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Biochem Biophys Res Commun. 2005 Dec 2;337(4):1072-9. Epub 2005 Oct 5.

Probing luminal negative charge in the type 3 ryanodine receptor.

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The Laboratory of Functional Immunogenetics, The Babraham Institute, Cambridge CB2 4AT, UK.


In this study, we have investigated block of potassium (K(+)) current by neomycin, a large polycation, from the luminal face of the type 3 ryanodine receptor (RyR3). Previous studies have shown that neomycin is an open channel blocker of RyR2 that interacts with negatively charged residues in the mouth of the conduction pathway to partially occlude it. In the current study, we have used neomycin as a probe to investigate proposed negatively charged regions in the luminal pore mouth of RyR3. Luminal neomycin induces concentration- and voltage-dependent partial block to a subconductance state in RyR3. Blocking parameters calculated in this study show that neomycin has a higher affinity for RyR3 than RyR2, but block may occur at the same site within the pore mouth. The change in affinity may be due to altered negative charge density at the site of interaction.

[Indexed for MEDLINE]

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