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Biochemistry Insights

Synopsis: An open access, peer reviewed electronic journal that covers biochemistry.


Indexing: Two major databases. Pubmed indexing for NIH-funded research.

Processing time: Decision in 2 weeks for 90% of papers.

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About this journal

Aims and scope:

Biochemistry Insights is a peer-reviewed, open-access online journal encompassing all topics within the field of biochemistry. This includes the chemistry, structure and functionality of proteins, carbohydrates, lipids, nucleic acids and smaller molecular components of cells and tissues. Cell metabolism, genomes, protein synthesis, cell signalling, transportation, and signal transduction are included but are not exclusive subjects. The journal also accepts articles on related topics applicable to this area, such as technology, outcomes, techniques and applications.

Editorial standards and procedures:

Submissions, excluding editorials, letters to the editor and dedications, will be peer reviewed by two reviewers.  Reviewers are required to provide fair, balanced and constructive reports.  

Under our Fairness in Peer Review Policy authors may appeal against reviewers' recommendations which are ill-founded, unobjective or unfair.  Appeals are considered by the Editor in Chief or Associate Editor.

Papers are not sent to peer reviewers following submission of a revised manuscript. Editorial decisions on re-submitted papers are based on the author's response to the initial peer review report.

Indexing:

This journal is indexed by:

  • CAS 
  • DOAJ
National Institutes of Health Public Access Policy compliant:

As of April 7 2008, the US NIH Public Access Policy requires that all peer reviewed articles resulting from research carried out with NIH funding be deposited in the Pubmed Central archive.

If you are an NIH employee or grantee Libertas Academica will ensure that you comply with the policy by depositing your paper at Pubmed Central on your behalf. 

ISSN: 1178-6264


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A Novel Mechanism in Regulating the Alpha-Subunit of the Epithelial Sodium Channel (α ENaC) by the Alternatively Spliced Form α ENaC-b

Authors: Marlene F. Shehata
Publication Date: 15 Apr 2009
Biochemistry Insights 2009:2 21-27

Marlene F. Shehata

Department of Cellular and Molecular Medicine, Faculty of Medicine, University of Ottawa, Ottawa ON, Canada.

Abstract

Introduction:  In Dahl rats’ kidney cortex, the alternatively spliced form of the epithelial sodium channel α subunit (α ENaC-b) is the most abundant mRNA transcript (32+/-3 fold    α ENaC-wt) as was investigated by quantitative RT-PCR analysis. α ENaC-b mRNA levels were significantly higher in Dahl R versus S rats, and were further augmented by high salt diet.

Objectives: In the present study, we described the molecular cloning and searched for a possible role of α ENaC-b by testing its potential expression in COS7 cells as well as its impact on α ENaC-wt expression levels when co-expressed in COS7 cells in a dose-dependent manner.

Methods: Using RT-PCR strategy, the full-length wildtype α ENaC transcript and the alternatively spliced form α ENaC-b were amplified, sequenced, cloned, subcloned into PCMV-sport6 expression vector, expressed and co-expressed into COS7 cells in a dose-dependent manner. A combination of denaturing and native western blotting techniques was employed to examine the expression of α ENaC-b in vitro, and to determine if an interaction between α ENaC-b and α ENaC-wt occurs in vitro, and finally to demonstrate if degradation of α ENaC-wt protein does occur.

Results:  α ENaC-b is translated in COS7 cells. Co-expression of α ENaC-b together with α ENaC-wt reduced α ENaC-wt levels in a dose-dependent manner. α ENaC-wt and α ENaC-b appear to form a complex that enhances the degradation of α ENaC-wt.

Conclusions:  Western blots suggest a novel mechanism in α ENaC regulation whereby α ENaC-b exerts a dominant negative effect on α ENaC-wt expression. This is potentially by sequestering α ENaC-wt, enhancing its proteolytic degradation, and possibly explaining the mechanism of salt-resistance in Dahl R rats.

Categories: Biochemistry


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