ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • calcium channels  (1)
  • membrane surface potential  (1)
  • 1
    Electronic Resource
    Electronic Resource
    The permeability transition pore as a mitochondrial calcium release channel: A critical appraisal (1996)
    Springer
    Journal of bioenergetics and biomembranes 28 (1996), S. 131-138 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondrial channels ; permeability transition pore ; calcium channels ; cyclosporin A ; ryanodine receptor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Mitochondria from a variety of sources possess an inner membrane channel, the permeability transition pore. The pore is a voltage-dependent channel, activated by matrix Ca2+ and inhibited by matrix H+, which can be blocked by cyclosporin A, presumably after binding to mitochondrial cyclophilin. The physiological function of the permeability transition pore remains unknown. Here we evaluate its potential role as a fast Ca2+ release channel involved in mitochondrial and cellular Ca2+ homeostasis. We (i) discuss the theoretical and experimental reasons why mitochondria need a fast, inducible Ca2+ release channel; (ii) analyze the striking analogies between the mitochondrial permeability transition pore and the sarcoplasmic reticulum ryanodine receptor-Ca2+ release channel; (iii) argue that the permeability transition pore can act as a selective release channel for Ca2+ despite its apparent lack of selectivity for the transported speciesin vitro; and (iv) discuss the importance of mitochondria in cellular Ca2+ homeostasis, and how disruption of this function could impinge upon cell viability, particularly under conditions of oxidative stress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02110643
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane (1994)
    Springer
    Journal of bioenergetics and biomembranes 26 (1994), S. 509-517 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondrial permeability transition ; cyclosporin A ; cyclosporin analogs ; transmembrane potential ; membrane surface potential ; lipid mediators
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The mitochondrial permeability transition pore allows solutes with a m.w. ≲1500 to equilibrate across the inner membrane. A closed pore is favored by cyclosporin A acting at a high-affinity site, which may be the matrix space cylophilin isozyme. Early results obtained with cyclosporin A analogs and metabolites support this hypothesis. Inhibition by cyclosporin does not appear to require inhibition of calcineurin activity; however, it may relate to inhibition of cyclophilin peptide bond isomerase activity. The permeability transition pore is strongly regulated by both the membrane potential (Δψ) and ΔpH components of the mitochondrial protonmotive force. A voltage sensor which is influenced by the disulfide/sulhydryl state of vicinal sulfhydryls is proposed to render pore opening sensitive to Δψ. Early results indicate that this sensor is also responsive to membrane surface potential and/or to surface potential gradients. Histidine residues located on the matrix side of the inner membrane render the pore responsive to ΔpH. The pore is also regulated by several ions and metabolites which act at sites that are interactive. There are many analogies between the systems which regulate the permeability transition pore and the NMDA receptor channel. These suggest structural similarities and that the permeability transition pore belongs to the family of ligand gated ion channels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762735
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...