient (identical mutation with HPRTUtrecht). A C-to-A substitution at base 73 in exon 2, which predicted proline 25 to threonine, was detected in the gout patient (designated HPRTYonago). We transfected normal HPRT cDNA, mutant cDNA with HRPTUtrecht or mutant cDNA with HPRTYonago, respectively, to HPRT-deficient mouse cells and isolated permanent expression cell lines. The HPRT-deficient mouse cells had no detectable HPRT activity and a very low amount of HPRT mRNA. When the HPRT-deficient mouse cells were transfected with normal human cDNA, HPRT enzyme activity increased to 21.8% that of normal mouse cells. The mouse cells transfected with HPRTUtrecht showed no increase in HPRT activity; however, when the mouse cells were transfected with HPRTYonago, the activity increased to 2.4% that of normal activity. The proliferative phenotypes of these cells in HAT medium and in medium containing 6-thioguanine were similar to those of skin fibroblasts from the patients. This series of studies confirmed that each of the two point mutations was responsible for the decreases in HPRT enzyme activity, and the proliferative phenotypes in HAT medium and medium containing 6-thioguanine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00210606
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  • 9
    Electronic Resource
    Electronic Resource
    Restoration of the cholesterol metabolism in 3T3 cell lines derived from the sphingomyelinosis mouse (spm/spm) by transfer of a human chromosome 18 (1993)
    Springer
    Human genetics 〈Berlin〉 92 (1993), S. 157-162 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We searched for a human chromosome that would restore the cholesterol metabolism in 3T3 cell lines (SPM-3T3) derived from homozygous sphingomyelinosis mice (spm/spm). Mouse A9 cells containing a single copy of pSV2neo-tagged chromosomes 9, 11, or 18 derived from normal human fibroblasts served as donor cells for transfer of human chromosomes. Purified A9 microcells were fused with SPM-3T3 cells, and the microcell hybrids were selected in medium containing G418 antibiotics. The microcell hybrids that contained human chromosomes 9, 11, or 18 in a majority of cells were examined. The accumulation of intracellular cholesterol in the microcell hybrids containing a chromosome 18 decreased markedly, whereas in the microcell hybrids containing either chromosomes 9 or 11 it was similar to that in SPM3T3 cells. The SPM-3T3 cells with an intact chromosome 18 were further passaged and subcloned. Clones which again accumulated intracellular cholesterol had concurrently lost the introduced chromosome 18. The abnormal accumulation was associated with a decrement in the esterification of exogenous cholesterol. These findings suggest that the gene responsible for the abnormal cholesterol metabolism in the spm/spm mice can be restored by a hu man chromosome 18. The gene was tentatively mapped on 18pter→18p11.3 or 18q21.3→qter that was lost during subcloning, thereby resulting in reaccumulation of the intracellular cholesterol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00219684
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  • 10
    Electronic Resource
    Electronic Resource
    A C57BL/KsJ mouse model of Niemann-Pick disease (spm) belongs to the same complementation group as the major childhood type of Niemann-Pick disease type C (1997)
    Springer
    Human genetics 〈Berlin〉 99 (1997), S. 350-353 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A cell line (SPM-3T3) derived from a C57BL/ KsJ mouse model of Niemann-Pick disease type C (NP-C) shows biochemical abnormalities similar to those in fibroblasts derived from NP-C. Somatic cell hybridization analysis of the SPM-3T3 cells and five fibroblast strains derived from NP-C patients (four childhood cases and one adult case) was carried out. The criterion for complementation was the restoration of a normal intracellular fluorescent pattern in multinucleated cells stained with filipin to demonstrate cholesterol accumulation. These cells can be assigned to two complementation groups. The SPM-3T3 cells did not complement cell strains derived from childhood-type NP-C, while they complemented a cell strain derived from an adult patient. Our results suggest that SPM-3T3 represents a genetically authentic model of a major complementation group of NP-C, and that NP-C consists of genetically heterogeneous groups.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050370
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