The fatty acid-binding protein from human skeletal muscle

Peeters, Roger A.; Groen, Monique A.in't; Veerkamp, J.H.

doi:10.1016/0003-9861(89)90470-0

Cited by 48 publications

(25 citation statements)

References 40 publications

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“…In myotubes, the amount of H-FABP increases nearly twofold, as in cultured primary rat muscle cells, but is still 30-fold lower than in quadriceps muscle [5,6]. A larger differentiation-dependence of expression of H-FABP was found in the mouse C2C12 cell line, which shows a much lower FABP content in myoblasts [17].…”

Section: Discussionmentioning

confidence: 99%

“…No marked differences were detected in total incorporation among the four different types of clone on both media. The extent of uptake varied for different Table 6 Distribution of [1][2][3][4][5][6][7][8][9][10][11][12][13][14] …”

Section: Distribution Of [ 14 C]palmitic Acid In Neutral and Phospholmentioning

confidence: 99%

“…The function significance of the different FABP types is not clear and may vary with the tissues and the physiological conditions. Adaptation may be related to metabolic requirements of the cell, ligand trafficking and\or modulatory functions.A relation has been observed between fatty acid-oxidation capacity and FABP content of various rat tissues and various human and rat muscles [5][6][7]. FABP content of muscle showed no change under various physiological conditions, except an increase in fast-twitch muscles on chronic electrostimulation and endurance training [7].…”

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confidence: 94%

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Transfection of L6 myoblasts with adipocyte fatty acid-binding protein cDNA does not affect fatty acid uptake but disturbs lipid metabolism and fusion

Prinsen

Veerkamp

1998

Biochemical Journal

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We studied the involvement of fatty acid-binding protein (FABP) in growth, differentiation and fatty acid metabolism of muscle cells by lipofection of rat L6 myoblasts with rat heart (H) FABP cDNA or with rat adipocyte (A) FABP cDNA in a eukaryotic expression vector which contained a puromycin acetyltransferase cassette. Stable transfectants showed integration into the genome for all constructs and type-specific overexpression at the mRNA and protein level for the clones with H-FABP and A-FABP cDNA constructs. The rate of proliferation of myoblasts transfected with rat A-FABP cDNA was 2-fold higher compared with all other transfected cells. In addition, these myoblasts showed disturbed fusion and differentiation, as assessed by morphological examination and creatine kinase activity. Uptake rates of palmitate were equal for all clone types, in spite of different FABP INTRODUCTIONFatty acid-binding proteins (FABPs) belong to a conserved family of intracellular lipid-binding proteins with low molecular mass (14-15 kDa) [1][2][3]. Eight different FABP types have been described : heart, liver, adipose, myelin, intestinal, epidermal, brain and ileal. Many FABP cDNAs have been isolated, cloned and the proteins expressed in bacterial systems. In this way, large amounts of proteins have become available for three-dimensional analysis by crystallography and\or NMR (reviewed in [1,3]). All FABPs studied thus far contain a folding motif designated an up-and-down β-barrel [3].The main function of FABP is thought to be intracellular binding and targeting of fatty acids. FABPs may also modulate the effect of fatty acids on various metabolic enzymes and receptors and cellular processes such as signal transduction and gene expression [1,4]. The function significance of the different FABP types is not clear and may vary with the tissues and the physiological conditions. Adaptation may be related to metabolic requirements of the cell, ligand trafficking and\or modulatory functions.A relation has been observed between fatty acid-oxidation capacity and FABP content of various rat tissues and various human and rat muscles [5][6][7]. FABP content of muscle showed no change under various physiological conditions, except an increase in fast-twitch muscles on chronic electrostimulation and endurance training [7]. Heart FABP (H-FABP) content and fatty acid-oxidation capacity increase in skeletal and heart muscle during postnatal development [7,8]. Some indications of a role Abbreviations used : A-FABP, adipocyte fatty acid-binding protein ; CHO, Chinese hamster ovary ; CK, creatine kinase ; CS, citrate synthase ; D-PBS, Dulbecco's modified PBS ; H-FABP, heart fatty acid-binding protein ; I-FABP, intestinal fatty acid-binding protein ; L-FABP, liver fatty acid-binding protein ; PC, phosphatidylcholine ; PE, phosphatidylethanolamine ; RT, reverse transcriptase ; DMEM, Dulbecco's modified Eagle's medium ; SV40, simian virus 40 ; GAPDH, glyceraldehyde-3-phosphate dehydrogenase ; pac, puromycin acetyltransferase.1 To whom correspondence shou...

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Section: Discussionmentioning

confidence: 99%

Section: Distribution Of [ 14 C]palmitic Acid In Neutral and Phospholmentioning

confidence: 99%

mentioning

confidence: 94%

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Transfection of L6 myoblasts with adipocyte fatty acid-binding protein cDNA does not affect fatty acid uptake but disturbs lipid metabolism and fusion

Prinsen

Veerkamp

1998

Biochemical Journal

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“…H-FABP has a wider tissue distribution than the other FABPs, but is found in the highest concentration in heart and red skeletal muscle (Heuckeroth et al, 1987;Watanabe et al, 1991). Assessment of H-FABP expression in various skeletal muscles suggests that the levels of both protein (Crisman et al, 1987;Claffey et al, 1987;Miller et al, 1988;Paulussen et al, 1989Paulussen et al, , 1990Peeters et al, 1989; Moerkerk, 1993) and mRNA (Heuckeroth et al, 1987;Claffey et al, 1987) correspond to the red oxidative-fibre type content in a given muscle. Thus it appears that the tissue distribution of H-FABP seems to correspond with the degree to which a tissue utilizes fatty acids as a fuel source (Glatz et al, 1988; Moerkerk, 1993).…”

Section: Introductionmentioning

confidence: 99%

Transcriptional regulation of muscle fatty acid-binding protein

Carey

Neufer

Farrar

et al. 1994

Biochemical Journal

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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.

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“…Moreover, if elevation of the serum H-FABP concentration in patients with AD is caused by minor myocardial damage that is associated with acute hemodynamic deterioration, our finding of a positive correlation between length score and the H-FABP value cannot be explained. H-FABP is present in skeletal muscle tissue 11,12 and a long segmental aortic injury can result in an extensive minor injury of skeletal muscle tissue without pain. This can occur because of impaired perfusion of the aortic branches, such as the intercostal arteries, whereas malperfusion, which is preceded by almost complete obstruction of an aortic branch, causes significant local injury of skeletal muscle with pain.…”

Section: Discussionmentioning

confidence: 99%