Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
2005-7-26
pubmed:abstractText
Although studies in vitro and in yeast suggest that acyl-CoA binding protein ACBP may modulate long-chain fatty acyl-CoA (LCFA-CoA) distribution, its physiological function in mammals is unresolved. To address this issue, the effect of ACBP on liver LCFA-CoA pool size, acyl chain composition, distribution, and transacylation into more complex lipids was examined in transgenic mice expressing a higher level of ACBP. While ACBP transgenic mice did not exhibit altered body or liver weight, liver LCFA-CoA pool size increased by 69%, preferentially in saturated and polyunsaturated, but not monounsaturated, LCFA-CoAs. Intracellular LCFA-CoA distribution was also altered such that the ratio of LCFA-CoA content in (membranes, organelles)/cytosol increased 2.7-fold, especially in microsomes but not mitochondria. The increased distribution of specific LCFA-CoAs to the membrane/organelle and microsomal fractions followed the same order as the relative LCFA-CoA binding affinity exhibited by murine recombinant ACBP: saturated > monounsaturated > polyunsaturated C14-C22 LCFA-CoAs. Consistent with the altered microsomal LCFA-CoA level and distribution, enzymatic activity of liver microsomal glycerol-3-phosphate acyltransferase (GPAT) increased 4-fold, liver mass of phospholipid and triacylglyceride increased nearly 2-fold, and relative content of monounsaturated C18:1 fatty acid increased 44% in liver phospholipids. These effects were not due to the ACBP transgene altering the protein levels of liver microsomal acyltransferase enzymes such as GPAT, lysophosphatidic acid acyltransferase (LAT), or acyl-CoA cholesterol acyltransferase 2 (ACAT-2). Thus, these data show for the first time in a physiological context that ACBP expression may play a role in LCFA-CoA metabolism.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Diazepam Binding Inhibitor, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, http://linkedlifedata.com/resource/pubmed/chemical/Glycerol-3-Phosphate..., http://linkedlifedata.com/resource/pubmed/chemical/Glycolipids, http://linkedlifedata.com/resource/pubmed/chemical/Lipids, http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sterol O-Acyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Triglycerides, http://linkedlifedata.com/resource/pubmed/chemical/glycerolglycolipids, http://linkedlifedata.com/resource/pubmed/chemical/sterol O-acyltransferase 2
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10282-97
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:16042405-Acyl Coenzyme A, pubmed-meshheading:16042405-Animals, pubmed-meshheading:16042405-Body Weight, pubmed-meshheading:16042405-Carrier Proteins, pubmed-meshheading:16042405-Diazepam Binding Inhibitor, pubmed-meshheading:16042405-Fatty Acid-Binding Proteins, pubmed-meshheading:16042405-Fatty Acids, pubmed-meshheading:16042405-Glycerol-3-Phosphate O-Acyltransferase, pubmed-meshheading:16042405-Glycolipids, pubmed-meshheading:16042405-Lipid Metabolism, pubmed-meshheading:16042405-Lipids, pubmed-meshheading:16042405-Liver, pubmed-meshheading:16042405-Mice, pubmed-meshheading:16042405-Mice, Transgenic, pubmed-meshheading:16042405-Organ Size, pubmed-meshheading:16042405-Phospholipids, pubmed-meshheading:16042405-Protein Binding, pubmed-meshheading:16042405-Recombinant Proteins, pubmed-meshheading:16042405-Sterol O-Acyltransferase, pubmed-meshheading:16042405-Triglycerides
pubmed:year
2005
pubmed:articleTitle
Acyl-coenzyme A binding protein expression alters liver fatty acyl-coenzyme A metabolism.
pubmed:affiliation
Department of Physiology and Pharmacology, Texas A&M University, College Station, Texas 77843-4466, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural