Referenced in: Kv5.1

Automatically associated channels: Kv2.1 , Kv5.1 , Kv6.1 , Kv6.2 , Kv6.3 , Slo1

Title: Properties and molecular basis of the mouse urinary bladder voltage-gated K+ current.

Authors: Kevin S Thorneloe, Mark T Nelson

Journal, date & volume: J. Physiol. (Lond.), 2003 May 15 , 549, 65-74

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/12679374

Abstract
Potassium channels play an important role in controlling the excitability of urinary bladder smooth muscle (UBSM). Here we describe the biophysical, pharmacological and molecular properties of the mouse UBSM voltage-gated K+ current (IK(V)). The IK(V) activated, deactivated and inactivated slowly with time constants of 29.9 ms at +30 mV, 131 ms at -40 mV and 3.4 s at +20 mV. The midpoints of steady-state activation and inactivation curves were 1.1 mV and -61.4 mV, respectively. These properties suggest that IK(V) plays a role in regulating the resting membrane potential and contributes to the repolarization and after-hyperpolarization phases of action potentials. The IK(V) was blocked by tetraethylammonium ions with an IC50 of 5.2 mM and was unaffected by 1 mM 4-aminopyridine. RT-PCR for voltage-gated K+ channel (KV) subunits revealed the expression of Kv2.1, Kv5.1, Kv6.1, Kv6.2 and Kv6.3 in isolated UBSM myocytes. A comparison of the biophysical properties of UBSM IK(V) with those reported for Kv2.1 and Kv5.1 and/or Kv6 heteromultimeric channels demonstrated a marked similarity. We propose that heteromultimeric channel complexes composed of Kv2.1 and Kv5.1 and/or Kv6 subunits form the molecular basis of the mouse UBSM IK(V).