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10.1074/jbc.RA118.002333 http://scihub22266oqcxt.onion/10.1074/jbc.RA118.002333 C5936833!5936833!29555681     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29555681&cmd=llinks): Failed to open stream: HTTP request failed! 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Patatin-like phospholipase domain?containing protein 3 promotes transfers of essential fatty acids from triglycerides to phospholipids in hepatic lipid droplets |pdf=|usr=}}{{29555681}} gab.com Text Patatin-like phospholipase domain containing protein 3 promotes transfers of essential fatty acids from triglycerides to phospholipids in hepatic lipid droplets JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=29555681 #FOAvip Fatty liver disease (FLD) is a burgeoning health problem. A missense variant (I148M) in patatin-like phospholipase domain?containing protein 3 (PNPLA3) confers susceptibility to FLD, although the mechanism is not known. To glean first insights into the physiological function of PNPLA3, we performed detailed lipidomic profiling of liver lysates and lipid droplets (LDs) from WT and Pnpla3?/? (KO) mice and from knock-in (ki) mice expressing either the 148M variant (IM-ki mice) or a variant (S47A) that renders the protein catalytically inactive (SA-ki mice). The four strains differed in composition of very-long-chain polyunsaturated fatty acids (vLCPUFA) in hepatic LDs. In the LDs of IM-ki mice, vLCPUFAs were depleted from triglycerides and enriched in phospholipids. Conversely, vLCPUFAs were enriched in triglycerides and depleted from phospholipids in SA-ki and Pnpla3?/? mice. Release of vLCPUFAs from hepatic LDs incubated ex vivo was increased in droplets from IM-ki mice and decreased from droplets isolated from Pnpla3?/? and SA-ki mice relative to those of WT mice. Thus, the physiological role of PNPLA3 appears to be to remodel triglycerides and phospholipids in LDs, perhaps to accommodate changes in LD size in response to feeding. Because SA-ki and IM-ki both cause FLD and yet have opposite effects on the lipidomic profile of LDs, we conclude that the FLD associated with genetic variation in PNPLA3 is not related to the enzyme's role in remodeling LD lipids. Twit Text FOAVip Patatin-like phospholipase domain containing protein 3 promotes transfers of essential fatty acids from triglycerides to phospholipids in hepatic lipid droplets ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=29555681 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29555681 #FOAvip English Wikipedia <ref>{{Cite pmid|29555681}}</ref> Patatin-like phospholipase domain?containing protein 3 promotes transfers of essential fatty acids from triglycerides to phospholipids in hepatic lipid droplets #MMPMID29555681 Mitsche MA; Hobbs HH; Cohen JC J Biol Chem 2018[May]; 293 (18): 6958-68 PMID29555681show ga Fatty liver disease (FLD) is a burgeoning health problem. A missense variant (I148M) in patatin-like phospholipase domain?containing protein 3 (PNPLA3) confers susceptibility to FLD, although the mechanism is not known. To glean first insights into the physiological function of PNPLA3, we performed detailed lipidomic profiling of liver lysates and lipid droplets (LDs) from WT and Pnpla3?/? (KO) mice and from knock-in (ki) mice expressing either the 148M variant (IM-ki mice) or a variant (S47A) that renders the protein catalytically inactive (SA-ki mice). The four strains differed in composition of very-long-chain polyunsaturated fatty acids (vLCPUFA) in hepatic LDs. In the LDs of IM-ki mice, vLCPUFAs were depleted from triglycerides and enriched in phospholipids. Conversely, vLCPUFAs were enriched in triglycerides and depleted from phospholipids in SA-ki and Pnpla3?/? mice. Release of vLCPUFAs from hepatic LDs incubated ex vivo was increased in droplets from IM-ki mice and decreased from droplets isolated from Pnpla3?/? and SA-ki mice relative to those of WT mice. Thus, the physiological role of PNPLA3 appears to be to remodel triglycerides and phospholipids in LDs, perhaps to accommodate changes in LD size in response to feeding. Because SA-ki and IM-ki both cause FLD and yet have opposite effects on the lipidomic profile of LDs, we conclude that the FLD associated with genetic variation in PNPLA3 is not related to the enzyme's role in remodeling LD lipids. �Patatin-like phospholipase domain?containing protein 3 promotes transf(epmc).pdf DeepDyve Pubget Overpricing