TY - JOUR
T1 - Trypsin-sensitive, rapid inactivation of calcium-activated potassium channel
AU - Solaro, Christopher R.
AU - Lingle, Christopher J.
PY - 1992
Y1 - 1992
N2 - Most calcium-activated potassium channels couple changes in intracellular calcium to membrane excitability by conducting a current with a probability that depends directly on submembrane calcium concentration. In rat adrenal chromaffin cells, however, a large conductance, voltage- and calcium-activated potassium channel (BK) undergoes rapid inactivation, suggesting that this channel has a physiological role different than that of other BK channels. The inactivation of the BK channel, like that of the voltage-gated Shaker B potassium channel, is removed by trypsin digestion and channels are blocked by the Shaker B amino-terminal inactivating domain. Thus, this BK channel shares functional and possibly structural homologies with other inactivating voltage-gated potassium channels.
AB - Most calcium-activated potassium channels couple changes in intracellular calcium to membrane excitability by conducting a current with a probability that depends directly on submembrane calcium concentration. In rat adrenal chromaffin cells, however, a large conductance, voltage- and calcium-activated potassium channel (BK) undergoes rapid inactivation, suggesting that this channel has a physiological role different than that of other BK channels. The inactivation of the BK channel, like that of the voltage-gated Shaker B potassium channel, is removed by trypsin digestion and channels are blocked by the Shaker B amino-terminal inactivating domain. Thus, this BK channel shares functional and possibly structural homologies with other inactivating voltage-gated potassium channels.
UR - http://www.scopus.com/inward/record.url?scp=0026733206&partnerID=8YFLogxK
U2 - 10.1126/science.1529355
DO - 10.1126/science.1529355
M3 - Article
C2 - 1529355
AN - SCOPUS:0026733206
SN - 0036-8075
VL - 257
SP - 1694
EP - 1698
JO - Science
JF - Science
IS - 5077
ER -