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]

Family membersEdit

Members of this family include:

Protein name Gene Tissue distribution Comment
FABP 1 FABP1 liver
FABP 2 FABP2 intestinal
FABP 3 FABP3 muscle and heart mammary-derived growth inhibitor
FABP 4 FABP4 adipocyte
FABP 5 FABP5 epidermal psoriasis-associated
FABP 6 FABP6 ileal gastrotropin
FABP 7 FABP7 brain
FABP 8 PMP2 peripheral nervous system peripheral myelin protein 2
FABP 9 FABP9
FABP 11 fabp11 restricted to fishes
FABP 12 FABP12 presence shown in human retinoblastoma cell lines, rodent retina and testis.[8]

PseudogenesEdit

Pseudogene Comment
FABP3P2
FABP5P1
FABP5P2
FABP5P3
FABP5P4
FABP5P5
FABP5P6
FABP5P7
FABP5P8
FABP5P9
FABP5P10
FABP5P11
FABP5P12
FABP5P13
FABP5P14
FABP5P15
FABP7P1
FABP7P2
FABP12P1

ReferencesEdit

  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.
  2. ^ Smathers RL, Petersen DR (March 2011). "The human fatty acid-binding protein family: evolutionary divergences and functions". Human Genomics. 5 (3): 170–91. 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.
  4. ^ Tan NS, Shaw NS, Vinckenbosch N, Liu P, Yasmin R, Desvergne B, Wahli W, Noy N (July 2002). "Selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating transcription". Molecular and Cellular Biology. 22 (14): 5114–27. 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, Sweeney JM, Miyauchi JT, Tsirka SE, Ojima I, Deutsch DG (April 2015). "Fatty acid-binding proteins (FABPs) are intracellular carriers for Δ9-tetrahydrocannabinol (THC) and cannabidiol (CBD)". The Journal of Biological Chemistry. 290 (14): 8711–21. 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.
  8. ^ Liu RZ, Li X, Godbout R (December 2008). "A novel fatty acid-binding protein (FABP) gene resulting from tandem gene duplication in mammals: transcription in rat retina and testis". Genomics. 92 (6): 436–45. doi:10.1016/j.ygeno.2008.08.003. PMID 18786628.

External linksEdit