Referenced in: none

Automatically associated channels: BKβ1 , Slo1

Title: Cloning and expression of the large-conductance Ca(2+)-activated K+ channel from colonic smooth muscle.

Authors: F Vogalis, T Vincent, I Qureshi, F Schmalz, M W Ward, K M Sanders, B Horowitz

Journal, date & volume: Am. J. Physiol., 1996 Oct , 271, G629-39

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/8897882

Abstract
We have cloned cDNAs encoding the alpha- and beta-subunits of a large-conductance Ca(2+)-activated K+ channel (BK channel) from canine colonic smooth muscle (cslo-alpha and cslo-beta). Nucleotide sequence homology of cslo-alpha with mslo and dslo suggests that it is the canine homologue of these genes. The carboxy-terminal end of the protein is the most diverse between species, and we have also found alternative exons in cslo-alpha in this region. We have identified a unique splice site in the carboxy-terminal region of cslo-alpha, which we term site 5. Northern analysis demonstrates expression of both alpha- and beta-subunits in all canine vascular and visceral smooth muscles tested. Expression of alpha-1 alone and alpha + beta-subunit cRNA in Xenopus oocytes results in a Ca(2+)- and voltage-dependent conductance. The activity of alpha/beta-channels, measured as either changes in the voltage of half-maximal activation (V0.5) in open probability (NP0) or in the normalized conductance (G/Cmax), was more sensitive to [Ca2+]free than channels composed of the alpha-subunit alone. Neither alpha- nor alpha/beta-channels expressed in membrane patches of Xenopus oocytes were found to be regulated by protein kinase G.