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Calcium-mediated changes in gap junction structure: evidence from the low angle X-ray pattern.

P N Unwin, P D Ennis

    The Journal of Cell Biology
    |November 1, 1983
    PubMed
    Summary
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    Calcium ions (Ca2+) influence rat liver gap junction structure, causing connexons to align more parallel, potentially closing the channel. This structural change is sensitive to low Ca2+ but not Mg2+ or pH variations.

    Area of Science:

    • Cell biology
    • Structural biology
    • Biophysics

    Background:

    • Gap junctions are crucial for intercellular communication in tissues like the liver.
    • Understanding the structural basis of gap junction regulation is key to deciphering cellular signaling.

    Purpose of the Study:

    • To investigate the structural effects of calcium ions (Ca2+) on isolated rat liver gap junctions.
    • To determine the specific Ca2+ concentrations that induce structural changes in gap junction lattices.

    Main Methods:

    • Isolation of rat liver gap junctions in Ca2+-free media.
    • X-ray diffraction analysis of partially oriented gap junction pellets.
    • Comparison of structural responses to varying Ca2+, Mg2+, and pH conditions.

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    Main Results:

    • Ordered hexagonal lattices of gap junctions were observed.
    • Low Ca2+ concentrations (0.05 mM) significantly altered lattice structure, affecting peak intensities and dimensions.
    • Structural changes were insensitive to Mg2+ and pH variations within the tested ranges.
    • Ca2+ induced a ~2% decrease in lattice dimension and a ~4% increase in the perpendicular dimension.

    Conclusions:

    • Calcium ions induce a conformational change in connexons, aligning them more parallel to the channel axis.
    • This rearrangement results in a longer, more radially compact connexon, potentially contributing to channel closure.
    • The observed Ca2+-mediated structural changes provide insight into the gating mechanism of gap junction channels.