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Pregnant rats were fed diets deficient in folic acid (\u2013F) or in three key methyl donors, folic acid, choline and methionine (\u2013FLMLC) and the maternal liver was analysed on day 21 of gestation. Two-dimensional gel electrophoresis of soluble proteins identified differentially abundant proteins, which could be allocated into nine functional groups. Five involved in metabolic processes, namely, folate\/methionine cycle, tyrosine metabolism, protein metabolism, energy metabolism and lipid metabolism, and three in cellular processes, namely, endoplasmic reticulum function, bile production and antioxidant defence. The mRNA for sterol regulatory element-binding protein-1c and acetyl-CoA carboxylase-1 (fatty acid synthesis) were decreased by both \u2013F and \u2013FLMLC diets. The mRNA for PPAR\u03b1 and PPAR\u03b3 and carnitine palmitoyl transferase (fatty acid oxidation) were increased in the animals fed the \u2013FLMLC diets. Changes in the abundance of proteins associated with intracellular lipid transport suggest that folate deficiency interferes with lipid export. Reduced fatty acid synthesis appeared to prevent steatosis in animals fed the \u2013F diet. Even with increased oxidation, TAG concentrations were approximately three-fold higher in animals fed the \u2013FLMLC diet and were associated with an increase in the relative abundance of proteins associated with oxidative stress. Fetal development may be indirectly affected by these changes in hepatic lipid metabolism.<\/jats:p>","DOI":"10.1017\/s0007114507798999","type":"journal-article","created":{"date-parts":[[2007,8,13]],"date-time":"2007-08-13T14:48:04Z","timestamp":1187016484000},"page":"262-271","source":"Crossref","is-referenced-by-count":33,"title":["Disruption of lipid metabolism in the liver of the pregnant rat fed folate-deficient and methyl donor-deficient diets"],"prefix":"10.1017","volume":"99","author":[{"given":"Christopher J.","family":"McNeil","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susan M.","family":"Hay","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Garry J.","family":"Rucklidge","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Reid","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gary","family":"Duncan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher A.","family":"Maloney","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William D.","family":"Rees","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"56","published-online":{"date-parts":[[2008,2,1]]},"reference":[{"key":"S0007114507798999_ref36","doi-asserted-by":"publisher","DOI":"10.1194\/jlr.M500277-JLR200"},{"key":"S0007114507798999_ref28","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.96.6.1548"},{"key":"S0007114507798999_ref21","doi-asserted-by":"publisher","DOI":"10.1111\/j.1440-1746.2006.04581.x"},{"key":"S0007114507798999_ref19","doi-asserted-by":"publisher","DOI":"10.1152\/ajpgi.00056.2004"},{"key":"S0007114507798999_ref16","doi-asserted-by":"publisher","DOI":"10.1093\/jn\/126.3.611"},{"key":"S0007114507798999_ref6","doi-asserted-by":"publisher","DOI":"10.1093\/ajcn\/71.5.1295s"},{"key":"S0007114507798999_ref37","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.nutr.24.012003.132249"},{"key":"S0007114507798999_ref4","doi-asserted-by":"publisher","DOI":"10.1093\/ajcn\/83.5.993"},{"key":"S0007114507798999_ref17","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80213-5"},{"key":"S0007114507798999_ref26","doi-asserted-by":"publisher","DOI":"10.1379\/1466-1268(2002)007<0309:AHFCMM>2.0.CO;2"},{"key":"S0007114507798999_ref23","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M301982200"},{"key":"S0007114507798999_ref29","first-page":"1106","article-title":"The structure and organization of the bile canalicular cytoskeleton with special reference to actin and actin-binding proteins","volume":"21","author":"Tsukada","year":"1995","journal-title":"Hepatology"},{"key":"S0007114507798999_ref13","doi-asserted-by":"publisher","DOI":"10.1016\/S1096-7192(02)00113-0"},{"key":"S0007114507798999_ref33","doi-asserted-by":"publisher","DOI":"10.1093\/jn\/135.11.2524"},{"key":"S0007114507798999_ref12","doi-asserted-by":"publisher","DOI":"10.1079\/BJN20051447"},{"key":"S0007114507798999_ref25","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M210904200"},{"key":"S0007114507798999_ref32","doi-asserted-by":"publisher","DOI":"10.1016\/j.mce.2003.11.006"},{"key":"S0007114507798999_ref31","first-page":"509","article-title":"The 3alpha-hydroxy-steroid-dehydrogenase-mRNA and -protein are more prevalent in pericentral than in periportal hepatocytes","volume":"15","author":"Baumgartner","year":"2003","journal-title":"Eur J Gastroenterol Hepatol"},{"key":"S0007114507798999_ref18","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M601277200"},{"key":"S0007114507798999_ref3","doi-asserted-by":"publisher","DOI":"10.1038\/nrg1181"},{"key":"S0007114507798999_ref27","doi-asserted-by":"publisher","DOI":"10.1194\/jlr.M200488-JLR200"},{"key":"S0007114507798999_ref34","doi-asserted-by":"publisher","DOI":"10.1093\/jn\/131.1.33"},{"key":"S0007114507798999_ref2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1753-4887.2004.tb00070.x"},{"key":"S0007114507798999_ref30","doi-asserted-by":"publisher","DOI":"10.1096\/fasebj.11.4.9068609"},{"key":"S0007114507798999_ref5","doi-asserted-by":"publisher","DOI":"10.1079\/BJN20041395"},{"key":"S0007114507798999_ref35","doi-asserted-by":"publisher","DOI":"10.1152\/ajpgi.00402.2005"},{"key":"S0007114507798999_ref10","doi-asserted-by":"publisher","DOI":"10.1096\/fj.04-2974fje"},{"key":"S0007114507798999_ref24","doi-asserted-by":"crossref","first-page":"16655","DOI":"10.1016\/S0021-9258(19)85468-6","article-title":"Cloning and expression of a novel phosphatidylethanolamine N- methyltransferase. 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