Phosphate ion channels in sarcoplasmic reticulum of rabbit skeletal muscle

Derek R. Laver*, Gerlinde K.E. Lenz, Angela F. Dulhunty

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    31 Citations (Scopus)

    Abstract

    1. Phosphate ions (Pi) enter intracellular Ca2+ stores and precipitate Ca2+. Since transport pathways for Pi across the membrane of intracellular calcium stores have not been identified and anion channels could provide such a pathway, we have examined the Pi conductance of single anion channels from the sarcoplasmic reticulum (SR) of rabbit skeletal muscle using the lipid bilayer technique. 2. Two anion channels in skeletal muscle SR, the small conductance (SCI) and big conductance (BCl) chloride channels, were both found to have a Pi conductance of 10 pS in 50 mM Pi. The SCl channel is a divalent anion channel which can pass HPO42- as well as SO42- (60 pS in 100 mM free SO42-). The BCl channel is primarily a monovalent anion channel. The SCl and BCl channels are permeable to a number of small monovalent anions, showing minor selectivity between Cl-, I- and Br- (Cl- > I- > Br-) and relative impermeability to cations and large polyatomic anions (Cs+, Na+, choline+, Tris+, Hepes- and CH3O3S-). 3. The Pi conductance of SCl and BCl channels suggests that both channel types could sustain the observed Pi fluxes across the SR membrane. Comparison of the blocking effects of the phosphonocarboxylic acids, ATP and DIDS, on the anion channels with their effects on Pi transport suggests that the SCl channel is the more likely candidate for the SR Pi transport mechanism. 4. The SCl channel, with previously unknown function, provides a regulated pathway for Pi across the SR membrane which would promote Pi entry and thereby changes in the rapidly releasable Ca2+ store during onset and recovery from muscle fatigue. Anion channels may provide a pathway for Pi movement into and out of Ca2+ stores in general.

    Original languageEnglish
    Pages (from-to)715-728
    Number of pages14
    JournalJournal of Physiology
    Volume535
    Issue number3
    DOIs
    Publication statusPublished - 15 Sept 2001

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