Literature DB >> 1320431

The crystalline lens. A system networked by gap junctional intercellular communication.

D A Goodenough1.   

Abstract

The vertebrate eye lens is a solid cyst of cells which grows throughout life by addition of new cells at the surface. The older cells, buried by the newer generations, differentiate into long, prismatic fibers, losing their cellular organelles and filling their cytoplasms with high concentrations of soluble proteins, the crystallins. The long-lived lens fibers are interconnected by gap junctions, both with themselves and with an anterior layer of simple cuboidal epithelial cells at the lens surface. This network of gap junctions joins the lens cells into a syncytium with respect to small molecules, permitting metabolic co-operation: intercellular diffusion of ions, metabolites, and water. In contact with nutrients at the lens surface, the epithelial cells retain their cellular organelles, and are able to provide the metabolic energy to maintain correct ion and metabolite concentrations within the lens fiber cytoplasms, such that the crystallins remain in solution and do not aggregate (cataract). Gap junctions are formed by a family of integral membrane channel-forming proteins called connexins. Gap junctions between lens epithelial cells are composed of a connexin which is common between many different cell types, notably myocardial cells and connective tissue fibroblasts. The gap junctions between epithelial cells and lens fibers have not yet been biochemically characterized. The gap junctions formed between lens fibers are composed of at least two different connexins, one of which has not been detected between other cell types. The unusual physiology and longevity of the lens fibers may require the special set of connexins which are found joining these cells.

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Year:  1992        PMID: 1320431     DOI: 10.1016/s1043-4682(10)80007-8

Source DB:  PubMed          Journal:  Semin Cell Biol        ISSN: 1043-4682


  69 in total

1.  Properties of gap junction channels formed by Cx46 alone and in combination with Cx50.

Authors:  M G Hopperstad; M Srinivas; D C Spray
Journal:  Biophys J       Date:  2000-10       Impact factor: 4.033

Review 2.  Structure of the gap junction channel and its implications for its biological functions.

Authors:  Shoji Maeda; Tomitake Tsukihara
Journal:  Cell Mol Life Sci       Date:  2010-10-21       Impact factor: 9.261

3.  A novel role for FGF and extracellular signal-regulated kinase in gap junction-mediated intercellular communication in the lens.

Authors:  A C Le; L S Musil
Journal:  J Cell Biol       Date:  2001-07-09       Impact factor: 10.539

Review 4.  Lens Biology and Biochemistry.

Authors:  J Fielding Hejtmancik; S Amer Riazuddin; Rebecca McGreal; Wei Liu; Ales Cvekl; Alan Shiels
Journal:  Prog Mol Biol Transl Sci       Date:  2015-06-04       Impact factor: 3.622

5.  Voltage gating and permeation in a gap junction hemichannel.

Authors:  E B Trexler; M V Bennett; T A Bargiello; V K Verselis
Journal:  Proc Natl Acad Sci U S A       Date:  1996-06-11       Impact factor: 11.205

Review 6.  Gap junctions or hemichannel-dependent and independent roles of connexins in cataractogenesis and lens development.

Authors:  J X Jiang
Journal:  Curr Mol Med       Date:  2010-12       Impact factor: 2.222

7.  Cross-talk between fibroblast growth factor and bone morphogenetic proteins regulates gap junction-mediated intercellular communication in lens cells.

Authors:  Bruce A Boswell; Pamela J Lein; Linda S Musil
Journal:  Mol Biol Cell       Date:  2008-04-09       Impact factor: 4.138

Review 8.  Connexins in lens development and cataractogenesis.

Authors:  Xiaohua Gong; Catherine Cheng; Chun-hong Xia
Journal:  J Membr Biol       Date:  2007-06-20       Impact factor: 1.843

9.  A novel role of gap junction connexin46 protein to protect breast tumors from hypoxia.

Authors:  Debarshi Banerjee; Gunjan Gakhar; Dan Madgwick; Amy Hurt; Dolores Takemoto; Thu Annelise Nguyen
Journal:  Int J Cancer       Date:  2010-08-15       Impact factor: 7.396

10.  Cataract-associated D3Y mutation of human connexin46 (hCx46) increases the dye coupling of gap junction channels and suppresses the voltage sensitivity of hemichannels.

Authors:  Barbara Schlingmann; Patrik Schadzek; Stefan Busko; Alexander Heisterkamp; Anaclet Ngezahayo
Journal:  J Bioenerg Biomembr       Date:  2012-07-28       Impact factor: 2.945

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