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10.1074/jbc.M115.640763 http://scihub22266oqcxt.onion/10.1074/jbc.M115.640763 C4416860!4416860 !25767115     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25767115 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 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\25767115 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Biol+Chem 2015 ; 290 (18 ): 11569-77 Nephropedia Template TP {{tp|p=25767115 |t=2015. Intracellular Na+ regulates epithelial Na+ channel maturation |pdf=|usr=}}{{25767115 }} gab.com Text Intracellular Na+ regulates epithelial Na+ channel maturation JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25767115 #FOAvip Epithelial Na(+) channel (ENaC) function is regulated by the intracellular Na(+) concentration ([Na(+)]i) through a process known as Na(+) feedback inhibition. Although this process is known to decrease the expression of proteolytically processed active channels on the cell surface, it is unknown how [Na(+)]i alters ENaC cleavage. We show here that [Na(+)]i regulates the posttranslational processing of ENaC subunits during channel biogenesis. At times when [Na(+)]i is low, ENaC subunits develop mature N-glycans and are processed by proteases. Conversely, glycan maturation and sensitivity to proteolysis are reduced when [Na(+)]i is relatively high. Surface channels with immature N-glycans were not processed by endogenous channel activating proteases, nor were they sensitive to cleavage by exogenous trypsin. Biotin chase experiments revealed that the immature surface channels were not converted into mature cleaved channels following a reduction in [Na(+)]i. The hypothesis that [Na(+)]i regulates ENaC maturation within the biosynthetic pathways is further supported by the finding that Brefeldin A prevented the accumulation of processed surface channels following a reduction in [Na(+)]i. Therefore, increased [Na(+)]i interferes with ENaC N-glycan maturation and prevents the channel from entering a state that allows proteolytic processing. Twit Text FOAVip Intracellular Na+ regulates epithelial Na+ channel maturation ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25767115 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25767115 #FOAvip English Wikipedia <ref>{{Cite pmid|25767115 }}</ref> Intracellular Na+ regulates epithelial Na+ channel maturation #MMPMID25767115 Heidrich E ; Carattino MD ; Hughey RP ; Pilewski JM ; Kleyman TR ; Myerburg MM J Biol Chem 2015[May]; 290 (18 ): 11569-77 PMID25767115 show ga Epithelial Na(+) channel (ENaC) function is regulated by the intracellular Na(+) concentration ([Na(+)]i) through a process known as Na(+) feedback inhibition. Although this process is known to decrease the expression of proteolytically processed active channels on the cell surface, it is unknown how [Na(+)]i alters ENaC cleavage. We show here that [Na(+)]i regulates the posttranslational processing of ENaC subunits during channel biogenesis. At times when [Na(+)]i is low, ENaC subunits develop mature N-glycans and are processed by proteases. Conversely, glycan maturation and sensitivity to proteolysis are reduced when [Na(+)]i is relatively high. Surface channels with immature N-glycans were not processed by endogenous channel activating proteases, nor were they sensitive to cleavage by exogenous trypsin. Biotin chase experiments revealed that the immature surface channels were not converted into mature cleaved channels following a reduction in [Na(+)]i. The hypothesis that [Na(+)]i regulates ENaC maturation within the biosynthetic pathways is further supported by the finding that Brefeldin A prevented the accumulation of processed surface channels following a reduction in [Na(+)]i. Therefore, increased [Na(+)]i interferes with ENaC N-glycan maturation and prevents the channel from entering a state that allows proteolytic processing. |Epithelial Sodium Channels/biosynthesis/*metabolism [MESH] |Humans [MESH] |Intracellular Space/*metabolism [MESH] |Peptide Hydrolases/metabolism [MESH] |Polysaccharides/metabolism [MESH] |Protein Processing, Post-Translational [MESH]Intracellular Na+ regulates epithelial Na+ channel maturation (epmc).pdf DeepDyve Pubget Overpricing