Biology:FABP5

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Fatty acid-binding protein, epidermal is a protein that in humans is encoded by the FABP5 gene.[1][2]

Function

This gene encodes the fatty acid binding protein found in epidermal cells, and was first identified as being upregulated in psoriasis tissue. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism.[2]

The phytocannabinoids (THC and CBD) inhibit endocannabinoid anandamide (AEA) uptake by targeting FABP5, and competition for FABPs may in part or wholly explain the increased circulating levels of endocannabinoids reported after consumption of cannabinoids.[3] Results show that cannabinoids inhibit keratinocyte proliferation, and therefore support a potential role for cannabinoids in the treatment of psoriasis.[4]

Interactions

FABP5 has been shown to interact with S100A7.[5][6]

References

  1. "Molecular cloning and expression of a novel keratinocyte protein (psoriasis-associated fatty acid-binding protein [PA-FABP]) that is highly up-regulated in psoriatic skin and that shares similarity to fatty acid-binding proteins". The Journal of Investigative Dermatology 99 (3): 299–305. September 1992. doi:10.1111/1523-1747.ep12616641. PMID 1512466. 
  2. 2.0 2.1 "Entrez Gene: FABP5 fatty acid binding protein 5 (psoriasis-associated)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2171. 
  3. "Fatty acid-binding proteins (FABPs) are intracellular carriers for Δ9-tetrahydrocannabinol (THC) and cannabidiol (CBD)". The Journal of Biological Chemistry 290 (14): 8711–21. April 2015. doi:10.1074/jbc.M114.618447. PMID 25666611. 
  4. "Cannabinoids inhibit human keratinocyte proliferation through a non-CB1/CB2 mechanism and have a potential therapeutic value in the treatment of psoriasis" (in en). Journal of Dermatological Science 45 (2): 87–92. February 2007. doi:10.1016/j.jdermsci.2006.10.009. PMID 17157480. https://www.jdsjournal.com/article/S0923-1811(06)00315-X/fulltext. 
  5. "S100A7 (psoriasin) interacts with epidermal fatty acid binding protein and localizes in focal adhesion-like structures in cultured keratinocytes". The Journal of Investigative Dermatology 121 (1): 132–41. July 2003. doi:10.1046/j.1523-1747.2003.12309.x. PMID 12839573. 
  6. "Probable interaction between S100A7 and E-FABP in the cytosol of human keratinocytes from psoriatic scales". Molecular and Cellular Biochemistry 192 (1–2): 123–8. February 1999. doi:10.1023/A:1006894909694. PMID 10331666. 

Further reading