ABCMdb

PMID: 12475777

Proks P, Reimann F, Green N, Gribble F, Ashcroft F
Sulfonylurea stimulation of insulin secretion.
Diabetes. 2002 Dec;51 Suppl 3:S368-76., [PubMed]

Sentences

No. Mutations Sentence Comment

123 ABCC8 p.Ser1237Tyr The curves are fit to equation 2. beta-cell KATP channels, is not easily reversed in electrophysiological recordings, whereas glibenclamide block is rapidly reversed when SUR1 contains the S1237Y mutation. Login to comment 124 ABCC8 p.Ser1237Tyr The curves are fit to equation 2. beta-cell KATP channels, is not easily reversed in electrophysiological recordings, whereas glibenclamide block is rapidly reversed when SUR1 contains the S1237Y mutation. Login to comment 125 ABCC8 p.Ser1237Tyr In addition, glibenclamide binding to SUR1 is greatly decreased by the S1237Y mutation (35), whereas glibenclamide binding to SUR2B is enhanced by the reverse mutation (36,37). Login to comment 126 ABCC8 p.Ser1237Tyr In addition, glibenclamide binding to SUR1 is greatly decreased by the S1237Y mutation (35), whereas glibenclamide binding to SUR2B is enhanced by the reverse mutation (36,37). Login to comment 128 ABCC8 p.Ser1237Tyr The fact that glibenclamide blocks Kir6.2/SUR1-S1237Y channels indicates that residues other than S1237 are critical for binding of this drug. Login to comment 129 ABCC8 p.Ser1237Tyr ABCC8 p.Ser1237Tyr The fact that glibenclamide blocks Kir6.2/SUR1-S1237Y channels indicates that residues other than S1237 are critical for binding of this drug. Login to comment 130 ABCC8 p.Ser1237Tyr Likewise, the block of Kir6.2/SUR1 by meglitinide and repaglinide, which do not possess a sulfonylurea moiety, is unaltered by the S1237Y mutation (35,53), suggesting that these drugs do not interact with this residue. Login to comment