Lipocalin-Type Prostaglandin D Synthase Is a Novel Phytocannabinoid-Binding Protein
© 2018 AOCS..
Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5.3.99.2) is an enzyme with dual functional roles as a prostaglandin D2 -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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2018 |
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| Erschienen: |
2018 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:53 |
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| Enthalten in: |
Lipids - 53(2018), 3 vom: 26. März, Seite 353-360 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Elmes, Matthew W [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 08.04.2019 Date Revised 25.02.2020 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1002/lipd.12035 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM283162856 |
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| 245 | 1 | 0 | |a Lipocalin-Type Prostaglandin D Synthase Is a Novel Phytocannabinoid-Binding Protein |
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| 520 | |a © 2018 AOCS. | ||
| 520 | |a Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5.3.99.2) is an enzyme with dual functional roles as a prostaglandin D2 -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 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, N.I.H., Extramural | |
| 650 | 4 | |a Cannabinoid | |
| 650 | 4 | |a Endocannabinoid | |
| 650 | 4 | |a Lipocalin | |
| 650 | 4 | |a Lipocalin-type prostaglandin D synthase | |
| 650 | 4 | |a N-Acylethanolamine | |
| 650 | 4 | |a Prostaglandin | |
| 650 | 7 | |a 7-nitrobenzo-2-oxa-1,3-diazole |2 NLM | |
| 650 | 7 | |a Cannabinoids |2 NLM | |
| 650 | 7 | |a Dansyl Compounds |2 NLM | |
| 650 | 7 | |a Fatty Acids |2 NLM | |
| 650 | 7 | |a Lipocalins |2 NLM | |
| 650 | 7 | |a Nitrobenzenes |2 NLM | |
| 650 | 7 | |a Oxadiazoles |2 NLM | |
| 650 | 7 | |a Prostaglandins |2 NLM | |
| 650 | 7 | |a Recombinant Proteins |2 NLM | |
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| 650 | 7 | |a 11-(dansylamino)undecanoic acid |2 NLM | |
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| 650 | 7 | |a Tryptophan |2 NLM | |
| 650 | 7 | |a 8DUH1N11BX |2 NLM | |
| 650 | 7 | |a Intramolecular Oxidoreductases |2 NLM | |
| 650 | 7 | |a EC 5.3.- |2 NLM | |
| 650 | 7 | |a prostaglandin R2 D-isomerase |2 NLM | |
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| 700 | 1 | |a Volpe, Anthony D |e verfasserin |4 aut | |
| 700 | 1 | |a d'Oelsnitz, Simon |e verfasserin |4 aut | |
| 700 | 1 | |a Sweeney, Joseph M |e verfasserin |4 aut | |
| 700 | 1 | |a Kaczocha, Martin |e verfasserin |4 aut | |
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