Fatty acid transport protein

Gene activated Lipoprotein lipase fatty acid transporter protein adipocyte fatty acid binding protein acyl-CoA synthetase malic enzyme GLUT-4 glucose transporter phosphoenolpyruvate carboxykinase... 

Fatty acid transport protein paralogues 1-6 FATP 1-6 Gene symbols SLC27A1-6 Solute carrier family 27A Very long-chain acyl-CoA synthetase VLCS... 

Fatty acid transport proteins (FATPs) are an evolutionary conserved family of integral membrane proteins found at the plasma membrane and on internal membranes. FATPs facilitate the unidirectional uptake and/ or intracellular activation of unesterified long-chain and very long-chain fatty acids (LCFAs) into a variety of lipid-metabolizing cells and tissues. 

Schaffer, J. E. and H. F. Lodish. Expression cloning and characterization of a novel adipocyte long chain fatty acid transport protein. Cell 1994, 79, 427-436. 

Stahl, A., et al. Identification of the major intestinal fatty acid transport protein. Mol. Cell 1999, 4, 299-308. 

Herrmann, T., et al. Mouse fatty acid transport protein 4 (FATP4) characterization of the gene and functional assessment as a very long chain acyl-CoA synthetase. Gene 2001, 270,... 

Martin, G., et al. The human fatty acid transport protein-1 (SLC27A1 FATP-1) cDNA and gene organization, chromosomal localization, and expression. Genomics 2000, 66, 296—304. 

Intestinal fatty acid transport protein (FATP4)... 

Chiu, H. C., Kovacs, A., Blanton, R. M., et al. (2005) Transgenic expression of fatty acid transport protein 1 in the heart causes lipotoxic cardiomyopathy. Circ. Res. 96, 225-233. 

Several studies have evaluated the effects of oral di(2-ethylhexyl) adipate on various aspects of hepatic lipid metabolism. Feeding di(2-ethylhexyl) adipate (2% of diet) to male Wistar rats for seven days resulted in increased hepatic fatty acid-binding protein as well as in increased microsomal stearoyl-CoA desaturation activity (Kawashima et al., 1983a,b). Feeding the compound at this dose for 14 days resulted in increased levels of hepatic phospholipids and a decline in phosphatidyl-choline phosphatidylethanolamine ratio (Yanagita et al., 1987). Feeding di(2-ethyl-hexyl) adipate (2% of diet) to male NZB mice for five days resulted in induction of fatty acid translocase, fatty acid transporter protein and fatty acid binding protein in the liver (Motojima et al., 1998). 

Martin, G., Poirier, H., Hennuyer, N., Crombie, D., Fruchart, J. C., Heyman, R. A., Besnard, P., and Auwerx, J. (2000). Induction Of The Fatty Acid Transport Protein 1 and Acyl-Coa Synthase Genes by Dimer-Selective Rexinoids Suggests That the Peroxisome Proliferator-Activated Receptor-Retinoid X Receptor Heterodimer is Their Molecular Target./ Bid. Chem. 275, 12612-12618. 

In the intestine fatty acid translocase (FAT), fatty acid transporting protein (FATP4) and fatty acid binding protein (FABPpm) have been identified (for review, see Stahl 2003). Natural substrates are long chain fatty acids like myristate, oleate, palmitoate. 

Stahl A (2003) A current review of fatty acid transport proteins (SLC27). Pflugers Arch 447(5) 722-727... 

Long-chain fatty acids were previously believed to enter cells by diffusion, but evidence now implicates a family of protein-mediated transporters, the fatty acid transport protein (FATP) family. Internally, fatty acid-binding proteins (FABPs) constimte a family of low-molecular-weight proteins that function as intracellular transporters of fatty acids. 

Fatty acid transport protein 1 (FATPl) and long chain acyl-CoA synthetase 1 (ASCLl) were identified as components of a fatty acid transport system in expression cloning experiments, which specifically targeted cellular fatty acid uptake (15). As both FATP and ACSLl were selected in these experiments, it was suggested that fatty acid transport occurred by a coupled transport-activation (15). This mechanism was first shown to occur in gram-negative bacteria and is referred to as vectorial acylation (3). Six different isoforms of FATP have subsequently been identified experimentally in mice, rats, and humans (e.g., in mice, mmFATPl-6). 

Hui TY, Frohnert BI, Smith AJ, Schaffer JE, Bernlohr DA. Characterization of the murine fatty acid transport protein gene and its insulin response sequence. J. Biol. Chem. 1998 273 27420-27429. 

Kim JK, Gimeno RE, Higashimori T, Kim HJ, Choi H, Punreddy S, Mozell RL, Tan G, Stricker-Krongrad A, Hirsch DJ, Fillmore, JJ, Liu ZX, Dong J, CUne G, Stahl A, Lodish HF, Shul-man GI. Inactivation of fatty acid transport protein 1 prevents fat-induced insulin resistance in skeletal muscle. J. CUn. Invest. 2004 113 756-763. 

Herrmann T, van der Hoeven F, Grone HJ, Stewart AF, Langbein L, Kaiser I, Liebisch G, Gosch I, Buchkremer F, Drobnik W, Schmitz G, Stremmel W. Mice with targeted disruption of the fatty acid transport protein 4 (Fatp 4, Slc27a4) gene show features of lethal restrictive dermopathy. J. Cell. Biol. 2003 161 1105-1115. 

Fatty acids are more efficiently degraded because of increased synthesis of molecules that facilitate fatty acid transport and oxidation. The concentration of citric acid cycle and (3-oxidation enzymes increases, as well as the components of the ETC. In addition, the capacity of the muscle cell to remove fatty acids from blood and to transport them into mitochondria increases. For example, increases in the synthesis of fatty acid transporter proteins and fatty acid-binding proteins, as well as carnitine and carnitine acyltransferase, have been observed. 

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