Document Type

Article

Version Deposited

Published Version

Publication Date

9-27-2002

Publication Title

Journal of Biological Chemistry

DOI

10.1074/jbc.M109797200

Abstract

Gap junctions, composed of proteins from the connexin family, are the only channels that directly connect the cytoplasm of adjacent cells to allow for the intercellular transfer of small hydrophilic molecules. Gap junctional communication is essential for proper development and health in animals and humans. Whereas the study of biological molecules that pass through gap junctions is extremely important, the identification of endogenous transjunctional metabolites is challenging. To help address this problem, we have developed a layered culture system to identify and quantitate the transfer of endogenous molecules that pass between cells through gap junctions. Using these techniques, we have identified several endogenous molecules that showed differential transfer between channels composed of Cx32 versus Cx43. For example, adenosine passed about 12-fold better through channels formed by Cx32. In contrast, AMP and ADP passed about 8-fold better, and ATP greater than 300-fold better, through channels formed by Cx43. Thus, addition of phosphate to adenosine appears to shift its relative permeability from channels formed by Cx32 to channels formed by Cx43. This suggests functional consequence because the energy status of a cell could be controlled via connexin expression and channel formation.

Comments

American Society of Biochemistry and Molecular Biology

Permitted :

- to post the accepted manuscript version of the work, the “Paper in Press,” on the author’s personal web page, their personal or institutional repository, or their funding body’s archive or designated noncommercial repository, provided that a link to the article in the journal

- post the final edited PDFs, created by ASBMB, to their own departmental/university websites, provided that the posting does not happen until 12 months after publication, and that a link to the article in the journal is included.

Published Citation

Goldberg GS, Moreno AP, Lampe PD. Gap junctions between cells expressing connexin 43 or 32 show inverse permselectivity to adenosine and ATP. J Biol Chem. 2002 Sep 27;277(39):36725-30. Epub 2002 Jul 15. doi: 10.1074/jbc.M109797200. PMID: 12119284.

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