ArticleInternational journal of molecular sciences2023
Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Insulin Resistance and Inflammation.International journal of molecular sciences · 2026Review
- Association Between FABP3 and FABP4 Genes with Changes in Milk Composition and Fatty Acid Profiles in the Native Southern Yellow Cattle Breed.Veterinary sciences · 2025Article
- LC-MS/MS-based simultaneous quantification of acylcarnitines, eicosapentaenoic acid, and docosahexaenoic acid: exploring potential biomarkers in human plasma.Analytical and bioanalytical chemistry · 2025Article
- Identification and Functional Validation ofGenes · 2025Article
- Endothelial dysfunction: mechanisms and contribution to diseases.Acta pharmacologica Sinica · 2024Review
- A versatile delivery vehicle for cellular oxygen and fuels or metabolic sensor? A review and perspective on the functions of myoglobin.Physiological reviews · 2024Review
- EPA and DHA acylcarnitines are less cardiotoxic than are saturated and monounsaturated long-chain acylcarnitines.BioFactors (Oxford, England)Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.