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Related Experiment Videos

Critical steps in cellular fatty acid uptake and utilization.

Ger J van der Vusse1, Marc van Bilsen, Jan F C Glatz

  • 1Department of Physiology, Cardiovascular Research Institute Maastricht, Maastricht University, Maastricht, The Netherlands. vandervusse@fys.unimaas.nl

Molecular and Cellular Biochemistry
|December 14, 2002
PubMed
Summary

Understanding long-chain fatty acid (FA) transport in mammalian organs remains incomplete. Key proteins like fatty acid translocase (FAT/CD36) and fatty acid-binding proteins (FABPs) facilitate FA uptake and utilization, crucial for cellular energy and preventing toxicity.

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Area of Science:

  • Cellular Biology
  • Metabolic Biochemistry
  • Physiology

Background:

  • Long-chain fatty acid (FA) transport and utilization in mammalian organs are complex and not fully elucidated.
  • Cellular membranes, including endothelial, sarcolemmal, and mitochondrial membranes, present barriers to FA uptake.
  • FA are cytotoxic at high concentrations, necessitating tightly regulated uptake and utilization mechanisms.

Purpose of the Study:

  • To review the current understanding of long-chain fatty acid transport mechanisms in mammalian organs.
  • To identify key proteins and pathways involved in FA uptake, intracellular trafficking, and utilization.
  • To explore the regulatory mechanisms controlling FA flux at short-term and long-term levels.

Main Methods:

  • Literature review and synthesis of existing research on fatty acid metabolism and transport.

Related Experiment Videos

  • Analysis of the roles of membrane-associated proteins (e.g., FABPpm, FAT/CD36, FABPc) in FA uptake.
  • Discussion of intracellular transport (e.g., carnitine-mediated) and utilization pathways (e.g., malonyl-CoA, PPARs).

    • Main Results:

    • Membrane proteins like plasmalemmal fatty acid-binding protein (FABPpm) and fatty acid translocase (FAT/CD36) enhance FA delivery to cells.
    • Cytoplasmic fatty acid-binding proteins (FABPc) facilitate FA diffusion within the cell.
    • Mitochondrial FA transport involves carnitine-mediated mechanisms, and uptake is regulated by FAT translocation and substrate availability.

    Conclusions:

    • FA transport and utilization are tightly regulated by protein-mediated processes and substrate availability to prevent cytotoxicity.
    • Short-term regulation involves protein translocation and substrate gradients, while long-term control is achieved through gene expression modulation.
    • Nuclear transcription factors like PPARs may regulate FA-handling genes, indicating a feedback mechanism for FA metabolism.