Molecular characterization of the epithelial Na-K-Cl cotransporter isoforms.
Recent advances in the molecular characterization of specific isoforms of the Na-K-Cl cotransporter have allowed rapid progress in the study of the structure, function, and regulation of these members of a family of Cl-dependent cation cotransporters. Two distinct isoforms have been identified, one from Cl(-)-secretory epithelia and another found specifically in the diluting segment of the vertebrate kidney, a Cl(-)-absorptive epithelium. The discovery of three alternatively spliced variants of the absorptive isoform, which differ only by 31 amino acids and which appear to be differentially distributed within the mammalian thick ascending limb of the loop of Henle, highlight this spliced region as an important functional component of the protein.
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D002712:Chlorides / Q000378:metabolism*; D004848:Epithelium / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D011188:Potassium / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism*; D028021:Sodium-Potassium-Chloride Symporters; D013329:Structure-Activity Relationship
D002352:Carrier Proteins; D002712:Chlorides; D008565:Membrane Proteins; D028021:Sodium-Potassium-Chloride Symporters; D012964:Sodium; D011188:Potassium