Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

Diana Zelencova-Gopejenko (Coresponding Author), Melita Videja, Aiga Grandane, Linda Pudnika-Okinčica, Anda Sipola, Karlis Vilks, Maija Dambrova, Kristaps Jaudzems, Edgars Liepinsh

Research output: Contribution to journalArticlepeer-review


Heart-type fatty-acid binding protein (FABP3) is an essential cytosolic lipid transport protein found in cardiomyocytes. FABP3 binds fatty acids (FAs) reversibly and with high affinity. Acylcarnitines (ACs) are an esterified form of FAs that play an important role in cellular energy metabolism. However, an increased concentration of ACs can exert detrimental effects on cardiac mitochondria and lead to severe cardiac damage. In the present study, we evaluated the ability of FABP3 to bind long-chain ACs (LCACs) and protect cells from their harmful effects. We characterized the novel binding mechanism between FABP3 and LCACs by a cytotoxicity assay, nuclear magnetic resonance, and isothermal titration calorimetry. Our data demonstrate that FABP3 is capable of binding both FAs and LCACs as well as decreasing the cytotoxicity of LCACs. Our findings reveal that LCACs and FAs compete for the binding site of FABP3. Thus, the protective mechanism of FABP3 is found to be concentration dependent.

Original languageEnglish
Article number5528
JournalInternational Journal of Molecular Sciences
Issue number6
Publication statusPublished - 14 Mar 2023


  • Fatty Acid Binding Protein 3/metabolism
  • Fatty Acid-Binding Proteins/metabolism
  • Fatty Acids pharmacology
  • Carnitine
  • Myocytes
  • Cardiac metabolism
  • isothermal titration calorimetry
  • long-chain acylcarnitines

Field of Science*

  • 1.6 Biological sciences
  • 3.1 Basic medicine

Publication Type*

  • 1.1. Scientific article indexed in Web of Science and/or Scopus database


Dive into the research topics of 'Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity'. Together they form a unique fingerprint.

Cite this