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Interfering amino terminal peptides and functional implications for heteromeric gap junction formation

Overview of attention for article published in Frontiers in Pharmacology, January 2013
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Title
Interfering amino terminal peptides and functional implications for heteromeric gap junction formation
Published in
Frontiers in Pharmacology, January 2013
DOI 10.3389/fphar.2013.00067
Pubmed ID
Authors

Eric C. Beyer, Xianming Lin, Richard D. Veenstra

Abstract

Connexin43 (Cx43) is widely expressed in many different tissues of the human body. In cells of some organs, Cx43 is co-expressed with other connexins (Cx), including Cx46 and Cx50 in lens, Cx40 in atrium, Purkinje fibers, and the blood vessel wall, Cx45 in heart, and Cx37 in the ovary. Interactions with the co-expressed connexins may have profound functional implications. The abilities of Cx37, Cx45, Cx46, and Cx50 to function in heteromeric gap junction combinations with Cx43 are well documented. Different studies disagree regarding the ability of Cx43 and Cx40 to produce functional heteromeric gap junctions with each other. We review previous studies regarding the heteromeric interactions of Cx43. The possibility of negative functional interactions between the cytoplasmic pore-forming amino-terminal (NT) domains of these connexins was assessed using pentameric connexin sequence-specific NT domain [interfering NT (iNT)] peptides applied to cells expressing homomeric Cx40, Cx37, Cx45, Cx46, and Cx50 gap junctions. A Cx43 iNT peptide corresponding to amino acids 9-13 (Ac-KLLDK-NH2) specifically inhibited the electrical coupling of Cx40 gap junctions in a transjunctional voltage (V j)-dependent manner without affecting the function of homologous Cx37, Cx46, Cx50, and Cx45 gap junctions. A Cx40 iNT (Ac-EFLEE-OH) peptide counteracted the V j-dependent block of Cx40 gap junctions, whereas a similarly charged Cx50 iNT (Ac-EEVNE-OH) peptide did not, suggesting that these NT domain interactions are not solely based on electrostatics. These data are consistent with functional Cx43 heteromeric gap junction formation with Cx37, Cx45, Cx46, and Cx50 and suggest that Cx40 uniquely experiences functional suppressive interactions with a Cx43 NT domain sequence. These findings present unique functional implications about the heteromeric interactions between Cx43 and Cx40 that may influence cardiac conduction in atrial myocardium and the specialized conduction system.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 17 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 17 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 3 18%
Student > Doctoral Student 2 12%
Student > Bachelor 2 12%
Student > Master 2 12%
Student > Ph. D. Student 2 12%
Other 3 18%
Unknown 3 18%
Readers by discipline Count As %
Agricultural and Biological Sciences 9 53%
Biochemistry, Genetics and Molecular Biology 2 12%
Social Sciences 2 12%
Pharmacology, Toxicology and Pharmaceutical Science 1 6%
Medicine and Dentistry 1 6%
Other 0 0%
Unknown 2 12%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 21 May 2013.
All research outputs
#20,194,150
of 22,711,242 outputs
Outputs from Frontiers in Pharmacology
#9,922
of 15,939 outputs
Outputs of similar age
#248,752
of 280,734 outputs
Outputs of similar age from Frontiers in Pharmacology
#92
of 167 outputs
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