Fatty Acid Transporters (FABPpm, FAT, FATP) in Human Muscle

1999 ◽  
Vol 24 (6) ◽  
pp. 515-523 ◽  
Author(s):  
Arend Bonen ◽  
Dragana Miskovic ◽  
Bente Kiens

Recently, a number of putative LCFA transporters have been identified: fatty acid binding protein (FABPpm), fatty acid translocase (FAT/CD36), and fatty acid transport protein (FATP). We have demonstrated, for the first time, that transcripts of all three putative LCFA transporters (FAT mRNA, FATP mRNA, and mAspAT/FABPpm mRNA) are present in human skeletal muscle. Key words: mRNA, membrane


2007 ◽  
Vol 582 (1) ◽  
pp. 393-405 ◽  
Author(s):  
Graham P. Holloway ◽  
Jamie Lally ◽  
James G. Nickerson ◽  
Hakam Alkhateeb ◽  
Laelie A. Snook ◽  
...  


1991 ◽  
Vol 276 (1) ◽  
pp. 203-207 ◽  
Author(s):  
R A Peeters ◽  
J H Veerkamp ◽  
A Geurts van Kessel ◽  
T Kanda ◽  
T Ono

A cDNA clone for the human skeletal-muscle fatty-acid-binding protein (FABP) was isolated by screening of a human adult muscle lambda gt11 expression library with an anti-(muscle FABP) serum. The identify of the clone was confirmed by transcription/translation in vitro in plasmid pSP6.5, followed by immunoprecipitation. The nucleotide sequence of the 551 bp cDNA insert showed an open reading frame of 399 nucleotides, coding for a protein of 133 amino acid residues with a calculated molecular mass of 14858 Da and a pI of 4.94. Only one cysteine residue was found, at position 125. Peptide sequence analyses of human skeletal-muscle and heart FABP, after carbamoylmethylation and lysyl endopeptidase digestion followed by automatic Edman degradation, showed that both proteins are identical. No evidence was found for the existence of isoproteins in muscle. The chromosomal localization of the human muscle FABP gene was determined by analysing 31 human x rodent somatic-cell hybrid lines. The human muscle FABP gene could be assigned to chromosome 1pter-q31.







2004 ◽  
Vol 63 (2) ◽  
pp. 239-244 ◽  
Author(s):  
C. Roepstorff ◽  
J. Wulff Helge ◽  
B. Vistisen ◽  
B. Kiens

The first putative fatty acid transporter identified was plasma membrane fatty acid-binding protein (FABPpm). Later it was demonstrated that this protein is identical to the mitochondrial isoform of the enzyme aspartate aminotransferase. In recent years data from several cell types have emerged, indicating that FABPpm plays a role in the transport of long-chain saturated and unsaturated fatty acids. In the limited number of studies in human skeletal muscle it has been demonstrated that dietary composition and exercise training can influence the content of FABPpm. Ingestion of a fat-rich diet induces an increase in FABPpm protein content in human skeletal muscle in contrast to the decrease seen during consumption of a carbohydrate-rich diet. A similar effect of a fat-rich diet is also observed for cytosolic fatty acid-binding protein and fatty acid translocase/CD36 protein expression. Exercise training up regulates FABPpm protein content in skeletal muscle, but only in male subjects; no significant differences were observed in muscle FABPpm content in a cross-sectional study of female volunteers of varying training status, even though muscle FABPpm content did not depend on gender in the untrained state. A higher utilization of plasma long-chain fatty acids during exercise in males compared with females could explain the gender-dependent influence of exercise training on FABPpm. The mechanisms involved in the regulation of the function and expression of FABPpm protein remain to be clarified.





1997 ◽  
Vol 231 (2) ◽  
pp. 463-465 ◽  
Author(s):  
Bente Kiens ◽  
Søren Kristiansen ◽  
Palle Jensen ◽  
Erik A. Richter ◽  
Lorraine P. Turcotte


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