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  • Drosophila melanogaster  (2)
  • Biochemistry and Biotechnology
  • glycogen phosphorylase
  • Springer  (3)
  • Wiley-Blackwell  (1)
  • Blackwell Publishing Ltd
  • 1990-1994  (4)
Collection
Publisher
  • Springer  (3)
  • Wiley-Blackwell  (1)
  • Blackwell Publishing Ltd
Years
Year
  • 1
    ISSN: 1432-1432
    Keywords: Urate oxidase ; Drosophila pseudoobscura ; Drosophila melanogaster ; Nucleotide sequence ; Evolutionary comparison ; Gene regulation ; Malpighian tubules
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The urate oxidase (UO) transcription unit of Drosophila pseudoobscura was cloned, sequenced, and compared to the UO transcription unit from Drosophila melanogaster. In both species the UO coding region is divided into two exons of approximately equal size. The deduced D. pseudoobscura and D. melanogaster UO peptides have 346 and 352 amino acid residues, respectively. The nucleotide sequences of the D. pseudoobscura and D. melanogaster UO protein-coding regions are 82.2% identical whereas the deduced amino acid sequences are 87.6% identical with 42 amino acid changes, 33 of which occur in the first exon. Although the UO gene is expressed exclusively within the cells of the Malpighian tubules in both of these species, the temporal patterns of UO gene activity during development are markedly different. UO enzyme activity, UO protein, and UO mRNA are found in the third instar larva and adult of D. melanogaster but only in the adult stage of D. pseudoobscura. The intronic sequences and the extragenic 5′ and 3′ flanking regions of the D. pseudoobscura and D. melanogaster UO genes are highly divergent with the exception of eight small islands of conserved sequence along 772 by 5′ of the UO protein-coding region. These islands of conserved sequence are possible UO cis-acting regulatory elements as they reside along the 5′ flanking DNA of the D. melanogaster UO gene that is capable of conferring a wild-type D. melanogaster pattern of UO regulation on a UO-lacZ fusion gene.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 117 (1992), S. 63-70 
    ISSN: 1573-4919
    Keywords: glycogen phosphorylase ; alloxan-diabetes ; cardiomyocytes ; G-protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The basis for the hypersensitive response of glycogen phosphorylase to epinephrine stimulation was investigated in adult rat cardiomyocytes isolated from normal and alloxan-diabetic animals. To assess potential G-protein involvement in the response, normal and diabetic derived myocytes were incubated with either cholera or pertussis toxin prior to hormonal stimulation. Pretreatment of cardiomyocytes with cholera toxin resulted in a potentiated response to epinephrine stimulation whereas pertussis toxin did not affect the activation of this signaling pathway. To determine if the enhanced response of phosphorylase activation resulted from an alteration in adenylate cyclase activation, the cells were challenged with forskolin. After 3 hr in primary culture, diabetic cardiomyocytes exhibited a hypersensitive response to forskolin stimulation relative to normal cells. However, after 24 hr in culture, both normal and diabetic myocytes responded identically to forskolin challenge. The present data suggest that a cholera toxin sensitive G-protein mediates the hypersensitive response of glycogen phosphorylase to catecholamine stimulation in diabetic cardiomyocytes and this response which is present in alloxan-diabetic cells and is induced in vitro in normal cardiomyocytes is primarily due to a defect at a post-receptor site.
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  • 3
    ISSN: 1617-4623
    Keywords: Drosophila melanogaster ; Transcription map ; Faint bands ; Interband chromatin ; Polytene chromosomes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Urate oxidase mRNA and five other transcripts map along 38 kb of DNA in the region 28C on the Drosophila melanogaster second chromosome. Three biotinylated restriction fragments from this 38 kb of DNA, one from each end and one from the middle, were individually hybridized in situ to slightly stretched salivary gland polytene chromosomes. The data from these in situ hybridizations in combination with the transcription map of the 38 kb of DNA indicate that: (i) there are six discrete RNA species encoded along the 38 kb of DNA and (ii) these six transcripts map to the faint band/interband region which includes the proximal edge of 280, the three faint bands, 28C2, 280 and 28C4-5(−), and the adjacent interband chromatin. Our data are consistent with the few published studies directly demonstrating that faint band/interband regions of the Drosophila melanogaster salivary gland polytene chromosomes code for a high density of transcripts.
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  • 4
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Lipoprotein(a) resembles low density lipoprotein in structure, except that a unique apolipoprotein (apo), apo(a), is linked to apo B-100. Variations in the number of sequence repeats in the apo(a) gene give rise to a range of isoforms. Depending on the method used, 6-30 apo(a) isoforms have been observed; however, the correspondence of these different isoforms has not been reported, making between-study comparisons difficult. In the present study we address this question by characterizing the apo(a) phenotypes of 48 sera using two previously reported separation methods, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE, 3-12% gels) and SDS-agarose gel electrophoresis. In addition, the molecular weight of each isoform was estimated using haptoglobin 2-2 polymers as molecular weight standards. Among the 48 sera, 15 distinct apo(a) isoforms were separated by SDS-PAGE and 28 by SDS-agarose gel electrophoresis. There was excellent correlation between the two nomenclature systems (r = -0.97, p 〈 0.001, by rank correlation), and the ranges were totally overlapping, with the same two isoforms being identified as the largest and smallest by either method. The apparent molecular mass range for the isoforms was 294-624 kDa, which is in close agreement with the theoretical molecular mass range of 238-643 kDa, calculated from the sequence and carbohydrate content of recombinant apo(a). The disparity in number of isoforms between methods was expected, due to the poorer separation of apo(a) by SDS-PAGE; 3.1 ± 1.7 (median, 2.0) SDS-agarose isoforms were combined for each SDS-PAGE isoform. The present study demonstrates that the nomenclature systems for apo(a) isoforms separated by SDS-PAGE or by SDS-agarose gel electrophoresis are well correlated mathematically and encompass the same size range; however, the better resolution of SDS-agarose electrophoresis suggests that it is the method of choice for apo(a) phenotyping. As further apo(a) isoforms are identified, it will be important to address the question of a standardized nomenclature, in order to facilitate between-study comparisons.
    Additional Material: 3 Ill.
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