SLC27A4 Membrane Protein Introduction

Introduction of FATP4

SLC27A4 is encoded by FATP4 or SLC27A4 gene, which consists of 13 exons, produces a transmembrane protein that transports exogenous fatty acids into cells. SLC27A4 is also known as Long-chain fatty acid transport protein 4, Fatty acid transport protein 4 and Solute carrier family 27 member 4. It is a member of the fatty acid transport protein (FATP) family, a group of evolutionarily conserved proteins that are involved in cellular uptake and metabolism of long and very long chain fatty acids. SLC27A4 is the major enzyme producing very long chain fatty acid-CoA for lipid metabolic pathways.

Function of SLC27A4 Membrane Protein

SLC27A4 also renamed as ACSVL4, is a FATP which is broadly distributed in a variety of tissues including the skin, heart, brain, kidney, adipose tissue, skeletal muscle, and liver, and is the only FATP expressed in the small intestine. SLC27A4 is a 72-kDa protein with an N-terminal transmembrane domain, an ER localization signal, and ATP/AMP and FATP motifs. It mediates uptake of LCFA and VLCFA, and plays a central role in epidermal barrier formation. SLC27A4 exhibits low palmitoyl-CoA and high lignoceroyl-CoA synthetase activities. SLC27A4-mediated fatty acid uptake is associated with parameters related to insulin resistance, which is associated with disturbed fatty acid metabolism and homeostasis, such as obesity. SLC27A4 expression is positively correlated with acquired obesity. SLC27A4 is efficient acyl-CoA synthetases for both long and very long-chain fatty acids and is originally proposed to constitute the major intestinal fatty acid transporter. SLC27A4 catalyzes acyl-CoAs for β-oxidation, elongation and desaturation of fatty acids as well as for syntheses of neutral lipids, sphingolipids, and phospholipids, which lead to hepatocellular steatosis.

Fig.1 Regulation of fatty acid uptake by SLC27A4. (Digel, 2011)

Application of SLC27A4 Membrane Protein in Literature

1. Digel M., et al. FATP4 contributes as an enzyme to the basal and insulin-mediated fatty acid uptake of C2C12 muscle cells. American Journal of Physiology-Endocrinology and Metabolism. 2011, 301(5):E785-E796. PubMed ID: 21750264
   
   

   This article reports that SLC27A4 is colocalized to the endoplasmic reticulum by double immunofluorescence and subcellular fractionation, clearly distinct from the plasma membrane. The intrinsic enzymatic activity of SLC27A4 plays a significant role in cellular fatty acid uptake.

2. Seeβle J., et al. Palmitate activation by fatty acid transport protein 4 as a model system for hepatocellular apoptosis and steatosis. Biochim. Biophys. Acta. 2015, 1851(5):549-565. PubMed ID: 25603556
   
   

   This article reveals that the overexpressed of SLC27A4 in Huh-7 cells catalyzes palmitate with increased ACS activity and SLC27A4-sensitized lipoapoptosis was not mediated by ceramides.

3. Zhao M., et al. Sex-specific Alterations in Serology and the Expression of Liver SLC27A4 Protein in Offspring Exposed to High-Fat Diet during Pregnancy and/or Lactation. Lipids. 2018, 53(3):301-311. PubMed ID: 29701266
   
   

   Authors in this group apply HF animal models and conducted a cross-fostering program to reveal the mRNA levels of SLC27A4 in the placenta in the high-fat diet group were significantly upregulated compared to the control diet group, suggesting SLC27A4 plays an important role in regulation lipid metabolism.

4. Li S., et al. Fatty Acid Transport Protein 4 (FATP4) Prevents Light-Induced Degeneration of Cone and Rod Photoreceptors by Inhibiting RPE65 Isomerase. The Journal of neuroscience : the official journal of the Society for Neuroscience. 2013, 33(7):3178-3189. PubMed ID: 23407971
   
   

   This article shows that the accumulation of cytotoxic all-trans retinaldehyde and hyper are up-regulated in SLC27A4-deficient mice, which is susceptible to light-induced photoreceptor degeneration. Meanwhile, SLC27A4 and its products are important roles in protecting photoreceptors from degeneration induced by light damage.

5. Li H., et al. Interactions between FATP4 and ichthyin in epidermal lipid processing may provide clues to the pathogenesis of autosomal recessive congenital ichthyosis. Journal of Dermatological Science. 2013, 69(3):195-201. PubMed ID: 23290633
   
   

   The study suggests that SLC27A4 interacts with ichthyin and TGM1 in lipid processing, which is essential for maintaining the epidermal barrier function. More importantly, the data of this article also hypothesized that ichthyin serves as Mg²⁺ transporter for SLC27A4 in this process.

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Reference

1. Digel M., et al. (2011) FATP4 contributes as an enzyme to the basal and insulin-mediated fatty acid uptake of C2C12 muscle cells. American Journal of Physiology-Endocrinology and Metabolism. 301(5):E785-E796.

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