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  • Articles: DFG German National Licenses  (2)
  • 1995-1999  (2)
Source
  • Articles: DFG German National Licenses  (2)
Material
Years
  • 1995-1999  (2)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Human α-galactosidase A: High plasma activity expressed by the -30G→A allele (1997)
    Springer
    Journal of inherited metabolic disease 20 (1997), S. 643-657 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Human α-galactosidase A (EC 3.2.1.22; α-Gal A) is the lysosomal exoglycosidase responsible for the hydrolysis of terminal α-galactosyl residues from glycoconjugates and is the defective enzyme causing Fabry disease (McKusick 301500). An unsually elevated level of plasma α-Gal A activity (〉2.5 times the normal mean) was detected in two unrelated normal males and the elevated activities were inherited as X-linked traits in their families. Sequencing of the α-Gal A coding region, intron/exon boundaries and 5′-flanking region from the proband identified a single mutation, a G→A transition 30 nt upstream from the initiation of translation codon in exon 1. The -30G→A mutation occurred in a putative NFκB/Ets consensus binding site that was recently shown to inhibit protein binding to the 5′-untranslated region of the gene, providing a possible explanation for its high activity. To further characterize the mutation, the mRNA and protein expressed by this variant allele were studied. Purified plasma and lymphoblast α-Gal A activity from individuals with the -30G→A mutation had normal physical and kinetic properites. In vitro translation of mRNAs from the cloned normal and high plasma activity alleles resulted in similar levels of α-Gal A protein, indicating that this mutation did not enhance translation. These findings suggest that the -30G→A mutation in the 5′-untranslated region of the α-Gal A gene enhances transcription, presumably by interfering with the binding of negatively-acting transcription factors which normally decrease α-Gal A expression in various cells. Preliminary studies of the frequency of the -30G→A mutation in 395 unrelated normal males of mixed ancestry revealed two additional unrelated individuals who had high plasma enzymatic activity and the mutation, confirming the effect of this mutation on enzyme expression and suggesting that about 0.5% of normal individuals have high plasma α-Gal A activity due to this variant allele.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005366224351
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Mouse uroporphyrinogen decarboxylase: cDNA cloning, expression, and mapping (1996)
    Springer
    Mammalian genome 7 (1996), S. 349-352 
    Details
    ISSN: 1432-1777
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Uroporphyrinogen decarboxylase (URO-decarboxylase; EC 4.1.1.37), the heme biosynthetic enzyme responsible for the conversion of uroporphyrinogen III to coproporphyrinogen III, is the enzymatic defect in porphyria cutanea tarda, the most common porphyria. The mouse URO-decarboxylase cDNA was isolated from a mouse adult liver cDNA library. The longest clone of 1.5 kb, designated pmUROD-1, had 5′ and 3′ untranslated sequences of 281 and 97 bp, respectively, and an open reading frame of 1104 bp encoding a 367-amino acid polypeptide with a predicted molecular mass of 40,595 Da. The mouse and human coding sequences had 87.8% and 90.0% nucleotide and amino acid identity, respectively. The authenticity of the mouse cDNA was established by expression of the active enzyme in Escherichia coli. In addition, the analysis of two sets of multilocus genetic crosses localized the mouse gene, Urod, on Chromosome (Chr) 4, consistent with the map location of the human gene to a position of conserved synteny on Chr 1. The availability of the mouse URO-decarboxylase should facilitate studies of the structure and organization of the mouse genomic sequence and the development of a mouse model of this inherited porphyria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003359900101
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    Paper (German National Licenses)
    Fulltext
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