Kinetic interconversion of rat and bovine homologs of the α subunit of an amiloride-sensitive Na+ channel by C-terminal truncation of the bovine subunit

Catherine M. Fuller, Iskander I. Ismailov, Bakhram K. Berdiev, Vadim G. Shlyonsky, Dale J. Benos

Research output: Contribution to journalArticle

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Abstract

We have recently cloned the α subunit of a bovine amiloride-sensitive Na+ channel (αbENaC). This subunit shares extensive homology with both rat and human αENaC subunits but shows marked divergence at the C terminus beginning at amino acid 584 of the 697-residue sequence. When incorporated into planar lipid bilayers, αbENaC almost exclusively exhibits a main transition to 39 picosiemens (pS) with very rare 13 pS step transitions to one of two subconductance states (26 and 13 pS). In contrast, the α subunit of the rat renal homolog of ENaC (αrENaC) has a main transition step to 13 pS that is almost constituitively open, with a second stepwise transition of 26 to 39 pS. A deletion mutant of αbENaC, encompassing the entire C- terminal region (R567X), converts the kinetic behavior of αbENaC to that of αrENaC, i.e. a transition to 13 pS followed by a second 26 pS transition to 39 pS. Chemical cross-linking of R567X restores the wild-type αbENaC gating pattern, whereas treatment with the reducing agent dithiothreitol produced only 13 pS transitions. In contrast, an equivalent C-terminal truncation of αerENaC (R613X) had no effect on the gating pattern of αrENaC. These results are consistent with the hypothesis that interactions between the C termini of αbENaC account for the different kinetic behavior of this member of the ENaC family of Na+ channels.

Original languageEnglish
Pages (from-to)26602-26608
Number of pages7
JournalJournal of Biological Chemistry
Volume271
Issue number43
DOIs
Publication statusPublished - 1996
Externally publishedYes

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Amiloride
Rats
Kinetics
Kidney
Lipid bilayers
Dithiothreitol
Reducing Agents
Lipid Bilayers
Amino Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kinetic interconversion of rat and bovine homologs of the α subunit of an amiloride-sensitive Na+ channel by C-terminal truncation of the bovine subunit. / Fuller, Catherine M.; Ismailov, Iskander I.; Berdiev, Bakhram K.; Shlyonsky, Vadim G.; Benos, Dale J.

In: Journal of Biological Chemistry, Vol. 271, No. 43, 1996, p. 26602-26608.

Research output: Contribution to journalArticle

Fuller, Catherine M. ; Ismailov, Iskander I. ; Berdiev, Bakhram K. ; Shlyonsky, Vadim G. ; Benos, Dale J. / Kinetic interconversion of rat and bovine homologs of the α subunit of an amiloride-sensitive Na+ channel by C-terminal truncation of the bovine subunit. In: Journal of Biological Chemistry. 1996 ; Vol. 271, No. 43. pp. 26602-26608.
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abstract = "We have recently cloned the α subunit of a bovine amiloride-sensitive Na+ channel (αbENaC). This subunit shares extensive homology with both rat and human αENaC subunits but shows marked divergence at the C terminus beginning at amino acid 584 of the 697-residue sequence. When incorporated into planar lipid bilayers, αbENaC almost exclusively exhibits a main transition to 39 picosiemens (pS) with very rare 13 pS step transitions to one of two subconductance states (26 and 13 pS). In contrast, the α subunit of the rat renal homolog of ENaC (αrENaC) has a main transition step to 13 pS that is almost constituitively open, with a second stepwise transition of 26 to 39 pS. A deletion mutant of αbENaC, encompassing the entire C- terminal region (R567X), converts the kinetic behavior of αbENaC to that of αrENaC, i.e. a transition to 13 pS followed by a second 26 pS transition to 39 pS. Chemical cross-linking of R567X restores the wild-type αbENaC gating pattern, whereas treatment with the reducing agent dithiothreitol produced only 13 pS transitions. In contrast, an equivalent C-terminal truncation of αerENaC (R613X) had no effect on the gating pattern of αrENaC. These results are consistent with the hypothesis that interactions between the C termini of αbENaC account for the different kinetic behavior of this member of the ENaC family of Na+ channels.",
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AU - Benos, Dale J.

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