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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1988-11-21
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pubmed:abstractText |
1. Measurements were made of the activities of the following enzymes of glycerolipid synthesis in homogenates of interscapsular brown adipose tissue obtained from rats subjected to a 4 degrees C environment for time periods of 6 h up to 12 days: fatty acyl-CoA synthetase (FAS), mitochondrial and microsomal forms of glycerolphosphate acyltransferase (GPAT), monoacylglycerolphosphate acyltransferase (MGPAT) and Mg2+-dependent phosphatidate phosphohydrolase (PPH). 2. Relative to tissue DNA content, the activities of mitochondrial GPAT, MGPAT and Mg2+-dependent PPH were significantly increased after 1 day of exposure to cold, and continued to increase thereafter. By contrast, FAS and microsomal GPAT activities were unchanged relative to tissue DNA. 3. The time profile of the increase in MGPAT activity correlated well with a concomitant increase in the microsomal marker NADP+-cytochrome c reductase. Changes in mitochondrial GPAT and in Mg2+-dependent PPH activities were larger in amplitude than that of MGPAT. 4. It is proposed that these selective changes in enzyme activity may be associated with the onset of brown-adipose-tissue hyperplasia or possibly with an increase in triacylglycerol synthesis during cold-acclimation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-14228521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-14486217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-2888457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-2996504,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-3004406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-3028368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-3355527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-477972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-5087834,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-5166194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-5820645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-6117324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-6261899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-6285986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-6331400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-6372506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-6781482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178717-7272321
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-Acylglycerol-3-Phosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Coenzyme A Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/FAA2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Glycerol-3-Phosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Glycolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidate Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/long-chain-fatty-acid-CoA ligase
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
253
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
351-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3178717-1-Acylglycerol-3-Phosphate O-Acyltransferase,
pubmed-meshheading:3178717-Acyltransferases,
pubmed-meshheading:3178717-Adaptation, Physiological,
pubmed-meshheading:3178717-Adipose Tissue, Brown,
pubmed-meshheading:3178717-Animals,
pubmed-meshheading:3178717-Coenzyme A Ligases,
pubmed-meshheading:3178717-Cold Temperature,
pubmed-meshheading:3178717-Glycerol-3-Phosphate O-Acyltransferase,
pubmed-meshheading:3178717-Glycolipids,
pubmed-meshheading:3178717-Magnesium,
pubmed-meshheading:3178717-Male,
pubmed-meshheading:3178717-Microsomes,
pubmed-meshheading:3178717-Mitochondria,
pubmed-meshheading:3178717-Phosphatidate Phosphatase,
pubmed-meshheading:3178717-Rats,
pubmed-meshheading:3178717-Rats, Inbred Strains,
pubmed-meshheading:3178717-Repressor Proteins,
pubmed-meshheading:3178717-Saccharomyces cerevisiae Proteins
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pubmed:year |
1988
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pubmed:articleTitle |
Changes in activities of some enzymes of glycerolipid synthesis in brown adipose tissue of cold-acclimated rats.
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pubmed:affiliation |
Department of Biochemistry, University College London, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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