Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

In yeast, Ca2+ and octylguanidine interact with porin (VDAC) preventing the mitochondrial permeability transition.

In yeast, Ca2+ and octylguanidine interact with porin (VDAC) preventing the mitochondrial permeability transition. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • In yeast, Ca2+ and octylguanidine interact with porin (VDAC) preventing the mitochondrial permeability transition. Abstract Text:

    manuel Manuel ,victoriano Victoriano ,odile bunoustOdile Bunoust, manon Manon,michel rigouletMichel Rigoulet,salvador uribeSalvador Uribe,manuel Manuel ,victoriano Victoriano ,odile bunoustOdile Bunoust, manon Manon,michel rigouletMichel Rigoulet,salvador uribeSalvador Uribe,

    In yeast, Ca(2+) and long chain alkylguanidines interact with mitochondria modulating the opening of the yeast mitochondrial unspecific channel. Mammalians possess a similar structure, the mitochondrial permeability transition pore. The composition of these pores is under debate. Among other components, the voltage-dependent anion channel has been proposed as a component of either pore. In yeast from an industrial strain, octylguanidine and calcium closed the yeast mitochondrial unspecific channel. Here, the effects of the cations Ca(2+) or octylguanidine and the voltage-dependent anion channel effector decavanadate were evaluated in yeast mitochondria from either a wild type or a voltage-dependent anion channel deletion laboratory strain. It was observed that in the absence of voltage-dependent anion channel, the yeast mitochondrial unspecific channel was desensitized to Ca(2+), octylguanidine or decavanadate but remained sensitive to phosphate. It is thus suggested that in yeast mitochondria, the voltage-dependent anion channel has a cation binding site where Ca(2+) and octylguanidine interact, conferring cation sensitivity to the yeast mitochondrial unspecific channel.

    In yeast, Ca2+ and octylguanidine interact with porin (VDAC) preventing the mitochondrial permeability transition. Publishing Authors By Initials

    m M ,v V ,o bunoustO Bunoust,s manonS Manon,m rigouletM Rigoulet,s uribeS Uribe,m M ,v V ,o bunoustO Bunoust,s manonS Manon,m rigouletM Rigoulet,s uribeS Uribe,

    For similar proteins: carrier proteins: membrane transport proteins: ion channels: porins: voltage-dependent anion channels research abstracts see: proteins: carrier proteins: membrane transport proteins: ion channels: porins: voltage-dependent anion channels research

    PUBMED ID PMID:

    MEDLINE DATE:

    In yeast, Ca2+ and octylguanidine interact with porin (VDAC) preventing the mitochondrial permeability transition. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Biochimica et biophysica acta

    VOLUME: 1767

    Page Numbers: 1245-51

    Journal Abbreviation: Biochim. Biophys. Acta

    ISSN: 0006-3002

    DAY: 19

    MONTH: 07

    YEAR: 2007

    In yeast, Ca2+ and octylguanidine interact with porin (VDAC) preventing the mitochondrial permeability transition. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 217513

    In yeast, Ca2+ and octylguanidine interact with porin (VDAC) preventing the mitochondrial permeability transition. Keywords Mesh Terms:

    KEYWORDS: Voltage-Dependent Anion Channels

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: In yeast, Ca2+ and octylguanidine interact with porin (VDAC) preventing the mitochondrial permeability transition. Information

    Substance Name: Oxygen

    Registry Number: 7782-44-7

    Grant and Affiliation Information for In yeast, Ca2+ and octylguanidine interact with porin (VDAC) preventing the mitochondrial permeability transition.

    AFFILIATION: Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, 04510 México D. F., Mexico.

    Country: Netherlands

    Netherlands Research PublicationNetherlands Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: Biochim Biophys Acta

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    In yeast, Ca2+ and octylguanidine interact with porin VDAC preventing the mitochondrial permeability transition Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News