Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/12952
ชื่อเรื่อง: P2Y receptor regulation of K2p channels that facilitate K + secretion by human mammary epithelial cells
ผู้แต่ง: Srisomboon Y.
Zaidman N.A.
Maniak P.J.
Deachapunya C.
O’Grady S.M.
Keywords: epithelial sodium channel
KCa3.1 channel
messenger RNA
potassium channel
protein kinase C
purinergic P2Y receptor
TASK1 channel
TASK3 channel
TREK1 channel
TREK2 channel
TWIK1 channel
two pore potassium channel
unclassified drug
epithelial sodium channel
potassium
potassium channel blocking agent
protein kinase C
purinergic P2Y receptor
purinergic P2Y receptor agonist
sodium
tandem pore domain potassium channel
uridine triphosphate
apical membrane
Article
breast epithelium cell
cellular distribution
controlled study
human
human cell
immunocytochemistry
lipid raft
membrane current
potassium transport
priority journal
reverse transcription polymerase chain reaction
sodium absorption
sodium transport
voltage clamp technique
antagonists and inhibitors
cytology
drug effect
epithelium cell
female
genetics
mammary gland
membrane potential
metabolism
secretory pathway
transformed cell line
Cell Line, Transformed
Epithelial Cells
Epithelial Sodium Channels
Female
Humans
Mammary Glands, Human
Membrane Potentials
Potassium
Potassium Channel Blockers
Potassium Channels, Tandem Pore Domain
Protein Kinase C
Purinergic P2Y Receptor Agonists
Receptors, Purinergic P2Y
Secretory Pathway
Sodium
Uridine Triphosphate
วันที่เผยแพร่: 2018
บทคัดย่อ: The objective of this study was to determine the molecular identity of ion channels involved in K + secretion by the mammary epithelium and to examine their regulation by purinoceptor agonists. Apical membrane voltage-clamp experiments were performed on human mammary epithelial cells where the basolateral membrane was exposed to the pore-forming antibiotic amphotericin B dissolved in a solution with intracellular-like ionic composition. Addition of the Na + channel inhibitor benzamil reduced the basal current, consistent with inhibition of Na + uptake across the apical membrane, whereas the K Ca 3.1 channel blocker TRAM-34 produced an increase in current resulting from inhibition of basal K + efflux. Treatment with two-pore potassium (K2P) channel blockers quinidine, bupivacaine and a selective TASK1/TASK3 inhibitor (PK-THPP) all produced concentration-dependent inhibition of apical K + efflux. qRT-PCR experiments detected mRNA expression for nine K2P channel subtypes. Western blot analysis of biotinylated apical membranes and confocal immunocytochemistry revealed that at least five K2P subtypes (TWIK1, TREK1, TREK2, TASK1, and TASK3) are expressed in the apical membrane. Apical UTP also increased the current, but pretreatment with the PKC inhibitor GF109203X blocked the response. Similarly, direct activation of PKC with phorbol 12-myristate 13-acetate produced a similar increase in current as observed with UTP. These results support the conclusion that the basal level of K + secretion involves constitutive activity of apical K Ca 3.1 channels and multiple K2P channel subtypes. Apical UTP evoked a transient increase in K Ca 3.1 channel activity, but over time caused persistent inhibition of K2P channel function leading to an overall decrease in K + secretion. © 2018 the American Physiological Society.
URI: https://ir.swu.ac.th/jspui/handle/123456789/12952
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85061338059&doi=10.1152%2fajpcell.00342.2016&partnerID=40&md5=bdef96ce851b2a809fb5a5467a79a6e0
ISSN: 3636143
Appears in Collections:Scopus 1983-2021

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