Does fatty acid-binding protein play a role in fatty acid transport?

1989 ◽  
Vol 88 (1-2) ◽  
Author(s):  
RogerA. Peeters ◽  
JacquesH. Veerkamp
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Transport ◽  
Acid Transport ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals A Polymorphism in the Human Intestinal Fatty Acid Binding Protein Alters Fatty Acid Transport across Caco-2 Cells

1996 ◽  
Vol 271 (18) ◽  
pp. 10892-10896 ◽  
Author(s):  
Leslie J. Baier ◽  
Clifton Bogardus ◽  
James C. Sacchettini
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Transport ◽  
Acid Transport ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Fatty acid binding protein facilitates sarcolemmal fatty acid transport but not mitochondrial oxidation in rat and human skeletal muscle

2007 ◽  
Vol 582 (1) ◽  
pp. 393-405 ◽  
Author(s):  
Graham P. Holloway ◽  
Jamie Lally ◽  
James G. Nickerson ◽  
Hakam Alkhateeb ◽  
Laelie A. Snook ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Human Skeletal Muscle ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Transport ◽  
Acid Transport ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Mitochondrial Oxidation

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

1999 ◽  
Vol 24 (6) ◽  
pp. 515-523 ◽  
Author(s):  
Arend Bonen ◽  
Dragana Miskovic ◽  
Bente Kiens
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Human Skeletal Muscle ◽  
Fatty Acid Binding Protein ◽  
Human Muscle ◽  
Fatty Acid Transport ◽  
Acid Transport ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
First Time

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

Expression pattern of fatty acid transport protein-1 (FATP-1), FATP-4 and heart-fatty acid binding protein (H-FABP) genes in human term placenta

2006 ◽  
Vol 82 (10) ◽  
pp. 697-701 ◽  
Author(s):  
Elvira Larqué ◽  
Hans Demmelmair ◽  
Mario Klingler ◽  
Sylvia De Jonge ◽  
Brigitta Bondy ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Expression Pattern ◽  
Fatty Acid Binding Protein ◽  
Fatty Acid Transport ◽  
Acid Transport ◽  
Fatty Acid Binding ◽  
Human Term Placenta ◽  
Fatty Acid Transport Protein ◽  
Term Placenta ◽  
Acid Binding Protein

Fatty acid binding protein in heart and skeletal muscles of the migratory barnacle goose throughout development

1999 ◽  
Vol 276 (3) ◽  
pp. R637-R643 ◽  
Author(s):  
Maurice M. A. L. Pelsers ◽  
Patrick J. Butler ◽  
Charles M. Bishop ◽  
Jan F. C. Glatz
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Muscle Protein ◽  
Binding Protein ◽  
Fatty Acid Transport ◽  
Long Distance ◽  
Barnacle Goose ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

The long-distance migratory flights of birds are predominantly fueled by the oxidation of fatty acids, which are sourced primarily from extracellular adipose stores. These fatty acids have to be transported, via the circulatory system, to the mitochondria of the active muscles. An important facilitator of fatty acid transport within the cytoplasm of muscle cells is fatty acid binding protein (FABP), which serves as an intracellular carrier of long-chain fatty acids. In mammals, the muscular FABP content is related to the fatty acid oxidation capacity of the tissue. The aim of this study was to measure FABP in samples taken from the cardiac, pectoralis, and semimembranosus muscles of a long-distance avian migrant, the barnacle goose ( Branta leucopsis), at various stages of development. Western blot analysis identified a single goose muscle protein of 15 kDa that was able to bind fatty acids and showed a 66% cross-reactivity with antibodies against human heart-type FABP. Captive goslings showed no significant changes in FABP content of either the heart (62.6 ± 10.6 μg/g wet wt) or the semimembranosus muscle (8.4 ± 1.9 μg/g wet wt) during development. However, in both peripheral and deep sites within the pectoralis muscle, FABP content of samples taken from captive goslings were ∼10-fold higher throughout development and reached values of 30–40 μg/g wet wt in fledging goslings at 7 wk of age. A further twofold higher value was seen in wild but not in captive goslings immediately before migration (12 wk of age). Similarly, FABP content was significantly higher in pectoralis samples taken from wild adults (94.3 ± 3.6 μg/g wet wt) compared with those from captive adults (60.5 ± 3.6 μg/g wet wt). These results suggest that the experience of flight activity may be of critical importance in achieving maximal expression of FABP in the pectoralis muscles of postfledging and mature geese immediately before migration.

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