Molecular analysis of subtype-selective inhibition of cloned KATP channels by PNU-37883A

University of Manchester (2003) J Physiol 552P, P54

Communications: Molecular analysis of subtype-selective inhibition of cloned KATP channels by PNU-37883A

H. Kuhlman*, J.M. Quayle†, T. Kamishim*† and D. Lodwick*

*Department of Medicine, University of Leicester, Clinical Sciences Building, Leicester LE2 7LX and †Department of Human Anatomy and Cell Biology, University of Liverpool, Ashton Street, Liverpool L69 3GE, UK

View other abstracts by:


PNU-37883A inhibits vascular KATP channels (Wellman et al. 1999). It is selective for Kir6.1 over Kir6.2, and Kir6.1 may therefore form the pore of arterial KATP channels (Surah-Narwal et al. 1999; Kovalev et al. 2001). However, in some systems PNU-37883A cannot distinguish between different KATP channel subtypes (Cui et al. 2003). In this study, we have used Kir6.1/Kir6.2 chimeric proteins and current recordings to further investigate the basis of PNU-37883A inhibition of cloned KATP channels.

Chimeras between rat Kir6.1 and Kir6.2 were made by site-directed mutagenesis and subcloning. Channels were expressed following RNA injection into Xenopus oocytes. Membrane current was recorded by two-microelectrode voltage clamp of whole oocytes in a 98 mM K+ extracellular solution and at a membrane potential of -60 mV. Kir6.x constructs were co-expressed with either SUR1 or SUR2B, and currents were induced by 100 µM pinacidil (for SUR2B) or 100 µM diazoxide and 10 µM carbonyl cyanide m-chlorophenyl-hydrazone (for SUR1). Solutions and drugs were delivered by chamber perfusion (flow rate, 2 ml min-1; chamber vol., 200 µl). Kir6.1, Kir6.2, and chimeras between Kir6.1 and Kir6.2 were expressed with SUR2B, and fractional inhibition by 10 µM PNU-37883A reported.

Channels containing Kir6.1 were more sensitive to inhibition than those containing Kir6.2 (fractional inhibition: means ± S.E.M., 0.70 ± 0.05, n = 10, cf. 0.07 ± 0.03, n = 5). A chimeric channel with the Kir6.1 pore and the Kir6.2 intracellular N and C terminal domains was PNU-37883A insensitive (0.06 ± 0.07, n = 5). A chimera with the Kir6.1 C terminus and Kir6.2 N terminus and pore was inhibited (0.48 ± 0.04, n = 5). These results, and those obtained with other chimeras, suggest the C terminus is an important determinant of PNU-37883A inhibition by Kir6.1. Similar results were seen when constructs were co-expressed with SUR1. Further chimeric constructs localised PNU-37883A sensitivity to an 87 amino acid residue-long section in the Kir6.1C terminus.

Our data show structural differences between Kir6.1 and Kir6.2 are important in determining sensitivity to PNU-37883A. This compound may prove useful in probing structural and functional differences between the two channel subtypes.

Helen Kuhlman was a British Heart Foundation PhD student (FS/98047).



Where applicable, experiments conform with Society ethical requirements.

Site search

Filter

Content Type