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  • Matrix calcium  (2)
  • Musca domestica  (2)
  • 1995-1999  (4)
  • 1955-1959
  • 1996  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Identification of mutations in the houseflypara-type sodium channel gene associated with knockdown resistance (kdr) to pyrethroid insecticides (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 51-60 
    Details
    ISSN: 1617-4623
    Keywords: Knockdown resistance (kdr) ; Musca domestica ; para ; Pyrethroid ; Sodium channel gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We report the isolation of cDNA clones containing the full 6.3-kb coding sequence of thepara-type sodium channel gene of the housefly,Musca domestica. This gene has been implicated as the site of knockdown resistance (kdr), an important resistance mechanism that confers nerve insensitivity to DDT and pyrethroid insecticides. The cDNAs predict a polypeptide of 2108 amino acids with close sequence homology (92% identity) to theDrosophila para sodium channel, and around 50% homology to vertebrate sodium channels. Only one major splice form of the housefly sodium channel was detected, in contrast to theDrosophila para transcript which has been reported to undergo extensive alternative splicing. Comparative sequence analysis of housefly strains carryingkdr or the more potentsuper-kdr factor revealed two amino acid mutations that correlate with these resistance phenotypes. Both mutations are located in domain II of the sodium channel. A leucine to phenylalanine replacement in the hydrophobic IIS6 transmembrane segment was found in two independentkdr strains and sixsuper-kdr strains of diverse geographic origin, while an additional methionine to threonine replacement within the intracellular IIS4-S5 loop was found only in thesuper-kdr strains. Neither mutation was present in five pyrethroid-sensitive strains. The mutations suggest a binding site for pyrethroids at the intracellular mouth of the channel pore in a region known to be important for channel inactivation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02173204
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of mutations in the housefly para-type sodium channel gene associated with knockdown resistance (kdr) to pyrethroid insecticides (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 51-60 
    Details
    ISSN: 1617-4623
    Keywords: Key words Knockdown resistance (kdr) ; Musca domestica ; para ; Pyrethroid ; Sodium channel gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We report the isolation of cDNA clones containing the full 6.3-kb coding sequence of the para-type sodium channel gene of the housefly, Musca domestica. This gene has been implicated as the site of knockdown resistance (kdr), an important resistance mechanism that confers nerve insensitivity to DDT and pyrethroid insecticides. The cDNAs predict a polypeptide of 2108 amino acids with close sequence homology (92% identity) to the Drosophila para sodium channel, and around 50% homology to vertebrate sodium channel. Only one major splice from of the housefly sodium channel was detected, in contrast to the Drosophila para transcript which has been reported to undergo extensive alternative splicing. Comparative sequence analysis of housefly strains carrying kdr or the more potent super-kdr factor revealed two amino acid mutations that correlate with these resistance phenotypes. Both mutations are located in domain II of the sodium channel. A leucine to phenylalanine replacement in the hydrophobic IIS6 transmembrane segment was found in two independend kdr strains and six super-kdr strains of diverse geographic origin, while an additional methionine to threonine replacement within the intracellular IIS4-S5 loop was found only in the super-kdr strains. Neither mutation was present in five pyrethroid-sensitive strains. The mutations suggest a binding site for pyrethroids at the intracellular mouth of the channel pore in a region known to be important for channel inactivation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004389670006
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Modulation of matrix Ca2+ content by the ADP/ATP carrier in brown adipose tissue mitochondria. Influence of membrane lipid composition (1996)
    Springer
    Journal of bioenergetics and biomembranes 28 (1996), S. 69-76 
    Details
    ISSN: 1573-6881
    Keywords: Matrix calcium ; BAT mitochondria ; membrane permeability transition ; adenine nucleotide translocase ; calcium transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The role of the adenine nucleotide translocase on Ca2+ homeostasis in mitochondria from brown adipose tissue was examined. It was found that in mitochondria incubated with 50 μM Ca2+, ADP was not needed to retain the cation, but it was required for strengthening the inhibitory effect of cyclosporin on membrane permeability transition as induced by menadione. In addition, carboxyatractyloside was unable to promote matrix Ca2+ release, even though it inhibits the ADP exchange reaction. However, when the Ca2+ concentration was increased to 150 μM, carboxyatractyloside did induce Ca2+ release, and ADP favored Ca2+ retention. Determination of cardiolipin content in the inner membrane vesicles showed a greater concentration in brown adipose tissue mitochondria than that found in kidney mitochondria. It is suggested that the failure of the adenine nucleotide translocase to influence membrane permeability transition depends on the lipid composition of the inner membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02109905
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  • 4
    Electronic Resource
    Electronic Resource
    Modulation of matrix Ca2+ content by the ADP/ATP carrier in brown adipose tissue mitochondria. Influence of membrane lipid composition (1996)
    Springer
    Journal of bioenergetics and biomembranes 28 (1996), S. 69-76 
    Details
    ISSN: 1573-6881
    Keywords: Matrix calcium ; BAT mitochondria ; membrane permeability transition ; adenine nucleotide translocase ; calcium transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The role of the adenine nucleotide translocase on Ca2+ homeostasis in mitochondria from brown adipose tissue was examined. It was found that in mitochondria incubated with 50 μM Ca2+, ADP was not needed to retain the cation, but it was required for strengthening the inhibitory effect of cyclosporin on membrane permeability transition as induced by menadione. In addition, carboxyatractyloside was unable to promote matrix Ca2+ release, even though it inhibits the ADP exchange reaction. However, when the Ca2+ concentration was increased to 150 μM, carboxyatractyloside did induce Ca2+ release, and ADP favored Ca2+ retention. Determination of cardiolipin content in the inner membrane vesicles showed a greater concentration in brown adipose tissue mitochondria than that found in kidney mitochondria. It is suggested that the failure of the adenine nucleotide translocase to influence membrane permeability transition depends on the lipid composition of the inner membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02150680
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    Paper (German National Licenses)
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