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  • membrane permeability transition  (3)
  • cry gene expression  (2)
  • Springer  (5)
  • American Chemical Society (ACS)
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Keywords
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  • Springer  (5)
  • American Chemical Society (ACS)
Years
  • 1
    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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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Analysis ofcrylAa expression insigE andsigK mutants ofBacillus thuringiensis (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 734-741 
    Details
    ISSN: 1617-4623
    Keywords: Bacillus thuringiensis ; cry gene expression ; Encapsulation ; Sigma factors ; Sporulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract ThesigE andsigK genes, encoding the sporulation-specific sigma factorsσ 35 andσ 28 ofBacillus thuringiensis, were each disrupted by inserting a gene conferring resistance to kanamycin into their coding sequence. TheB. thuringiensis SigE− and SigK− mutant strains were blocked at different sporulation stages and were unable to sporulate. The SigE− strain was blocked at stage II of sporulation, whereas the SigK− strain was blocked at stage IV. The expression of acryIAa′-′lacZ transcriptional fusion was analysed in these genetic backgrounds and it was found that both sigma factors are involved in the in vivo transcription of this gene. However, the SigK− strain harbouring thecryIAa gene produced amounts of toxin similar to those produced by theB. thuringiensis Spo+ strain. The toxins accumulated in the mother cell compartment to form a crystal inclusion which remained encapsulated within the cell wall. Thus, transcription from theσ E-dependent promoter alone (Bt I promoter) is sufficient to support high levels of toxin production inB. thuringiensis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172985
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  • 4
    Electronic Resource
    Electronic Resource
    Analysis of cryIAa expression in sigE and sigK mutants of Bacillus thuringiensis (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 734-741 
    Details
    ISSN: 1617-4623
    Keywords: Key words Bacillus thuringiensis ; cry gene expression ; Encapsulation ; Sigma factors ; Sporulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The sigE and sigK genes, encoding the sporulation-specific sigma factors σ35 and σ28 of Bacillus thuringiensis, were each disrupted by inserting a gene conferring resistance to kanamycin into their coding sequence. The B. thuringiensis SigE- and SigK- mutant strains were blocked at different sporulation stages and were unable to sporulate. The SigE- strain was blocked at stage II of sporulation, whereas the SigK- strain was blocked at stage IV. The expression of a cryIAa′-′lacZ transcriptional fusion was analysed in these genetic backgrounds and it was found that both sigma factors are involved in the in vivo transcription of this gene. However, the SigK- strain harbouring the cryIAa gene produced amounts of toxin similar to those produced by the B. thuringiensis Spo+ strain. The toxins accumulated in the mother cell compartment to form a crystal inclusion which remained encapsulated within the cell wall. Thus, transcription from the σE-dependent promoter alone (Bt I promoter) is sufficient to support high levels of toxin production in B. thuringiensis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172985
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  • 5
    Electronic Resource
    Electronic Resource
    On the Protection by Inorganic Phosphate of Calcium-Induced Membrane Permeability Transition (1997)
    Springer
    Journal of bioenergetics and biomembranes 29 (1997), S. 571-577 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondrial calcium ; inorganic phosphate ; membrane permeability transition ; calcium transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The role of inorganic phosphate as inhibitor of mitochondrial membrane permeability transition was studied. It is shown that in mitochondria containing a high phosphate concentration, i.e., 68 nmol/mg, Ca2+ did not activate the pore opening. Conversely, at lower levels of matrix phosphate, i.e., 38 nmol/mg, Ca2+ was able to induce subsequent pore opening. The inhibitory effect of phosphate was apparent in sucrose-based media, but it was not achieved in KCl media. The matrix free Ca2+ concentration and matrix pH were lowered by phosphate, but they were always higher in K+-media. In the absence of ADP, phosphate strengthened the inhibitory effect of cyclosporin A on carboxyatractyloside-induced Ca2+ efflux. Acetate was unable to replace phosphate in the induction of the aforementioned effects. It is concluded that phosphate preserves selective membrane permeability by diminishing the matrix free Ca2+ concentration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1022483018482
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