Disease relevance of Slc27a1

• Northern blot analysis revealed that, compared with normal liver tissue, hepatoma 7288CTC overexpressed mRNA transcripts for a plasma membrane-associated FA transport protein (FATP) [1].
• In this range the reduced FATP with P can largely be attributed to decreased metabolic demand of contraction, as evident from a comparison with the responses to hypoxia of portal veins relaxed in nominally Ca2+-free medium [2].

High impact information on Slc27a1

• FATP mRNA expression was unaffected by the treatment of tumor-bearing rats with daily afternoon melatonin injections or exposure to constant light [1].
• These studies provide the first evidence that protein-mediated long chain fatty acid transport is subject to long term regulation by leptin [3].
• Through the use of heterodimer-selective compounds, it was demonstrated that the modulatory effect of these rexinoids on FATP-1 and ACS gene expression was mediated through activation of RXR in the context of the PPAR-RXR heterodimer [4].
• The aim of this investigation was to determine the effects of retinoic acid derivatives on the expression of FATP-1 and ACS [4].
• In several cultured cell lines, it was shown that the expression of both the FATP-1 and ACS mRNAs was specifically induced at the transcriptional level by selective retinoid X receptor (RXR) but not by retinoic acid receptor (RAR) ligands [4].

Chemical compound and disease context of Slc27a1

• The calculated ATP production (FATP) was linearly related to P for P greater than 10% of the control value in 96% O2, with the same slope for hypoxia and both inhibitors [2].

Biological context of Slc27a1

• The inferred amino acid sequence indicates that rat FATP is highly homologous (97%) with its murine equivalent [5].
• Fatty acid translocase (FAT) transfection did not significantly increase the palmitate uptake rate, raising the possibility that H9c2 cells lack a protein (or set of proteins) that acts as an obligatory partner of FAT in long-chain fatty acid transport from the extracellular compartment to the cytoplasm [6].
• Fatty acid transport was stimulated using different cAMP derivatives with varying susceptibilities to hydrolysis by the cAMP-degrading enzyme phosphodiesterase [7].

Anatomical context of Slc27a1

• 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 [4].
• Here, we demonstrate for the first time that FABPpm and FATP1 are also present in intracellular depots in cardiac myocytes [8].
• Adipocyte mRNA levels of three putative transporters, mitochondrial aspartate aminotransferase, fatty acid translocase, and fatty acid transporting protein (FATP) were also determined; mitochondrial aspartate aminotransferase and FATP mRNAs correlated strongly with fatty acid uptake [9].
• Long chain fatty acid transport is selectively up-regulated in adipocytes of Zucker fatty rats, diverting fatty acids from sites of oxidation toward storage in adipose tissue [10].
• Fatty acid transport through the blood-brain barrier [11].

Associations of Slc27a1 with chemical compounds

• BACKGROUND/AIMS: Carnitine is a co-factor of the enzymatic system involved in long chain fatty acid transport across the mitochondrial membrane [12].

Other interactions of Slc27a1

• In the presence of DEHP, MEHP, and EHA, the expression of PPARalpha, PPARgamma, FATP1, and HFABP were up-regulated in a dose- and time- dependent manner, while PPARbeta and FABPpm demonstrated variable expression [13].

Analytical, diagnostic and therapeutic context of Slc27a1

• Gene expression for rat fatty acid transport protein (FATP) and fatty acid translocase (FAT) were examined by Northern and in situ hybridization analysis [14].
• Western blot analysis demonstrated that Caco-2 cells express a protein immunoreactive with antibodies to the rat liver plasma membrane fatty acid binding protein (FABPpm), which is thought to be involved in long chain fatty acid transport [15].

References