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10.1164/rccm.201405-0833OC http://scihub22266oqcxt.onion/10.1164/rccm.201405-0833OC C4214088!4214088!25029038     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Am+J+Respir+Crit+Care+Med 2014 ; 190 (5): 522-32 Nephropedia Template TP {{tp|p=25029038|t=2014. A Novel Tumor Necrosis Factor?mediated Mechanism of Direct Epithelial Sodium Channel Activation |pdf=|usr=}}{{25029038}} gab.com Text A Novel Tumor Necrosis Factor mediated Mechanism of Direct Epithelial Sodium Channel Activation JO: Am J Respir Crit Care Med http://www.kidney.de/pget.php?&tw=1&pmid=25029038 #FOAvip Rationale: Alveolar liquid clearance is regulated by Na+ uptake through the apically expressed epithelial sodium channel (ENaC) and basolaterally localized Na+-K+-ATPase in type II alveolar epithelial cells. Dysfunction of these Na+ transporters during pulmonary inflammation can contribute to pulmonary edema.Objectives: In this study, we sought to determine the precise mechanism by which the TIP peptide, mimicking the lectin-like domain of tumor necrosis factor (TNF), stimulates Na+ uptake in a homologous cell system in the presence or absence of the bacterial toxin pneumolysin (PLY).Methods: We used a combined biochemical, electrophysiological, and molecular biological in vitro approach and assessed the physiological relevance of the lectin-like domain of TNF in alveolar liquid clearance in vivo by generating triple-mutant TNF knock-in mice that express a mutant TNF with deficient Na+ uptake stimulatory activity.Measurements and Main Results: TIP peptide directly activates ENaC, but not the Na+-K+-ATPase, upon binding to the carboxy-terminal domain of the ? subunit of the channel. In the presence of PLY, a mediator of pneumococcal-induced pulmonary edema, this binding stabilizes the ENaC-PIP2-MARCKS complex, which is necessary for the open probability conformation of the channel and preserves ENaC-? protein expression, by means of blunting the protein kinase C-? pathway. Triple-mutant TNF knock-in mice are more prone than wild-type mice to develop edema with low-dose intratracheal PLY, correlating with reduced pulmonary ENaC-? subunit expression.Conclusions: These results demonstrate a novel TNF-mediated mechanism of direct ENaC activation and indicate a physiological role for the lectin-like domain of TNF in the resolution of alveolar edema during inflammation. Twit Text FOAVip A Novel Tumor Necrosis Factor mediated Mechanism of Direct Epithelial Sodium Channel Activation ????Am J Respir Crit Care Med http://www.kidney.de/pget.php?&tw=1&pmid=25029038 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25029038 #FOAvip English Wikipedia <ref>{{Cite pmid|25029038}}</ref> A Novel Tumor Necrosis Factor?mediated Mechanism of Direct Epithelial Sodium Channel Activation #MMPMID25029038 Czikora I; Alli A; Bao HF; Kaftan D; Sridhar S; Apell HJ; Gorshkov B; White R; Zimmermann A; Wendel A; Pauly-Evers M; Hamacher J; Garcia-Gabay I; Fischer B; Verin A; Bagi Z; Pittet JF; Shabbir W; Lemmens-Gruber R; Chakraborty T; Lazrak A; Matthay MA; Eaton DC; Lucas R Am J Respir Crit Care Med 2014[Sep]; 190 (5): 522-32 PMID25029038show ga Rationale: Alveolar liquid clearance is regulated by Na+ uptake through the apically expressed epithelial sodium channel (ENaC) and basolaterally localized Na+-K+-ATPase in type II alveolar epithelial cells. Dysfunction of these Na+ transporters during pulmonary inflammation can contribute to pulmonary edema.Objectives: In this study, we sought to determine the precise mechanism by which the TIP peptide, mimicking the lectin-like domain of tumor necrosis factor (TNF), stimulates Na+ uptake in a homologous cell system in the presence or absence of the bacterial toxin pneumolysin (PLY).Methods: We used a combined biochemical, electrophysiological, and molecular biological in vitro approach and assessed the physiological relevance of the lectin-like domain of TNF in alveolar liquid clearance in vivo by generating triple-mutant TNF knock-in mice that express a mutant TNF with deficient Na+ uptake stimulatory activity.Measurements and Main Results: TIP peptide directly activates ENaC, but not the Na+-K+-ATPase, upon binding to the carboxy-terminal domain of the ? subunit of the channel. In the presence of PLY, a mediator of pneumococcal-induced pulmonary edema, this binding stabilizes the ENaC-PIP2-MARCKS complex, which is necessary for the open probability conformation of the channel and preserves ENaC-? protein expression, by means of blunting the protein kinase C-? pathway. Triple-mutant TNF knock-in mice are more prone than wild-type mice to develop edema with low-dose intratracheal PLY, correlating with reduced pulmonary ENaC-? subunit expression.Conclusions: These results demonstrate a novel TNF-mediated mechanism of direct ENaC activation and indicate a physiological role for the lectin-like domain of TNF in the resolution of alveolar edema during inflammation. äA Novel Tumor Necrosis Factor?mediated Mechanism of Direct Epithelial (epmc).pdf DeepDyve Pubget Overpricing