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10.1007/s00018-016-2149-6 http://scihub22266oqcxt.onion/10.1007/s00018-016-2149-6 26874684!11108291!26874684     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26874684.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Mol+Life+Sci 2016 ; 73 (17): 3351-73 Nephropedia Template TP {{tp|p=26874684|t=2016. Function and regulation of TRPM7, as well as intracellular magnesium content, are altered in cells expressing DeltaF508-CFTR and G551D-CFTR |pdf=|usr=}}{{26874684}} gab.com Text Function and regulation of TRPM7, as well as intracellular magnesium content, are altered in cells expressing DeltaF508-CFTR and G551D-CFTR JO: Cell Mol Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=26874684 #FOAvip Cystic fibrosis (CF), one of the most common fatal hereditary disorders, is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. The CFTR gene product is a multidomain adenosine triphosphate-binding cassette (ABC) protein that functions as a chloride (Cl(-)) channel that is regulated by intracellular magnesium [Mg(2+)]i. The most common mutations in CFTR are a deletion of a phenylalanine residue at position 508 (DeltaF508-CFTR, 70-80 % of CF phenotypes) and a Gly551Asp substitution (G551D-CFTR, 4-5 % of alleles), which lead to decreased or almost abolished Cl(-) channel function, respectively. Magnesium ions have to be finely regulated within cells for optimal expression and function of CFTR. Therefore, the melastatin-like transient receptor potential cation channel, subfamily M, member 7 (TRPM7), which is responsible for Mg(2+) entry, was studies and [Mg(2+)]i measured in cells stably expressing wildtype CFTR, and two mutant proteins (DeltaF508-CFTR and G551D-CFTR). This study shows for the first time that [Mg(2+)]i is decreased in cells expressing DeltaF508-CFTR and G551D-CFTR mutated proteins. It was also observed that the expression of the TRPM7 protein is increased; however, membrane localization was altered for both DeltaF508del-CFTR and G551D-CFTR. Furthermore, both the function and regulation of the TRPM7 channel regarding Mg(2+) is decreased in the cells expressing the mutated CFTR. Ca(2+) influx via TRPM7 were also modified in cells expressing a mutated CFTR. Therefore, there appears to be a direct involvement of TRPM7 in CF physiopathology. Finally, we propose that the TRPM7 activator Naltriben is a new potentiator for G551D-CFTR as the function of this mutant increases upon activation of TRPM7 by Naltriben. Twit Text FOAVip Function and regulation of TRPM7, as well as intracellular magnesium content, are altered in cells expressing DeltaF508-CFTR and G551D-CFTR ????Cell Mol Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=26874684 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26874684 #FOAvip English Wikipedia <ref>{{Cite pmid|26874684}}</ref> Function and regulation of TRPM7, as well as intracellular magnesium content, are altered in cells expressing DeltaF508-CFTR and G551D-CFTR #MMPMID26874684 Huguet F; Calvez ML; Benz N; Le Hir S; Mignen O; Buscaglia P; Horgen FD; Ferec C; Kerbiriou M; Trouve P Cell Mol Life Sci 2016[Sep]; 73 (17): 3351-73 PMID26874684show ga Cystic fibrosis (CF), one of the most common fatal hereditary disorders, is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. The CFTR gene product is a multidomain adenosine triphosphate-binding cassette (ABC) protein that functions as a chloride (Cl(-)) channel that is regulated by intracellular magnesium [Mg(2+)]i. The most common mutations in CFTR are a deletion of a phenylalanine residue at position 508 (DeltaF508-CFTR, 70-80 % of CF phenotypes) and a Gly551Asp substitution (G551D-CFTR, 4-5 % of alleles), which lead to decreased or almost abolished Cl(-) channel function, respectively. Magnesium ions have to be finely regulated within cells for optimal expression and function of CFTR. Therefore, the melastatin-like transient receptor potential cation channel, subfamily M, member 7 (TRPM7), which is responsible for Mg(2+) entry, was studies and [Mg(2+)]i measured in cells stably expressing wildtype CFTR, and two mutant proteins (DeltaF508-CFTR and G551D-CFTR). This study shows for the first time that [Mg(2+)]i is decreased in cells expressing DeltaF508-CFTR and G551D-CFTR mutated proteins. It was also observed that the expression of the TRPM7 protein is increased; however, membrane localization was altered for both DeltaF508del-CFTR and G551D-CFTR. Furthermore, both the function and regulation of the TRPM7 channel regarding Mg(2+) is decreased in the cells expressing the mutated CFTR. Ca(2+) influx via TRPM7 were also modified in cells expressing a mutated CFTR. Therefore, there appears to be a direct involvement of TRPM7 in CF physiopathology. Finally, we propose that the TRPM7 activator Naltriben is a new potentiator for G551D-CFTR as the function of this mutant increases upon activation of TRPM7 by Naltriben. |*Gene Expression Regulation/drug effects[MESH] |Adenosine Triphosphate/chemistry/pharmacology[MESH] |Calcium/analysis[MESH] |Chloride Channels/metabolism[MESH] |Cymenes[MESH] |Cystic Fibrosis Transmembrane Conductance Regulator/genetics/*metabolism[MESH] |Cystic Fibrosis/genetics/pathology[MESH] |Fura-2/chemistry[MESH] |HeLa Cells[MESH] |Humans[MESH] |Kinetics[MESH] |Magnesium/*analysis/chemistry[MESH] |Monoterpenes/pharmacology[MESH] |Mutagenesis, Site-Directed[MESH] |Naltrexone/analogs & derivatives/pharmacology[MESH] |Patch-Clamp Techniques[MESH] |Protein Interaction Maps/drug effects[MESH] |Protein Serine-Threonine Kinases/antagonists & inhibitors/genetics/*metabolism[MESH] |RNA, Messenger/metabolism[MESH]Function and regulation of TRPM7, as well as intracellular magnesium c(epmc).pdf DeepDyve Pubget Overpricing