Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity
Autor: | Diana Zelencova-Gopejenko, Melita Videja, Aiga Grandane, Linda Pudnika-Okinčica, Anda Sipola, Karlis Vilks, Maija Dambrova, Kristaps Jaudzems, Edgars Liepinsh |
---|---|
Jazyk: | angličtina |
Rok vydání: | 2023 |
Předmět: |
Organic Chemistry
long-chain acylcarnitines palmitoylcarnitine fatty acids palmitate heart-type fatty acid-binding protein FABP3 isothermal titration calorimetry nuclear magnetic resonance General Medicine Catalysis Computer Science Applications Inorganic Chemistry Physical and Theoretical Chemistry Molecular Biology Spectroscopy |
Zdroj: | International Journal of Molecular Sciences; Volume 24; Issue 6; Pages: 5528 |
ISSN: | 1422-0067 |
DOI: | 10.3390/ijms24065528 |
Popis: | 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. |
Databáze: | OpenAIRE |
Externí odkaz: | |
Nepřihlášeným uživatelům se plný text nezobrazuje | K zobrazení výsledku je třeba se přihlásit. |