Cytoplasmic fatty acid-binding protein facilitates fatty acid utilization by skeletal muscle

2003 ◽  
Vol 178 (4) ◽  
pp. 367-371 ◽  
Author(s):  
J. F. C. Glatz ◽  
F. G. Schaap ◽  
B. Binas ◽  
A. Bonen ◽  
G. J. Van Der Vusse ◽  
...  
1994 ◽  
Vol 298 (3) ◽  
pp. 613-617 ◽  
Author(s):  
J O Carey ◽  
P D Neufer ◽  
R P Farrar ◽  
J H Veerkamp ◽  
G L Dohm

Heart fatty acid-binding protein (H-FABP) is present in a wide variety of tissues but is found in the highest concentration in cardiac and red skeletal muscle. It has been proposed that the expression of H-FABP correlates directly with the fatty acid-oxidative capacity of the tissue. In the present study, the expression of H-FABP was measured in red and white skeletal muscle under two conditions in which fatty acid utilization is known to be increased: streptozotocin-induced diabetes and fasting. Protein concentration, mRNA concentration and transcription rate were measured under both conditions. The level of both protein and mRNA increased approximately 2-fold under each condition. The transcription rate was higher in red skeletal muscle than in white muscle, was increased 2-fold during fasting, but was unchanged by streptozotocin-induced diabetes. In addition to supporting the hypothesis that H-FABP is induced during conditions of increased fatty acid utilization, these findings demonstrate that the regulation of H-FABP expression may or may not be at the level of transcription depending on the stimulus.


Biochemistry ◽  
1987 ◽  
Vol 26 (24) ◽  
pp. 7900-7904 ◽  
Author(s):  
Kevin P. Claffey ◽  
Victoria L. Herrera ◽  
Peter Brecher ◽  
Nelson Ruiz-Opazo

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.


1999 ◽  
Vol 13 (8) ◽  
pp. 805-812 ◽  
Author(s):  
Bert Binas ◽  
Heike Danneberg ◽  
Jim Mcwhir ◽  
Linda Mullins ◽  
A. John Clark

2006 ◽  
Vol 346 (1) ◽  
pp. 125-130 ◽  
Author(s):  
Heléne Fischer ◽  
Thomas Gustafsson ◽  
Carl Johan Sundberg ◽  
Jessica Norrbom ◽  
Marianne Ekman ◽  
...  

Proteomes ◽  
2013 ◽  
Vol 1 (3) ◽  
pp. 290-308 ◽  
Author(s):  
Zulezwan Malik ◽  
James Cobley ◽  
James Morton ◽  
Graeme Close ◽  
Ben Edwards ◽  
...  

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