Fatty acid-binding protein

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.

The fatty-acid-binding proteins (FABPs) are a family of transport proteins for fatty acids and other lipophilic substances such as eicosanoids and retinoids.[1][2] These proteins are thought to facilitate the transfer of fatty acids between extra- and intracellular membranes.[3] Some family members are also believed to transport lipophilic molecules from outer cell membrane to certain intracellular receptors such as PPAR.[4] The FABPs are intracellular carriers that “solubilize” the endocannabinoid anandamide (AEA), transporting AEA to the breakdown by FAAH, and compounds that bind to FABPs block AEA breakdown, raising its level. The cannabinoids (THC and CBD) are also discovered to bind human FABPs (1, 3, 5, and 7) that function as intracellular carriers, as THC and CBD inhibit the cellular uptake and catabolism of AEA by targeting FABPs.[5] Competition for FABPs may in part or wholly explain the increased circulating levels of endocannabinoids reported after consumption of cannabinoids.[6] Levels of fatty-acid-binding protein have been shown to decline with ageing in the mouse brain, possibly contributing to age-associated decline in synaptic activity.[7]

Fatty Acid Binding Proteins (FABPs) represent a family of proteins that play a pivotal role in cellular lipid metabolism. These proteins act as intracellular carriers, facilitating the transport and utilization of fatty acids within cells. With their diverse tissue-specific distribution and involvement in various cellular processes, FABPs contribute significantly to energy homeostasis, lipid metabolism, and even cellular signaling. Fatty acid-binding proteins (FABPs) are members of the intracellular lipid-binding protein (iLBP) family and are involved in reversibly binding intracellular hydrophobic ligands and trafficking them throughout cellular compartments, including the peroxisomes, mitochondria, endoplasmic reticulum and nucleus.[2] This comprehensive exploration aims to delve into the structure, function, types, and implications of FABPs in health and disease.

  1. ^ Chmurzyńska A (2006). "The multigene family of fatty acid-binding proteins (FABPs): function, structure and polymorphism". Journal of Applied Genetics. 47 (1): 39–48. doi:10.1007/BF03194597. PMID 16424607. S2CID 2622822.
  2. ^ a b Smathers RL, Petersen DR (March 2011). "The human fatty acid-binding protein family: evolutionary divergences and functions". Human Genomics. 5 (3): 170–191. doi:10.1186/1479-7364-5-3-170. PMC 3500171. PMID 21504868.
  3. ^ Weisiger RA (October 2002). "Cytosolic fatty acid binding proteins catalyze two distinct steps in intracellular transport of their ligands". Molecular and Cellular Biochemistry. 239 (1–2): 35–43. doi:10.1023/A:1020550405578. PMID 12479566. S2CID 9608133.
  4. ^ Tan NS, Shaw NS, Vinckenbosch N, Liu P, Yasmin R, Desvergne B, et al. (July 2002). "Selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating transcription". Molecular and Cellular Biology. 22 (14): 5114–5127. doi:10.1128/MCB.22.14.5114-5127.2002. PMC 139777. PMID 12077340.
  5. ^ Deutsch DG (2016-10-13). "A Personal Retrospective: Elevating Anandamide (AEA) by Targeting Fatty Acid Amide Hydrolase (FAAH) and the Fatty Acid Binding Proteins (FABPs)". Frontiers in Pharmacology. 7: 370. doi:10.3389/fphar.2016.00370. PMC 5062061. PMID 27790143.
  6. ^ Elmes MW, Kaczocha M, Berger WT, Leung K, Ralph BP, Wang L, et al. (April 2015). "Fatty acid-binding proteins (FABPs) are intracellular carriers for Δ9-tetrahydrocannabinol (THC) and cannabidiol (CBD)". The Journal of Biological Chemistry. 290 (14): 8711–8721. doi:10.1074/jbc.M114.618447. PMC 4423662. PMID 25666611.
  7. ^ Pu L, Igbavboa U, Wood WG, Roths JB, Kier AB, Spener F, Schroeder F (August 1999). "Expression of fatty acid binding proteins is altered in aged mouse brain". Molecular and Cellular Biochemistry. 198 (1–2): 69–78. doi:10.1023/A:1006946027619. PMID 10497880. S2CID 6180992.