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Lipocalin‐Type Prostaglandin D Synthase Is a Novel Phytocannabinoid‐Binding Protein
Author(s) -
Elmes Matthew W.,
Volpe Anthony D.,
d'Oelsnitz Simon,
Sweeney Joseph M.,
Kaczocha Martin
Publication year - 2018
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1002/lipd.12035
Subject(s) - lipocalin , chemistry , biochemistry , prostaglandin , enzyme , endocannabinoid system , cannabinoid , fatty acid binding protein , receptor , gene
Lipocalin‐type prostaglandin D synthase (L‐PGDS; EC:5.3.99.2) is an enzyme with dual functional roles as a prostaglandin D 2 ‐synthesizing enzyme and as an extracellular transporter for diverse lipophilic compounds in the cerebrospinal fluid (CSF). Transport of hydrophobic endocannabinoids is mediated by serum albumin in the blood and intracellularly by the fatty acid binding proteins, but no analogous transport mechanism has yet been described in CSF. L‐PGDS has been reported to promiscuously bind a wide variety of lipophilic ligands and is among the most abundant proteins found in the CSF. Here, we examine the binding of several classes of endogenous and synthetic ligands to L‐PGDS. Endocannabinoids exhibited low affinity toward L‐PGDS, while cannabinoid metabolites and synthetic cannabinoids displayed higher affinities for L‐PGDS. These results indicate that L‐PGDS is unlikely to function as a carrier for endocannabinoids in the CSF, but it may bind and transport a subset of cannabinoids.