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10.1194/jlr.M056622 http://scihub22266oqcxt.onion/10.1194/jlr.M056622 C4340311!4340311!25601960     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Lipid+Res 2015 ; 56 (3): 644-52 Nephropedia Template TP {{tp|p=25601960|t=2015. ABCB4 exports phosphatidylcholine in a sphingomyelin-dependent manner S |pdf=|usr=}}{{25601960}} gab.com Text ABCB4 exports phosphatidylcholine in a sphingomyelin-dependent manner S JO: J Lipid Res http://www.kidney.de/pget.php?&tw=1&pmid=25601960 #FOAvip ABCB4, which is specifically expressed on the canalicular membrane of hepatocytes, exports phosphatidylcholine (PC) into bile. Because SM depletion increases cellular PC content and stimulates PC and cholesterol efflux by ABCA1, a key transporter involved in generation of HDL, we predicted that SM depletion also stimulates PC efflux through ABCB4. To test this prediction, we compared the lipid efflux activity of ABCB4 and ABCA1 under SM depletion induced by two different types of inhibitors for SM synthesis, myriocin and (1R,3S)-N-(3-hydroxy-1-hydroxymethyl-3-phenylpropyl)dodecanamide, in human embryonic kidney 293 and baby hamster kidney cells. Unexpectedly, SM depletion exerted opposite effects on ABCB4 and ABCA1, suppressing PC efflux through ABCB4 while stimulating efflux through ABCA1. Both ABCB4 and ABCA1 were recovered from Triton-X-100-soluble membranes, but ABCB4 was mainly recovered from CHAPS-insoluble SM-rich membranes, whereas ABCA1 was recovered from CHAPS-soluble membranes. These results suggest that a SM-rich membrane environment is required for ABCB4 to function. ABCB4 must have evolved to exert its maximum activity in the SM-rich membrane environment of the canalicular membrane, where it transports PC as the physiological substrate. Twit Text FOAVip ABCB4 exports phosphatidylcholine in a sphingomyelin-dependent manner S ????J Lipid Res http://www.kidney.de/pget.php?&tw=1&pmid=25601960 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25601960 #FOAvip English Wikipedia <ref>{{Cite pmid|25601960}}</ref> ABCB4 exports phosphatidylcholine in a sphingomyelin-dependent manner S #MMPMID25601960 Zhao Y; Ishigami M; Nagao K; Hanada K; Kono N; Arai H; Matsuo M; Kioka N; Ueda K J Lipid Res 2015[Mar]; 56 (3): 644-52 PMID25601960show ga ABCB4, which is specifically expressed on the canalicular membrane of hepatocytes, exports phosphatidylcholine (PC) into bile. Because SM depletion increases cellular PC content and stimulates PC and cholesterol efflux by ABCA1, a key transporter involved in generation of HDL, we predicted that SM depletion also stimulates PC efflux through ABCB4. To test this prediction, we compared the lipid efflux activity of ABCB4 and ABCA1 under SM depletion induced by two different types of inhibitors for SM synthesis, myriocin and (1R,3S)-N-(3-hydroxy-1-hydroxymethyl-3-phenylpropyl)dodecanamide, in human embryonic kidney 293 and baby hamster kidney cells. Unexpectedly, SM depletion exerted opposite effects on ABCB4 and ABCA1, suppressing PC efflux through ABCB4 while stimulating efflux through ABCA1. Both ABCB4 and ABCA1 were recovered from Triton-X-100-soluble membranes, but ABCB4 was mainly recovered from CHAPS-insoluble SM-rich membranes, whereas ABCA1 was recovered from CHAPS-soluble membranes. These results suggest that a SM-rich membrane environment is required for ABCB4 to function. ABCB4 must have evolved to exert its maximum activity in the SM-rich membrane environment of the canalicular membrane, where it transports PC as the physiological substrate. äABCB4 exports phosphatidylcholine in a sphingomyelin-dependent manner (epmc).pdf DeepDyve Pubget Overpricing