Molecular pharmacology of the CFTR Cl- channel.
Dysfunction of the cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel is associated with a wide spectrum of disease. In the search for modulators of CFTR, pharmacological agents that interact directly with the CFTR Cl- channel have been identified. Some agents stimulate CFTR by interacting with the nucleotide-binding domains that control channel gating, whereas others inhibit CFTR by binding within the channel pore and preventing Cl- permeation. Knowledge of the molecular pharmacology of CFTR might lead to new treatments for diseases caused by the dysfunction of CFTR.
Hwang
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Department of Physiology, Dalton Cardiovascular Research Center, University of Missouri-Columbia, Columbia, MO 65211, USA. dcrctch@showme.missouri.edu
Sheppard
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D018528:ATP-Binding Cassette Transporters / Q000737:chemistry / Q000187:drug effects*; D000818:Animals; D018118:Chloride Channels / Q000737:chemistry / Q000187:drug effects*; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000737:chemistry / Q000187:drug effects*; D006801:Humans
D018528:ATP-Binding Cassette Transporters; C505032:CFTR protein, human; D018118:Chloride Channels; C099627:mrp2 protein, Oryctolagus cuniculus; D019005:Cystic Fibrosis Transmembrane Conductance Regulator