Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2009-4-7
pubmed:abstractText
Animals are remarkably efficient in absorbing dietary fat and assimilating this energy-dense nutrient into the white adipose tissue (WAT) for storage. Although this metabolic efficiency may confer an advantage in times of calorie deprivation, it contributes to obesity and associated metabolic disorders when dietary fat is abundant. Here we show that the intestinal lipid synthesis enzyme acyl CoA:monoacylglycerol acyltransferase-2 (MGAT2) has a crucial role in the assimilation of dietary fat and the accretion of body fat in mice. Mice lacking MGAT2 have a normal phenotype on a low-fat diet. However, on a high-fat diet, MGAT2-deficient mice are protected against developing obesity, glucose intolerance, hypercholesterolemia and fatty livers. Caloric intake is normal in MGAT2-deficient mice, and dietary fat is absorbed fully. However, entry of dietary fat into the circulation occurs at a reduced rate. This altered kinetics of fat absorption apparently results in more partitioning of dietary fat toward energy dissipation rather than toward storage in the WAT. Thus, our studies identify MGAT2 as a key determinant of energy metabolism in response to dietary fat and suggest that the inhibition of this enzyme may prove to be a useful strategy for treating obesity and other metabolic diseases associated with excessive fat intake.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-10766252, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-11481335, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-12077311, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-12576479, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-12618427, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-12621063, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-13832326, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-13910673, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-13937884, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-14216426, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-14966132, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-15236180, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-15738989, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-15834126, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-15834127, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-16756496, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-17498508, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-6061744, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-6250446, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-7193233, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-8898756, http://linkedlifedata.com/resource/pubmed/commentcorrection/19287392-9302267
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1546-170X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
442-6
pubmed:dateRevised
2010-9-22
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding.
pubmed:affiliation
Gladstone Institute of Cardiovascular Disease, San Francisco, California, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural