Polyamine block of inwardly rectifying potassium channels.

Harley T. Kurata; Wayland W.L. Cheng; Colin G. Nichols

doi:10.1007/978-1-61779-034-8_6

Polyamine block of inwardly rectifying potassium channels.

Harley T. Kurata, Wayland W.L. Cheng, Colin G. Nichols

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Abstract

Polyamine blockade of inwardly rectifying potassium (Kir) channels underlies their steep voltage--dependence observed in native cells. The structural determinants of polyamine blockade and the structure-activity profile of endogenous polyamines requires specialized methodology for characterizing polyamine interactions with Kir channels. Recent identification and growing interest in the structure and function of prokaryotic Kir channels (KirBacs) has driven the development of new techniques for measuring ion channel activity. Several methods for measuring polyamine interactions with prokaryotic and eukaryotic Kir channels are discussed.

Original language	English
Pages (from-to)	113-126
Number of pages	14
Journal	Methods in molecular biology (Clifton, N.J.)
Volume	720
DOIs	https://doi.org/10.1007/978-1-61779-034-8_6
State	Published - 2011

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abstract = "Polyamine blockade of inwardly rectifying potassium (Kir) channels underlies their steep voltage--dependence observed in native cells. The structural determinants of polyamine blockade and the structure-activity profile of endogenous polyamines requires specialized methodology for characterizing polyamine interactions with Kir channels. Recent identification and growing interest in the structure and function of prokaryotic Kir channels (KirBacs) has driven the development of new techniques for measuring ion channel activity. Several methods for measuring polyamine interactions with prokaryotic and eukaryotic Kir channels are discussed.",

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AU - Cheng, Wayland W.L.

AU - Nichols, Colin G.

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AB - Polyamine blockade of inwardly rectifying potassium (Kir) channels underlies their steep voltage--dependence observed in native cells. The structural determinants of polyamine blockade and the structure-activity profile of endogenous polyamines requires specialized methodology for characterizing polyamine interactions with Kir channels. Recent identification and growing interest in the structure and function of prokaryotic Kir channels (KirBacs) has driven the development of new techniques for measuring ion channel activity. Several methods for measuring polyamine interactions with prokaryotic and eukaryotic Kir channels are discussed.

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JO - Methods in molecular biology (Clifton, N.J.)

JF - Methods in molecular biology (Clifton, N.J.)

ER -

Polyamine block of inwardly rectifying potassium channels.

Abstract

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