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Article Commentary: The Alternatively Spliced Form “b” of the Epithelial Sodium Channel α subunit (α ENaC): Any Prior Evidence of its Existence?
Author(s) -
Marlene Shehata
Publication year - 2010
Publication title -
clinical medicine insights cardiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.634
H-Index - 21
ISSN - 1179-5468
DOI - 10.4137/cmc.s5270
Subject(s) - epithelial sodium channel , protein subunit , messenger rna , alternative splicing , aldosterone , biology , medicine , endocrinology , microbiology and biotechnology , chemistry , sodium , gene , genetics , organic chemistry
The epithelial sodium channel (ENaC) is critical in maintaining sodium balance across aldosterone-responsive epithelia. ENaC is a combined channel formed of three subunits (αβγ) with α ENaC subunit being the most critical for channel functionality. In a previous report, we have demonstrated the existence and mRNA expression levels of four alternatively spliced forms of the α ENaC subunit denoted by -a, -b, -c and -d in kidney cortex of Dahl S and R rats. Of the four alternatively spliced forms presently identified, α ENaC-b is considered the most interesting for the following reasons: Aside from being a salt-sensitive transcript, α ENaC-b mRNA expression is ∼32 fold higher than α ENaC wildtype in kidney cortex of Dahl rats. Additionally, the splice site used to generate α ENaC-b is conserved across species. Finally, α ENaC-b mRNA expression is significantly higher in salt-resistant Dahl R rats versus salt-sensitive Dahl S rats. As such, this commentary aims to highlight some of the previously published research articles that described the existence of an additional protein band on α ENaC western blots that could account for α ENaC-b in other rat species.

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