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10.1161/01.RES.0000161451.04649.a8 http://scihub22266oqcxt.onion/10.1161/01.RES.0000161451.04649.a8 15746441!ä!15746441 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Circ+Res 2005 ; 96 (7): 730-9 Nephropedia Template TP {{tp|p=15746441|t=2005. Impaired KCNQ1-KCNE1 and phosphatidylinositol-4,5-bisphosphate interaction underlies the long QT syndrome |pdf=|usr=}}{{15746441}} gab.com Text Impaired KCNQ1-KCNE1 and phosphatidylinositol-4,5-bisphosphate interaction underlies the long QT syndrome JO: Circ Res http://www.kidney.de/pget.php?&tw=1&pmid=15746441 #FOAvip Nearly a hundred different KCNQ1 mutations have been reported as leading to the cardiac long QT syndrome, characterized by prolonged QT interval, syncopes, and sudden death. We have previously shown that phosphatidylinositol-4,5-bisphosphate (PIP2) regulates the KCNQ1-KCNE1 complex. In the present study, we show that PIP2 affinity is reduced in three KCNQ1 mutant channels (R243H, R539W, and R555C) associated with the long QT syndrome. In giant excised patches, direct application of PIP2 on the cytoplasmic face of the three mutant channels counterbalances the loss of function. Reintroduction of a positive charge by application of methanethiosulfonate ethylammonium on the cytoplasmic face of R555C mutant channels also restores channel activity. The channel affinity for a soluble analog of PIP2 is decreased in the three mutant channels. By using a model that describes the KCNQ1-KCNE1 channel behavior and by fitting the relationship between the kinetics of deactivation and the current amplitude obtained in whole-cell experiments, we estimated the PIP2 binding and dissociation rates on wild-type and mutant channels. The dissociation rate of the three mutants was higher than for the wild-type channel, suggesting a decreased affinity for PIP2. PIP2 binding was magnesium-dependent, and the PIP2-dependent equilibrium constant in the absence of magnesium was higher with the wild-type than with the mutant channels. Altogether, our data suggest that a reduced PIP2 affinity of KCNQ1 mutants can lead to the long QT syndrome. Twit Text FOAVip Impaired KCNQ1-KCNE1 and phosphatidylinositol-4,5-bisphosphate interaction underlies the long QT syndrome ????Circ Res http://www.kidney.de/pget.php?&tw=1&pmid=15746441 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=15746441 #FOAvip English Wikipedia <ref>{{Cite pmid|15746441}}</ref> Impaired KCNQ1-KCNE1 and phosphatidylinositol-4,5-bisphosphate interaction underlies the long QT syndrome #MMPMID15746441 Park KH; Piron J; Dahimene S; Merot J; Baro I; Escande D; Loussouarn G Circ Res 2005[Apr]; 96 (7): 730-9 PMID15746441show ga Nearly a hundred different KCNQ1 mutations have been reported as leading to the cardiac long QT syndrome, characterized by prolonged QT interval, syncopes, and sudden death. We have previously shown that phosphatidylinositol-4,5-bisphosphate (PIP2) regulates the KCNQ1-KCNE1 complex. In the present study, we show that PIP2 affinity is reduced in three KCNQ1 mutant channels (R243H, R539W, and R555C) associated with the long QT syndrome. In giant excised patches, direct application of PIP2 on the cytoplasmic face of the three mutant channels counterbalances the loss of function. Reintroduction of a positive charge by application of methanethiosulfonate ethylammonium on the cytoplasmic face of R555C mutant channels also restores channel activity. The channel affinity for a soluble analog of PIP2 is decreased in the three mutant channels. By using a model that describes the KCNQ1-KCNE1 channel behavior and by fitting the relationship between the kinetics of deactivation and the current amplitude obtained in whole-cell experiments, we estimated the PIP2 binding and dissociation rates on wild-type and mutant channels. The dissociation rate of the three mutants was higher than for the wild-type channel, suggesting a decreased affinity for PIP2. PIP2 binding was magnesium-dependent, and the PIP2-dependent equilibrium constant in the absence of magnesium was higher with the wild-type than with the mutant channels. Altogether, our data suggest that a reduced PIP2 affinity of KCNQ1 mutants can lead to the long QT syndrome. |Animals[MESH] |COS Cells[MESH] |Ethyl Methanesulfonate/analogs & derivatives/pharmacology[MESH] |Humans[MESH] |KCNQ Potassium Channels[MESH] |KCNQ1 Potassium Channel[MESH] |Long QT Syndrome/*etiology/metabolism[MESH] |Magnesium/pharmacology[MESH] |Mutation[MESH] |Phosphatidylinositol 4,5-Diphosphate/*metabolism[MESH]Impaired KCNQ1-KCNE1 and phosphatidylinositol-4,5-bisphosphate interac(epmc).pdf DeepDyve Pubget Overpricing