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10.1007/s00424-014-1618-8 http://scihub22266oqcxt.onion/10.1007/s00424-014-1618-8 C4502298!4502298!25277268     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       Pflugers+Arch 2015 ; 467 (8): 1783-94 Nephropedia Template TP {{tp|p=25277268|t=2015. The cystic fibrosis transmembrane conductance regulator is an extracellular chloride sensor |pdf=|usr=}}{{25277268}} gab.com Text The cystic fibrosis transmembrane conductance regulator is an extracellular chloride sensor JO: Pflugers Arch http://www.kidney.de/pget.php?&tw=1&pmid=25277268 #FOAvip The cystic fibrosis transmembrane conductance regulator (CFTR) is a Cl? channel that governs the quantity and composition of epithelial secretions. CFTR function is normally tightly controlled as dysregulation can lead to life-threatening diseases such as secretory diarrhoea and cystic fibrosis. CFTR activity is regulated by phosphorylation of its cytosolic regulatory (R) domain, and ATP binding and hydrolysis at two nucleotide-binding domains (NBDs). Here, we report that CFTR activity is also controlled by extracellular Cl? concentration ([Cl?]o). Patch clamp current recordings show that a rise in [Cl?]o stimulates CFTR channel activity, an effect conferred by a single arginine residue, R899, in extracellular loop 4 of the protein. Using NBD mutants and ATP dose response studies in WT channels, we determined that [Cl?]o sensing was linked to changes in ATP binding energy at NBD1, which likely impacts NBD dimer stability. Biochemical measurements showed that increasing [Cl?]o decreased the intrinsic ATPase activity of CFTR mainly through a reduction in maximal ATP turnover. Our studies indicate that sensing [Cl?]o is a novel mechanism for regulating CFTR activity and suggest that the luminal ionic environment is an important physiological arbiter of CFTR function, which has significant implications for salt and fluid homeostasis in epithelial tissues. Twit Text FOAVip The cystic fibrosis transmembrane conductance regulator is an extracellular chloride sensor ????Pflugers Arch http://www.kidney.de/pget.php?&tw=1&pmid=25277268 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25277268 #FOAvip English Wikipedia <ref>{{Cite pmid|25277268}}</ref> The cystic fibrosis transmembrane conductance regulator is an extracellular chloride sensor #MMPMID25277268 Broadbent SD; Ramjeesingh M; Bear CE; Argent BE; Linsdell P; Gray MA Pflugers Arch 2015[]; 467 (8): 1783-94 PMID25277268show ga The cystic fibrosis transmembrane conductance regulator (CFTR) is a Cl? channel that governs the quantity and composition of epithelial secretions. CFTR function is normally tightly controlled as dysregulation can lead to life-threatening diseases such as secretory diarrhoea and cystic fibrosis. CFTR activity is regulated by phosphorylation of its cytosolic regulatory (R) domain, and ATP binding and hydrolysis at two nucleotide-binding domains (NBDs). Here, we report that CFTR activity is also controlled by extracellular Cl? concentration ([Cl?]o). Patch clamp current recordings show that a rise in [Cl?]o stimulates CFTR channel activity, an effect conferred by a single arginine residue, R899, in extracellular loop 4 of the protein. Using NBD mutants and ATP dose response studies in WT channels, we determined that [Cl?]o sensing was linked to changes in ATP binding energy at NBD1, which likely impacts NBD dimer stability. Biochemical measurements showed that increasing [Cl?]o decreased the intrinsic ATPase activity of CFTR mainly through a reduction in maximal ATP turnover. Our studies indicate that sensing [Cl?]o is a novel mechanism for regulating CFTR activity and suggest that the luminal ionic environment is an important physiological arbiter of CFTR function, which has significant implications for salt and fluid homeostasis in epithelial tissues. äThe cystic fibrosis transmembrane conductance regulator is an extracel(epmc).pdf DeepDyve Pubget Overpricing