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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1998-1-15
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pubmed:abstractText |
In the yeast Saccharomyces cerevisiae, fatty acid beta-oxidation is restricted to peroxisomes. Previous studies have shown two possible routes by which fatty acids enter the peroxisome. The first route involves transport of medium-chain fatty acids across the peroxisomal membrane as free fatty acids, followed by activation within the peroxisome by Faa2p, an acyl-CoA synthetase. The second route involves transport of long-chain fatty acids. Long-chain fatty acids enter the peroxisome via a route that involves activation in the extraperoxisomal space, followed by transport across the peroxisomal membrane. It has been suggested that this transport is dependent upon the peroxisomal ATP-binding-cassette transporters Pxa1p and Pxa2p. In this paper we investigated whether Pxa2p is directly responsible for the transport of C18:1-CoA, a long-chain acyl-CoA ester. Using protoplasts in which the plasma membrane has been selectively permeabilised by digitonin, we show that C18:1-CoA, but not C8:0-CoA, enters the peroxisome via Pxa2p, in an ATP-dependent fashion. The results obtained may contribute to the elucidation of the primary defect in the human disease X-linked adrenoleukodystrophy.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Digitonin,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PXA2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
249
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
657-61
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:9395310-ATP-Binding Cassette Transporters,
pubmed-meshheading:9395310-Acyl Coenzyme A,
pubmed-meshheading:9395310-Adenosine Triphosphate,
pubmed-meshheading:9395310-Adrenoleukodystrophy,
pubmed-meshheading:9395310-Biological Transport,
pubmed-meshheading:9395310-Cell Membrane Permeability,
pubmed-meshheading:9395310-Digitonin,
pubmed-meshheading:9395310-Fatty Acids,
pubmed-meshheading:9395310-Fungal Proteins,
pubmed-meshheading:9395310-Humans,
pubmed-meshheading:9395310-Microbodies,
pubmed-meshheading:9395310-Oxidation-Reduction,
pubmed-meshheading:9395310-Protoplasts,
pubmed-meshheading:9395310-Saccharomyces cerevisiae,
pubmed-meshheading:9395310-Saccharomyces cerevisiae Proteins
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pubmed:year |
1997
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pubmed:articleTitle |
Transport of activated fatty acids by the peroxisomal ATP-binding-cassette transporter Pxa2 in a semi-intact yeast cell system.
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pubmed:affiliation |
Department of Clinical Chemistry, University of Amsterdam, Academic Medical Centre, The Netherlands.
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pubmed:publicationType |
Journal Article
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