Source:http://linkedlifedata.com/resource/pubmed/id/11724471
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2001-11-28
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pubmed:abstractText |
Fatty acids are the main structural and energy sources of the human body. Within the organism, they are presented to cells as fatty acid:albumin complexes. Dissociation from albumin represents the first step of the cellular uptake process, involving membrane proteins with high affinity for fatty acids, e.g., fatty acid translocase (FAT/CD 36) or the membrane fatty acid-binding protein (FABPpm). According to the thus created transmembrane concentration gradient, uncharged fatty acids can flip-flop from the outer leaflet across the phospholipid bilayer. At the cytosolic surface of the plasma membrane, fatty acids can associate with the cytosolic FABP (FABP(c)) or with caveolin-1. Caveolins are constituents of caveolae, which are proposed to serve as lipid delivery vehicles for subcellular organelles. It is not known whether protein (FABP(c))- and lipid (caveolae)-mediated intracellular trafficking of fatty acids operates in conjunction or in parallel. Channeling fatty acids to the different metabolic pathways requires activation to acyl-CoA. For this process, the family of fatty acid transport proteins (FATP 1-5/6) might be relevant because they have been shown to possess acyl-CoA synthetase activity. Their variable N-terminal signaling sequences suggest that they might be targeted to specific organelles by anchoring in the phospholipid bilayer of the different subcellular membranes. At the highly conserved cytosolic AMP-binding site of FATP, fatty acids are activated to acyl-CoA for subsequent metabolic disposition by specific organelles. Overall, fatty acid uptake represents a continuous flow involving the following: dissociation from albumin by membrane proteins with high affinity for fatty acids; passive flip-flop across the phospholipid bilayer; binding to FABP(C) and caveolin-1 at the cytosolic plasma membrane; and intracellular trafficking via FABP(c) and/or caveolae to sites of metabolic disposition. The uptake process is terminated after activation to acyl-CoA by the members of the FATP family targeted intracellularly to different organelles.
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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/Antigens, CD36,
http://linkedlifedata.com/resource/pubmed/chemical/CAV1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolins,
http://linkedlifedata.com/resource/pubmed/chemical/FABP7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Organic Anion Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/SLC27A1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SLC27A6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0024-4201
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
36
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
981-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11724471-Animals,
pubmed-meshheading:11724471-Antigens, CD36,
pubmed-meshheading:11724471-Biological Transport,
pubmed-meshheading:11724471-Carrier Proteins,
pubmed-meshheading:11724471-Caveolin 1,
pubmed-meshheading:11724471-Caveolins,
pubmed-meshheading:11724471-Fatty Acid Transport Proteins,
pubmed-meshheading:11724471-Fatty Acid-Binding Proteins,
pubmed-meshheading:11724471-Fatty Acids,
pubmed-meshheading:11724471-Humans,
pubmed-meshheading:11724471-Membrane Glycoproteins,
pubmed-meshheading:11724471-Membrane Transport Proteins,
pubmed-meshheading:11724471-Neoplasm Proteins,
pubmed-meshheading:11724471-Organelles,
pubmed-meshheading:11724471-Organic Anion Transporters,
pubmed-meshheading:11724471-Tumor Suppressor Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
A new concept of cellular uptake and intracellular trafficking of long-chain fatty acids.
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pubmed:affiliation |
Department of Gastroenterology, Ruprecht-Karls-University, 69115 Heidelberg, Germany. wolfgang_stremmel@med.uni-heidelberg.de
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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