A current review of fatty acid transport proteins (SLC27)

  title={A current review of fatty acid transport proteins (SLC27)},
  author={Andreas Stahl},
  journal={Pfl{\"u}gers Archiv},
  • A. Stahl
  • Published 1 February 2004
  • Biology
  • Pflügers Archiv
Long-chain fatty acids (LCFAs) are not only important metabolites but contribute to many cellular functions including activation of protein kinase C (PKC) isoforms and nuclear transcription factors such as peroxisome proliferator-activated receptors (PPAPs). To assert their diverse effects LCFAs have first to traverse the plasma membrane, a process that can occur either through diffusion or be mediated by proteins. Considerable evidence has accumulated to show that in addition to a diffusional… 

Fatty acid transport proteins

  • R. Gimeno
  • Biology, Chemistry
    Current opinion in lipidology
  • 2007
Modulation of fatty acid transport protein function can result in altered energyHomeostasis and insulin sensitivity, defective skin homeostasis, and altered bile acid metabolism.

Fatty acid transport across cell membranes Slc43a3 is a regulator of free fatty acid uptake and efflux

Slc43a3 seems to regulate fatty acid flux in adipocytes, functioning as a positive regulator of fatty acid efflux and as a negative regulator of omega-3 fatty acid uptake.

Targeting the fatty acid transport proteins (FATP) to understand the mechanisms linking fatty acid transport to metabolism.

The current understanding of vectorial acylation and the contributions by specific FATP and Acsl isoforms are reviewed and the identification of small molecule inhibitors from high throughput screens that inhibit this process are reviewed to provide new insights into the underlying mechanistic basis of this process.

Comparative Biochemical Studies of the Murine Fatty Acid Transport Proteins (FATP) Expressed in Yeast*

Six murine FATP proteins were expressed and characterized in a genetically defined yeast strain and data support the conclusion that the different mmFATP isoforms play unique roles in fatty acid trafficking, including the transport of exogenous long-chain fatty acids.

Evidence for concerted action of FAT/CD36 and FABPpm to increase fatty acid transport across the plasma membrane.

Fatty Acid Transport Proteins: Targeting FATP2 as a Gatekeeper Involved in the Transport of Exogenous Fatty Acids.

The fatty acid transport proteins (FATP) are classified as members of the Solute Carrier 27 (Slc27) family of proteins based on their ability to function in the transport of exogenous fatty acids.

FATP2 is a hepatic fatty acid transporter and peroxisomal very long-chain acyl-CoA synthetase.

A model is proposed in which FATP2 is a multifunctional protein that shows subcellular localization-dependent activity and is a major contributor to peroxisomal (V)LACS activity and hepatic fatty acid uptake, suggesting FATP 2 as a potential novel target for the treatment of nonalcoholic fatty liver disease.



A family of fatty acid transporters conserved from mycobacterium to man.

The identification of four novel murine FATPs will allow a better understanding of the mechanisms whereby LCFAs traverse the lipid bilayer as well as yield insight into the control of energy homeostasis and its dysregulation in diseases such as diabetes and obesity.

Characterization of a Heart-specific Fatty Acid Transport Protein*

The cloning, expression pattern, and subcellular localization of a novel member of the fatty acid transport protein (FATP) family termed FATP6 are reported, suggesting that FATP 6 is involved in heart LCFA uptake, in which it may play a role in the pathogenesis of lipid-related cardiac disorders.

Localization of adipocyte long-chain fatty acyl-CoA synthetase at the plasma membrane.

It is demonstrated for the first time that FACS is an integral membrane protein and a model in which imported LCFAs are immediately esterified at the plasma membrane upon uptake, and in which FATP and FACS function coordinately to facilitate LCFA movement across the plasma membranes of mammalian cells is supported.

Fatty acid transport proteins: a current view of a growing family

Membrane transport of long-chain fatty acids: evidence for a facilitated process.

This review summarizes the body of work that has accumulated related to the mechanism of fatty acid transport and evidence in support of a facilitated uptake process is presented with relation to the different cell types or membrane systems where it was collected.

Transmembrane transport of fatty acids in the heart

  • W. Stremmel
  • Biology
    Molecular and Cellular Biochemistry
  • 2004
The inhibition of uptake of fatty acid but not of glucose by the antibody to MFABP indicated the physiologic significance of this protein as transmembrane carrier in the cellular uptake process of fatty acids.

Regulation of fatty acid transport protein and fatty acid translocase mRNA levels by endotoxin and cytokines.

The results demonstrate that LPS decreased FATP and FAT mRNA expression in adipose tissue, heart, skeletal muscle, brain, spleen, and kidney, tissues in which FA uptake and/or oxidation is decreased during sepsis.

Coordinate Regulation of the Expression of the Fatty Acid Transport Protein and Acyl-CoA Synthetase Genes by PPARα and PPARγ Activators*

Thiazolidinedione antidiabetic agents seem to favor adipocyte-specific FA uptake relative to muscle, perhaps underlying in part the beneficial effects of these agents on insulin-mediated glucose disposal.