Fatty acid-binding protein

[3] Some family members are also believed to transport lipophilic molecules from outer cell membrane to certain intracellular receptors such as PPAR.

[5] Competition for FABPs may in part or wholly explain the increased circulating levels of endocannabinoids reported after consumption of cannabinoids.

FABPs have broad specificity, including the ability to bind long-chain (C16-C20) fatty acids, eicosanoids, bile salts and peroxisome proliferators.

FABPs demonstrate strong evolutionary conservation and are present in a spectrum of species including Drosophila melanogaster, Caenorhabditis elegans, mouse and human.

FABPs also participate in the uptake of fatty acids from the extracellular environment and their subsequent delivery to specific cellular compartments, such as the nucleus, mitochondria, or endoplasmic reticulum.

Different types of FABPs exhibit tissue-specific expression, ensuring the efficient transport of fatty acids to locations where they are needed most for various cellular processes.

By transporting fatty acids to the nucleus, FABPs can modulate the activity of nuclear receptors involved in transcriptional regulation.

In adipocytes, A-FABP is involved in the storage of fatty acids as triglycerides, while in the liver, L-FABP contributes to the regulation of lipid metabolism and cholesterol homeostasis.

Some prominent examples include: Each type of FABP has a specific role in the metabolism and utilization of fatty acids within its respective tissue, highlighting the functional diversity of this protein family.

Additionally, in cardiovascular diseases, the dysregulation of FABPs in the heart and blood vessels may impact fatty acid utilization and contribute to pathological conditions.

Understanding the specific roles of FABPs in disease states is an active area of research, with potential implications for the development of targeted therapies.

[13] Fatty Acid Binding Proteins (FABPs) have shown significant promise in various medical applications due to their role in cellular lipid metabolism and their involvement in several physiological processes.

Studying their expression and function can contribute to a better understanding of the mechanisms underlying type 2 diabetes, potentially leading to the development of targeted therapies.

Conjugating therapeutic agents with molecules that bind to FABPs may enhance drug delivery to cancer cells expressing these proteins.

Structure of one of the FAB proteins known as Heart-type fatty acid binding protein.
Structure of one of the FABP proteins (FABP3) known as Heart-type fatty acid binding protein .