Abstract
The cytosol (105,000 xg supernatant) of nearly all tissues investigated appears to contain one or more proteins with a molecular weight of approximately 14,000 that bind long-chain fatty acids or their CoA and carnitine esters with a rather high affinity. The concentration of these fatty acid-binding proteins (FABPs) is high (30–50 μg mg -1 cytosolic protein) in tissues with a high capacity for fatty acid oxidation (liver, heart) or lipid metabolism (intestinal epithelium). Most investigations have been concentrated on the FABPs from these tissues (reviewed in Bass 1985; Glatz and Veerkamp 1985; Glatz et al. 1985a). FABPs occur in the rat in at least three tissue-specific forms (liver, intestinal and heart FABP), but two distinct forms may be present in one tissue (e.g. liver and intestinal forms in intestine). Liver FABP was also named Z-protein or protein A.
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References
Bass NM (1985) Function and regulation of hepatic and intestinal fatty acid-binding proteins. Chem Phys Lipids 38:95–114
Bass NM, Manning JA (1986) Tissue expression of three structurally different fatty acid-binding proteins from rat heart muscle, liver and intestine. Biochem Biophys Res Commun 137:929–935
Bass NM, Manning JA, Ockner RK, Gordon JL, Seetharam S, Alpers DH (1985) Regulation of the biosynthesis of two distinct fatty acid-binding proteins in rat liver and intestine. J Biol Chem 260:1432–1436
Founder NC, Rahim MH (1983) Self-aggregation, a new property of cardiac fatty acid-binding protein. J Biol Chem 258:2929–2933
Glatz JFC, Veerkamp JH (1985) Intracellular fatty acid-binding proteins. Int J Biochem 17:13–22
Glatz JFC, Paulussen RJA, Veerkamp JH (1985a) Fatty acid-binding proteins from heart. Chem Phys Lipids 38:115–129
Glatz JFC, Janssen AM, Baerwaldt CCF, Veerkamp JH (1985b) Purification and characterization of fatty acid-binding proteins from rat heart and liver. Biochim Biophys Acta 837:57–66
Gordon JL, Lowe JB (1985) Analyzing the structures, functions and evolution of two abundant gastrointestinal fatty acid-binding proteins with recombinant DNA and computational techniques. Chem Phys Lipids 38:137–158
Gordon JL, Elshourbagy N, Lowe JB, Liao WS, Alpers DH, Taylor JM (1985) Tissue specific expression and developmental regulation of two genes coding for rat fatty acid-binding proteins. J Biol Chem 260:2995–2998
Jagschies G, Reers M, Unterberg C, Spener F (1985) Bovine fatty acid-binding proteins. Eur J Biochem 152:537–545
Offner GD, Troxler RF, Brecher P (1986) Characterization of a fatty acid-binding protein from rat heart. J Biol Chem 261:5584–5589
Paulussen RJA, Jansen GPM, Veerkamp JH (1986) Fatty acid-binding capacity of cytosolic proteins of various rat tissues. Biochim Biophys Acta 877:342–349
Sacchettini JC, Said B, Schulz H, Gordon JI (1986) Rat heart fatty acid-binding protein is highly homologous to the murine adipocyte 422 protein and the P2 protein of peripheral nerve myelin. J Biol Chem 261:8218–8223
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© 1987 Springer-Verlag Berlin Heidelberg
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Veerkamp, J.H., Paulussen, R.J.A. (1987). Fatty Acid-Binding Proteins of Various Tissues. In: Paoletti, R., Kritchevsky, D., Holmes, W.L. (eds) Drugs Affecting Lipid Metabolism. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71702-4_18
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DOI: https://doi.org/10.1007/978-3-642-71702-4_18
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