Literature DB >> 10462379

The unique acyl chain specificity of biliary phosphatidylcholines in mice is independent of their biosynthetic origin in the liver.

L B Agellon1, C J Walkey, D E Vance, F Kuipers, H J Verkade.   

Abstract

The liver synthesizes phosphatidylcholine (PC) de novo from choline via the CDP-choline pathway, and from phosphatidylethanolamine (PE) via the phosphatidylethanolamine N-methyltransferase (PEMT) pathway. Significant amounts of PC, which are highly specific in their acyl chain composition, are secreted into bile by the liver. To determine whether either of the 2 PC biosynthetic routes is sufficient to provide physiological PC concentrations in bile, or is responsible for the unique acyl chain composition of bile PC, we analyzed gallbladder bile composition in mice that synthesized PC either via the PEMT pathway (induced by feeding a choline-deficient diet) or the CDP-choline pathway (based on genetic PEMT-deficiency). The PC concentration in gallbladder bile of mice that synthesize PC mainly via the CDP-choline pathway was comparable with control mice that synthesize PC via both pathways, whereas it was reduced by approximately 40% in mice that synthesize PC via the PEMT pathway. The acyl chain composition of bile PC was similar irrespective of the active PC biosynthetic pathway in the liver. These data demonstrate that the CDP-choline pathway alone, but not the PEMT pathway alone, can account for physiological concentrations of PC in gallbladder bile. Moreover, the specificity of biliary PC fatty acyl composition is determined independently from the synthetic origin of PC.

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Year:  1999        PMID: 10462379     DOI: 10.1002/hep.510300305

Source DB:  PubMed          Journal:  Hepatology        ISSN: 0270-9139            Impact factor:   17.425


  3 in total

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Journal:  J Biol Chem       Date:  2010-05-07       Impact factor: 5.157

2.  Modifying hepatic phospholipid synthesis associates with biliary phospholipid secretion rate in a transporter-independent manner in rats: relation to canalicular membrane fluidity.

Authors:  S Yasumiba; S Tazuma; H Ochi; G Kajiyama
Journal:  Dig Dis Sci       Date:  2001-06       Impact factor: 3.199

3.  Phosphorylation of the yeast choline kinase by protein kinase C. Identification of Ser25 and Ser30 as major sites of phosphorylation.

Authors:  Mal-Gi Choi; Vladlen Kurnov; Michael C Kersting; Avula Sreenivas; George M Carman
Journal:  J Biol Chem       Date:  2005-05-25       Impact factor: 5.157

  3 in total

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