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Inwardly rectifying potassium channels: their structure, function, and physiological roles.
The crystal structure of different Kir channels is opening the way to understanding the structure-function relationships of this simple but diverse ion channel family.
A Novel Sulfonylurea Receptor Forms with BIR (Kir6.2) a Smooth Muscle Type ATP-sensitive K+ Channel*
The reverse transcription-polymerase chain reaction analysis showed that mRNA of this clone was ubiquitously expressed in diverse tissues, including brain, heart, liver, urinary bladder, and skeletal muscle, suggesting that this novel isoform of sulfonylurea receptor is a subunit reconstituting the smooth muscle KATP channel.
Sulphonylurea receptor 2B and Kir6.1 form a sulphonylurea‐sensitive but ATP‐insensitive K+ channel.
The K+ channel composed of the sulphonylurea receptor 2B and an inwardly rectifying K+Channel subunit Kir6.1 is not a classical ATP‐sensitive K+channel but closely resembles the nucleotide diphosphate‐dependent K+ channels in vascular smooth muscle cells.
Immunogold evidence suggests that coupling of K+ siphoning and water transport in rat retinal Müller cells is mediated by a coenrichment of Kir4.1 and AQP4 in specific membrane domains
By its highly differentiated distribution of AQP4, the Müller cell may be able to direct the water flux to select extracellular compartments while protecting others (the subretinal space) from inappropriate volume changes.
An inwardly rectifying K(+) channel, Kir4.1, expressed in astrocytes surrounds synapses and blood vessels in brain.
Data suggest that Kir4.1 is expressed in a limited population of brain astrocytes and may play a specific role in the glial K(+)-buffering action.
G protein regulation of potassium ion channels.
Upon stimulation of vagal nerves, acetylcholine (ACh)c is released from axonal terminals and decelerates the heart beat and established the concept of chemical synaptic transmission.
The βγ subunits of GTP-binding proteins activate the muscarinic K+ channel in heart
Single-channel current measurements unexpectedly indicate that the βγ, and not the a subunits, are responsible for activating the muscarinic-gated potassium channel.
International Union of Pharmacology. LIV. Nomenclature and Molecular Relationships of Inwardly Rectifying Potassium Channels
Since the initial cDNA cloning of the first inward rectifiers Kir1.1 (ROMK1) and Kir2.1 (IRK1) in 1993, a succession of new members of this family have been identified, including the G
A Novel ATP-dependent Inward Rectifier Potassium Channel Expressed Predominantly in Glial Cells (*)
This is the first description of the cloning of a glial cell inward rectifier potassium channel, which may be responsible for K+ buffering action of glial cells in the brain.