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  • 1
    Electronic Resource
    Electronic Resource
    Peptide-specific antibodies and proteases as probes of the transmembrane topology of the bovine heart mitochondrial porin (1991)
    s.l. : American Chemical Society
    Biochemistry 30 (1991), S. 10191-10200 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00106a017
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of Channel-Forming Activity in Muscle Biopsy from a Porin-Deficient Human Patient (2000)
    Springer
    Journal of bioenergetics and biomembranes 32 (2000), S. 585-593 
    Details
    ISSN: 1573-6881
    Keywords: Porin deficiency ; muscle biopsy ; porin isoforms ; VDAC ; lipid-bilayer membrane ; volt age dependence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract A bioptic specimen from the muscles of a patient suffering from severe myopathy was inspected for the presence of human porin 31HL. Western blotting suggested that the specimen was free of the most abundant eukaryotic porin 31HL (HVDAC1). The specimen was treated with detergent and the soluble protein fraction was passed through a dry hydroxyapatite column. The passthrough of this column was inspected for channel formation in artificial lipid-bilayer membranes. The channel observed under these conditions had a single-channel conductance of about 2.5 nS in 1 M KCl, was cation selective, and was found to be virtually voltage independent. Experiments with a control specimen from a healthy human being, without any indication for muscle myopathy, revealed the presence of the voltage-dependent porin 31HL in the sample. It is discussed whether the patient's bioptic specimen contained another human porin, which has not been studied to date in its natural environment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005622611410
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Extramitochondrial Porin: Facts and Hypotheses (2000)
    Springer
    Journal of bioenergetics and biomembranes 32 (2000), S. 79-89 
    Details
    ISSN: 1573-6881
    Keywords: Porin ; VDAC ; caveolae ; plasmalemma ; cholesterol transport ; maxi chloride channel ; patch clamp ; biotin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Mitochondrial porin, or VDAC, is a pore-forming protein abundant in the outer mitochondrialmembrane. Several publications have reported extramitochondrial localizations as well, butthe evidence was considered insufficient by many, and the presence of porin in nonmitochondrialcellular compartments has remained in doubt for a long time. We have now obtained newdata indicating that the plasma membrane of hematopoietic cells contains porin, probablylocated mostly in caveolae or caveolae-like domains. Porin was purified from the plasmamembrane of intact cells by a procedure utilizing the membrane-impermeable labeling reagentNH-SS-biotin and streptavidin affinity chromatography, and shown to have the same propertiesas mitochondrial porin. A channel with properties similar to that of isolated VDAC wasobserved by patch-clamping intact cells. This review discusses the evidence supportingextramitochondrial localization, the putative identification of the plasma membrane porin with the“maxi” chloride channel, the hypothetical mechanisms of sorting porin to various cellularmembrane structures, and its possible functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005516513313
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  • 4
    Electronic Resource
    Electronic Resource
    Intracellular localization and isoform expression of the voltage-dependent anion channel (VDAC) in normal and dystrophic skeletal muscle (2000)
    Springer
    Journal of muscle research and cell motility 21 (2000), S. 433-442 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Voltage-dependent anion channels (VDACs) are a family of pore-forming proteins encoded by different genes, with at least three protein products expressed in mammalian tissues. The major recognized functional role of VDACs is to permit the almost free permeability of the outer mitochondrial membrane (OMM). Although VDAC1 is the best known among VDAC isoforms, its exclusively mitochondrial location is still debated. Therefore, we have measured its co-localization with markers of cellular organelles or compartments in skeletal muscle fibers by single or double immunofluorescence and traditional as well as confocal microscopy. Our results show that VDAC1 immunoreactivity corresponds to mitochondria and sarcoplasmic reticulum, while sarcolemmal reactivity, previously reported, was not observed. Since VDAC1 has been suggested to be involved in the control of oxidative phosphorylation, we sought for possible gene regulation of VDAC1, VDAC2 and VDAC3 in skeletal muscle of the dystrophin-deficient mdx mouse, which suffers of an impaired control of energy metabolism. Our results show that, while VDAC1 mRNA and protein and VDAC2 mRNA are normally expressed, VDAC3 mRNA is markedly down-regulated in mdx mouse muscle at different ages (before, during and after the outburst of myofiber necrosis). This finding suggests a possible involvement of VDAC3 expression in the early pathogenic events of the mdx muscular dystrophy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005688901635
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    Paper (German National Licenses)
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