Publication | Open Access
Calcium-mediated changes in gap junction structure: evidence from the low angle X-ray pattern.
91
Citations
14
References
1983
Year
X-ray CrystallographyGap Junction StructureMolecular BiologyCytoskeletonCell JunctionsCellular PhysiologyElectron MicroscopyMembrane TransportIntercellular CommunicationBiophysicsIon ChannelsMembrane BiologyCell BiologyCrystallographySignal TransductionGap JunctionsNatural SciencesPhysiologyX-ray DiffractionCalcium-mediated ChangesElectrophysiologyCellular BiochemistryMedicineExtracellular Matrix
Rat liver gap junctions were isolated in Ca2+-free media and analyzed in controlled environments by x-ray diffraction of partially oriented pellets. Different treatments of the same preparations were compared. The ordered hexagonal lattices gave rise to detail that was sensitive to low Ca2+ concentrations (0.05 mM), but not to Mg2+ (up to 0.16 mM) or pH (between 6.0 and 8.0). The major Ca2+-mediated responses were reductions in the intensity of the (1, 0) peak and in the off-equatorial contributions to the (2, 1) peak, and changes of scale equivalent to a decrease (approximately 2%) in lattice dimension, but an increase (approximately 4%) in the dimension perpendicular to the lattice. A simple structural interpretation of these findings is that Ca2+ induces the subunits of the channel-forming assembly, the connexon, to align more nearly parallel to the channel, thereby causing the connexon to become slightly longer and more radially compact. The rearrangement is of the same nature as one found under less physiological circumstances by electron microscopy (Unwin, P. N. T., and G. Zampighi, 1980, Nature (Lond.)., 283:545-549), and may be part of a coordinated mechanism by which the channel closes.
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