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SLC27A5 Membrane Protein Introduction

Introduction of SLC27A5

SLC27A5 is encoded by FATP5 or SLC27A5 gene and is also known as Bile acyl-CoA synthetase (BACS), Bile acid-CoA ligase (BA-CoA ligase, BAL), Cholate--CoA ligase, Fatty-acid-coenzyme A ligase, very long-chain 3, Solute carrier family 27 member 5 (SLC27A5). It belongs to the FATP or SLC27 gene family, which comprises of six members, SLC27A1-6, which encode FATP1-6. SLC27A5 mediates the uptake of long chain fatty acids (LCFAs) to the liver and is involved in bile acid re-conjugation during enterohepatic recirculation.

Basic Information of SLC27A5
Protein Name Bile acyl-CoA synthetase
Gene Name SLC27A5
Aliases Bile acyl-CoA synthetase (BACS), Bile acid-CoA ligase (BAL), Fatty acid transport protein 5 (FATP5), Fatty-acid-coenzyme A ligase, very long-chain 3 Solute carrier family 27 member 5 (SLC27A5), Very long-chain acyl-CoA synthetase homolog 2 (VLCS-H2), Very long-chain acyl-CoA synthetase-related protein (VLACSR)
Organism Homo sapiens (Human)
UniProt ID Q9Y2P5
Transmembrane Times 2
Length (aa) 690
Sequence MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWVPHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAFERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVLASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVDPLFVLDNRAQSFRPLTAEMYQAVCEGTWRL

Function of SLC27A5 Membrane Protein

SLC27A5 has been found to be strongly expressed in the liver that is primarily expressed by hepatocytes where it localizes to the basal membrane. Overexpression of SLC27A5 causes an increase in fatty acid uptake, using the fluorescently labeled LCFA analogue C1-BODIPY-C12 and has also been reported to increase long-chain and very-long-chain acyl-CoA synthetase as well as bile acid/CoA synthetase activities. Targeting of SLC27A5 to the hepatocyte/sinusoidal interface is congruent with a role in serum fatty acid uptake and the conjugation of bile acids from the enterohepatic circulation. Hubbard., et al have shown that SLC27A5 clearly enhances the uptake of oleate and also acts as a bile-CoA ligase and SLC27A5 may increase unconjugated bile acids intracellular concentration by metabolic trapping. Loss of SLC27A5 significantly impacted hepatic lipid metabolism. SLC27A5 knockout hepatocytes showed a 50% reduced uptake of both fluorescently and radioactively labeled LCFAs. SLC27A5 is a protein with multiple activities and can contribute to both bile acid reactivation and hepatic fatty acid uptake and lipid accumulation.

Signaling pathway of SLC27A5 in lipid metabolism Fig.1 Signaling pathway of SLC27A5 in lipid metabolism (Park, 2014)

Application of SLC27A5 Membrane Protein in Literature

  1. Doege H., et al. Targeted Deletion of FATP5 Reveals Multiple Functions in Liver Metabolism: Alterations in Hepatic Lipid Homeostasis. Gastroenterology. 2006, 130(4):1245-1258. PubMed ID: 16618416

    The findings of this article support the hypothesis that efficient hepatocellular uptake of LCFAs, and thus liver lipid homeostasis in general, is largely a protein-mediated process requiring SLC27A5. These new insights into the physiological role of SLC27A5 should lead to an improved understanding of liver function and disease.

  2. Ason B., et al. ApoB siRNA-induced Liver Steatosis is Resistant to Clearance by the Loss of Fatty Acid Transport Protein 5 (Fatp5). Lipids. 2011, 46(11):991-1003. PubMed ID: 21826528

    This article reports SLC27A5 is required for long chain fatty acid (LCFA) uptake and bile acid reconjugation by the liver. SLC27A5 knockout mice exhibited lower levels of hepatic triglycerides due to decreased fatty acid uptake, and shRNA-mediated knockdown of SLC27A5 protected mice from diet-induced liver steatosis.

  3. Doege H., et al. Silencing of Hepatic Fatty Acid Transporter Protein 5 in Vivo Reverses Diet-induced Non-alcoholic Fatty Liver Disease and Improves Hyperglycemia. The Journal of Biological Chemistry. 2008, 283(32):22186-22192. PubMed ID: 18524776

    This article suggests that the knockdown of SLC27A5 was also able to reverse already established non-alcoholic fatty liver disease, resulting in significantly improved whole-body glucose homeostasis. The continued activity of hepatic SLC27A5 is required to sustain caloric uptake and fatty acid flux into the liver during high-fat feeding and may present a novel avenue for the treatment of non-alcoholic fatty liver disease.

  4. Castro-Perez JM., et al. Attenuation of Slc27a5 Gene Expression Followed by LC-MS Measurement of Bile Acid Reconjugation Using Metabolomics and a Stable Isotope Tracer Strategy. Journal of Proteome Research. 2011, 10(10):4683-4691. PubMed ID: 21819150

    Authors in this article apply a novel high resolution mass spectrometry method in combination with metabolomics and a stable isotope metabolic tracer to indicate that the silencing of the SLC27A5 (SLC27A5) gene in primary hepatocytes and in mice is involved in the metabolism and reconjugation of bile acids (BAs).

  5. Hubbard B., et al. Mice Deleted for Fatty Acid Transport Protein 5 Have Defective Bile Acid Conjugation and Are Protected From Obesity. Gastroenterology. 2006, 130(4):1259-1269. PubMed ID: 16618417

    This article evaluates the important role for SLC27A5 in bile acid conjugation in vivo in SLC27A5 deletion mice, suggesting a specific requirement for SLC27A5 in reconjugation of bile acids during the enterohepatic recirculation.

SLC27A5 Preparation Options

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Reference

  1. Park J-W., et al. (2014) Ceramide synthases as potential targets for therapeutic intervention in human diseases. Biochim. Biophys. Acta. 1841(5):671-681.

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