Document Detail


Intracellular transport of fatty acids in muscle. Role of cytoplasmic fatty acid-binding protein.
MedLine Citation:
PMID:  9781327     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Long-chain fatty acids represent a major substrate for energy production in striated muscles, especially in those muscles which have a high oxidative enzymatic capacity. Following their uptake from the extracellular compartment the fatty acids have to translocate through the aqueous cytoplasm of the myocytes to reach the mitochondria where they undergo oxidative degradation. This intracellular transport is assisted by cytoplasmic fatty acid-binding protein (FABPc), a small (15 kD) protein which shows a high affinity for the non-covalent binding of long-chain fatty acids, and of which several types occur. So-called heart-type or muscle-type FABPc is found in muscle cells, and is abundant especially in oxidative fibers. The muscular FABPc content appears to relate to the rate of fatty acid utilization, and also changes in concert to modulations in fatty acid utilization induced by (patho)physiological stimuli (e.g. endurance training, diabetes). The facilitation of intracellular fatty acid transport by FABPc is accomplished by increasing the concentration of the diffusing fatty acids in the aqueous cytoplasm and, most likely, also by interacting directly with membranes to promote transfer of fatty acids to and from the cytosolic binding protein.
Authors:
J F Glatz; E Van Breda; G J Van der Vusse
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Advances in experimental medicine and biology     Volume:  441     ISSN:  0065-2598     ISO Abbreviation:  Adv. Exp. Med. Biol.     Publication Date:  1998  
Date Detail:
Created Date:  1998-12-01     Completed Date:  1998-12-01     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0121103     Medline TA:  Adv Exp Med Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  207-18     Citation Subset:  IM    
Affiliation:
Department of Physiology, Cardiovascular Research Institute Maastricht (CARIM), Maastricht University, The Netherlands.
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MeSH Terms
Descriptor/Qualifier:
Animals
Carrier Proteins / metabolism*
Fatty Acid-Binding Proteins
Fatty Acids / metabolism*
Humans
Muscle, Skeletal / metabolism*
Myelin P2 Protein / metabolism*
Neoplasm Proteins*
Tumor Suppressor Proteins*
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/FABP7 protein, human; 0/Fatty Acid-Binding Proteins; 0/Fatty Acids; 0/Myelin P2 Protein; 0/Neoplasm Proteins; 0/Tumor Suppressor Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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