Literature DB >> 6788727

Gap junction crystallization in lens fibers after an increase in cell calcium.

G Bernardini, C Peracchia.   

Abstract

Previous studies have shown that cell uncoupling is paralleled by an increase in tightness and crystallinity of gap junction particle arrays. Gap junction crystallinity is believed to be part of the uncoupling mechanism because it can be produced in gap junctions isolated from lens fibers on direct exposure to uncoupling agents such as divalent cations or hydrogen ions. Some doubts, however, have been raised on the capacity of lens fiber junctions to crystallize and uncouple in situ. The present study shows that the gap junctions of rat lens fibers indeed crystallize after a treatment that increases drastically the membrane permeability to ions. The treatment consists of a brief immersion of the lenses in liquid nitrogen, followed by incubation for several hours in Tyrode's solution at 37 degrees C. Immediately after liquid nitrogen treatment, the lenses start gaining sodium and calcium while losing potassium, and eventually become opaque. Addition of 10 mM EDTA to calcium and magnesium-free Tyrode's solutions inhibits particle crystallization and lens cataract, whereas low concentrations of EDTA (1 mM) are not effective. These findings, together with preliminary data on the capacity of lens fibers to heal over, indicate that the gap junctions of lens fibers are capable of crystallizing and uncoupling in situ.

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Year:  1981        PMID: 6788727

Source DB:  PubMed          Journal:  Invest Ophthalmol Vis Sci        ISSN: 0146-0404            Impact factor:   4.799


  11 in total

1.  Gating of connexin 43 gap junctions by a cytoplasmic loop calmodulin binding domain.

Authors:  Qin Xu; Richard F Kopp; Yanyi Chen; Jenny J Yang; Michael W Roe; Richard D Veenstra
Journal:  Am J Physiol Cell Physiol       Date:  2012-03-14       Impact factor: 4.249

2.  Channel reconstitution in liposomes and planar bilayers with HPLC-purified MIP26 of bovine lens.

Authors:  L Shen; P Shrager; S J Girsch; P J Donaldson; C Peracchia
Journal:  J Membr Biol       Date:  1991-10       Impact factor: 1.843

3.  Functional reconstitution of lens gap junction proteins into proteoliposomes.

Authors:  H Nikaido; E Y Rosenberg
Journal:  J Membr Biol       Date:  1985       Impact factor: 1.843

4.  Raised intracellular free calcium within the lens causes opacification and cellular uncoupling in the frog.

Authors:  T J Jacob
Journal:  J Physiol       Date:  1983-08       Impact factor: 5.182

5.  Properties of channels reconstituted from the major intrinsic protein of lens fiber membranes.

Authors:  G R Ehring; G Zampighi; J Horwitz; D Bok; J E Hall
Journal:  J Gen Physiol       Date:  1990-09       Impact factor: 4.086

6.  The structural organization and protein composition of lens fiber junctions.

Authors:  G A Zampighi; J E Hall; G R Ehring; S A Simon
Journal:  J Cell Biol       Date:  1989-06       Impact factor: 10.539

Review 7.  Calmodulin-Connexin Partnership in Gap Junction Channel Regulation-Calmodulin-Cork Gating Model.

Authors:  Camillo Peracchia; Lillian Mae Leverone Peracchia
Journal:  Int J Mol Sci       Date:  2021-12-02       Impact factor: 5.923

8.  Gap junction structures after experimental alteration of junctional channel conductance.

Authors:  T M Miller; D A Goodenough
Journal:  J Cell Biol       Date:  1985-11       Impact factor: 10.539

9.  Calmodulin Directly Interacts with the Cx43 Carboxyl-Terminus and Cytoplasmic Loop Containing Three ODDD-Linked Mutants (M147T, R148Q, and T154A) that Retain α-Helical Structure, but Exhibit Loss-of-Function and Cellular Trafficking Defects.

Authors:  Li Zheng; Sylvie Chenavas; Fabien Kieken; Andrew Trease; Sarah Brownell; Asokan Anbanandam; Paul L Sorgen; Gaelle Spagnol
Journal:  Biomolecules       Date:  2020-10-17

Review 10.  Regulation of Connexin Gap Junctions and Hemichannels by Calcium and Calcium Binding Protein Calmodulin.

Authors:  Zhengping Hu; Manuel A Riquelme; Sumin Gu; Jean X Jiang
Journal:  Int J Mol Sci       Date:  2020-11-02       Impact factor: 5.923

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