scholarly journals Cloning of the cDNA encoding human skeletal-muscle fatty-acid-binding protein, its peptide sequence and chromosomal localization

1991 ◽  
Vol 276 (1) ◽  
pp. 203-207 ◽  
Author(s):  
R A Peeters ◽  
J H Veerkamp ◽  
A Geurts van Kessel ◽  
T Kanda ◽  
T Ono
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Human Skeletal Muscle ◽  
Fatty Acid Binding Protein ◽  
Chromosomal Localization ◽  
Human Muscle ◽  
Peptide Sequence ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Fabp Gene

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.

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

scholarly journals Studies of plasma membrane fatty acid-binding protein and other lipid-binding proteins in human skeletal muscle

2004 ◽  
Vol 63 (2) ◽  
pp. 239-244 ◽  
Author(s):  
C. Roepstorff ◽  
J. Wulff Helge ◽  
B. Vistisen ◽  
B. Kiens
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Exercise Training ◽  
Human Skeletal Muscle ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Membrane Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Long Chain

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.

Fatty acid binding protein 4 in human skeletal muscle

2006 ◽  
Vol 346 (1) ◽  
pp. 125-130 ◽  
Author(s):  
Heléne Fischer ◽  
Thomas Gustafsson ◽  
Carl Johan Sundberg ◽  
Jessica Norrbom ◽  
Marianne Ekman ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Human Skeletal Muscle ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

The fatty acid-binding protein from human skeletal muscle

1989 ◽  
Vol 274 (2) ◽  
pp. 556-563 ◽  
Author(s):  
Roger A. Peeters ◽  
Monique A.in't Groen ◽  
Jacques H. Veerkamp
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Human Skeletal Muscle ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Up-regulation of the expression of the gene for liver fatty acid-binding protein by long-chain fatty acids

1996 ◽  
Vol 319 (2) ◽  
pp. 483-487 ◽  
Author(s):  
Claire MEUNIER-DURMORT ◽  
Hélène POIRIER ◽  
Isabelle NIOT ◽  
Claude FOREST ◽  
Philippe BESNARD
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Fold Increase ◽  
Long Chain Fatty Acids ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Fabp Gene ◽  
Long Chain

The role of fatty acids in the expression of the gene for liver fatty acid-binding protein (L-FABP) was investigated in the well-differentiated FAO rat hepatoma cell line. Cells were maintained in serum-free medium containing 40 µM BSA/320 µM oleate. Western blot analysis showed that oleate triggered an approx. 4-fold increase in the cytosolic L-FABP level in 16 h. Oleate specifically stimulated L-FABP mRNA in time-dependent and dose-dependent manners with a maximum 7-fold increase at 16 h in FAO cells. Preincubation of FAO cells with cycloheximide prevented the oleate-mediated induction of L-FABP mRNA, showing that protein synthesis was required for the action of fatty acids. Run-on transcription assays demonstrated that the control of L-FABP gene expression by oleate was, at least in part, transcriptional. Palmitic acid, oleic acid, linoleic acid, linolenic acid and arachidonic acid were similarly potent whereas octanoic acid was inefficient. This regulation was also found in normal hepatocytes. Therefore long-chain fatty acids are strong inducers of L-FABP gene expression. FAO cells constitute a useful tool for studying the underlying mechanism of fatty acid action.

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