Field | Value |
dc.contributor.author | Shehata, Marlene F. |
dc.date.accessioned | 2010-08-30T17:53:07Z |
dc.date.available | 2010-08-30T17:53:07Z |
dc.date.created | 2010 |
dc.date.issued | 2010-08-30T17:53:07Z |
dc.identifier.uri | http://hdl.handle.net/10393/19597 |
dc.description.abstract | 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. |
dc.language.iso | en |
dc.title | The alternatively spliced form "b" of the Epithelial Sodium Channel α subunit (α ENaC): Any prior evidence of its existence? |
dc.type | Article |
Collection | Médecine cellulaire et moléculaire // Cellular and Molecular Medicine Publications en libre accès financées par uOttawa // uOttawa financed open access publications
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