The interaction of ryanoids with individual ryanodine receptor channels

Ryanodine binds with high affinity and specificity to a class of Ca2+-release channels known as ryanodine receptors (RyR). The interaction with RyR results in a dramatic alteration in function with open probability (Po) increasing markedly and rates of ion translocation modified. We have investigate...

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Autores principales:	WILLIAMS,ALAN J, TANNA,BHAVNA
Lenguaje:	English
Publicado:	Sociedad de Biología de Chile 2004
Materias:	calcium Ca2+-release channel sarcoplasmic reticulum ryanodine single channel
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400006
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spelling	oai:scielo:S0716-976020040004000062005-06-02The interaction of ryanoids with individual ryanodine receptor channelsWILLIAMS,ALAN JTANNA,BHAVNA calcium Ca2+-release channel sarcoplasmic reticulum ryanodine single channel Ryanodine binds with high affinity and specificity to a class of Ca2+-release channels known as ryanodine receptors (RyR). The interaction with RyR results in a dramatic alteration in function with open probability (Po) increasing markedly and rates of ion translocation modified. We have investigated the features of ryanodine that govern the interaction of the ligand with RyR and the mechanisms underlying the subsequent alterations in function by monitoring the effects of congeners and derivatives of ryanodine (ryanoids) on individual RyR2 channels. While the interaction of all tested ryanoids results in an increased Po, the amplitude of the modified conductance state depends upon the structure of the ryanoid. We propose that different rates of cation translocation observed in the various RyR-ryanoid complexes represent different conformations of the channel stabilized by specific conformers of the ligand. On the time scale of a single channel experiment ryanodine binds irreversibly to the channel. However, alterations in structure yield some ryanoids with dissociation rate constants orders of magnitude greater than ryanodine. The probability of occurrence of the RyR-ryanoid complex is sensitive to trans-membrane voltage, with the vast majority of the influence of potential arising from a voltage-driven alteration in the affinity of the ryanoid-binding site.info:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.37 n.4 20042004-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400006en10.4067/S0716-97602004000400006
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	calcium Ca2+-release channel sarcoplasmic reticulum ryanodine single channel
spellingShingle	calcium Ca2+-release channel sarcoplasmic reticulum ryanodine single channel WILLIAMS,ALAN J TANNA,BHAVNA The interaction of ryanoids with individual ryanodine receptor channels
description	Ryanodine binds with high affinity and specificity to a class of Ca2+-release channels known as ryanodine receptors (RyR). The interaction with RyR results in a dramatic alteration in function with open probability (Po) increasing markedly and rates of ion translocation modified. We have investigated the features of ryanodine that govern the interaction of the ligand with RyR and the mechanisms underlying the subsequent alterations in function by monitoring the effects of congeners and derivatives of ryanodine (ryanoids) on individual RyR2 channels. While the interaction of all tested ryanoids results in an increased Po, the amplitude of the modified conductance state depends upon the structure of the ryanoid. We propose that different rates of cation translocation observed in the various RyR-ryanoid complexes represent different conformations of the channel stabilized by specific conformers of the ligand. On the time scale of a single channel experiment ryanodine binds irreversibly to the channel. However, alterations in structure yield some ryanoids with dissociation rate constants orders of magnitude greater than ryanodine. The probability of occurrence of the RyR-ryanoid complex is sensitive to trans-membrane voltage, with the vast majority of the influence of potential arising from a voltage-driven alteration in the affinity of the ryanoid-binding site.
author	WILLIAMS,ALAN J TANNA,BHAVNA
author_facet	WILLIAMS,ALAN J TANNA,BHAVNA
author_sort	WILLIAMS,ALAN J
title	The interaction of ryanoids with individual ryanodine receptor channels
title_short	The interaction of ryanoids with individual ryanodine receptor channels
title_full	The interaction of ryanoids with individual ryanodine receptor channels
title_fullStr	The interaction of ryanoids with individual ryanodine receptor channels
title_full_unstemmed	The interaction of ryanoids with individual ryanodine receptor channels
title_sort	interaction of ryanoids with individual ryanodine receptor channels
publisher	Sociedad de Biología de Chile
publishDate	2004
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400006
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The interaction of ryanoids with individual ryanodine receptor channels

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