Calcium-mediated changes in gap junction structure: evidence from the low angle X-ray pattern.
Open Access
- 1 November 1983
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 97 (5) , 1459-1466
- https://doi.org/10.1083/jcb.97.5.1459
Abstract
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 60 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 (.apprx. 2%) in lattice dimension, but an increase (.apprx. 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 EM, and may be part of a coordinated mechanism by which the channel closes.This publication has 15 references indexed in Scilit:
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