An intermediate-conductance Ca2+-activated K+ channel is important for secretion in pancreatic duct cells
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An intermediate-conductance Ca2+-activated K+ channel is important for secretion in pancreatic duct cells. / Hayashi, Mikio; Wang, Jing; Hede, Susanne Edeling; Novak, Ivana.
In: American Journal of Physiology: Cell Physiology, Vol. 303, No. 2, 2012, p. C151-C159.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - An intermediate-conductance Ca2+-activated K+ channel is important for secretion in pancreatic duct cells
AU - Hayashi, Mikio
AU - Wang, Jing
AU - Hede, Susanne Edeling
AU - Novak, Ivana
PY - 2012
Y1 - 2012
N2 - Potassium channels play a vital role in maintaining the membrane potential and the driving force for anion secretion in epithelia. In pancreatic ducts, which secrete bicarbonate-rich fluid, the identity of K(+) channels has not been extensively investigated. In this study, we investigated the molecular basis of functional K(+) channels in rodent and human pancreatic ducts (Capan-1, PANC-1, and CFPAC-1) using molecular and electrophysiological techniques. RT-PCR analysis revealed mRNAs for KCNQ1, KCNH2, KCNH5, KCNT1, and KCNT2, as well as KCNN4 coding for the following channels: KVLQT1; HERG; EAG2; Slack; Slick; and an intermediate-conductance Ca(2+)-activated K(+) (IK) channel (K(Ca)3.1). The following functional studies were focused on the IK channel. 5,6-Dichloro-1-ethyl-1,3-dihydro-2H-benzimidazole-2-one (DC-EBIO), an activator of IK channel, increased equivalent short-circuit current (I(sc)) in Capan-1 monolayer, consistent with a secretory response. Clotrimazole, a blocker of IK channel, inhibited I(sc). IK channel blockers depolarized the membrane potential of cells in microperfused ducts dissected from rodent pancreas. Cell-attached patch-clamp single-channel recordings revealed IK channels with an average conductance of 80 pS in freshly isolated rodent duct cells. These results indicated that the IK channels may, at least in part, be involved in setting the resting membrane potential. Furthermore, the IK channels are involved in anion and potassium transport in stimulated pancreatic ducts.
AB - Potassium channels play a vital role in maintaining the membrane potential and the driving force for anion secretion in epithelia. In pancreatic ducts, which secrete bicarbonate-rich fluid, the identity of K(+) channels has not been extensively investigated. In this study, we investigated the molecular basis of functional K(+) channels in rodent and human pancreatic ducts (Capan-1, PANC-1, and CFPAC-1) using molecular and electrophysiological techniques. RT-PCR analysis revealed mRNAs for KCNQ1, KCNH2, KCNH5, KCNT1, and KCNT2, as well as KCNN4 coding for the following channels: KVLQT1; HERG; EAG2; Slack; Slick; and an intermediate-conductance Ca(2+)-activated K(+) (IK) channel (K(Ca)3.1). The following functional studies were focused on the IK channel. 5,6-Dichloro-1-ethyl-1,3-dihydro-2H-benzimidazole-2-one (DC-EBIO), an activator of IK channel, increased equivalent short-circuit current (I(sc)) in Capan-1 monolayer, consistent with a secretory response. Clotrimazole, a blocker of IK channel, inhibited I(sc). IK channel blockers depolarized the membrane potential of cells in microperfused ducts dissected from rodent pancreas. Cell-attached patch-clamp single-channel recordings revealed IK channels with an average conductance of 80 pS in freshly isolated rodent duct cells. These results indicated that the IK channels may, at least in part, be involved in setting the resting membrane potential. Furthermore, the IK channels are involved in anion and potassium transport in stimulated pancreatic ducts.
KW - Animals
KW - Cells, Cultured
KW - Female
KW - Humans
KW - Intermediate-Conductance Calcium-Activated Potassium Channels
KW - Male
KW - Membrane Potentials
KW - Mice
KW - Mice, Inbred BALB C
KW - Mice, Inbred C57BL
KW - Pancreatic Ducts
KW - Potassium Channel Blockers
KW - Rats
KW - Rats, Wistar
U2 - 10.1152/ajpcell.00089.2012
DO - 10.1152/ajpcell.00089.2012
M3 - Journal article
C2 - 22555847
VL - 303
SP - C151-C159
JO - American Journal of Physiology: Cell Physiology
JF - American Journal of Physiology: Cell Physiology
SN - 0363-6143
IS - 2
ER -
ID: 43855262