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A role for the FAAH‐interacting protein ERp57 in endogenous cannabinoid signaling
Author(s) -
Yates Marla Leigh,
Barker Eric L
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1177-a
Subject(s) - fatty acid amide hydrolase , anandamide , endocannabinoid system , cannabinoid receptor , microbiology and biotechnology , cannabinoid , gpr18 , g protein coupled receptor , chemistry , endocytic cycle , cannabinoid receptor type 2 , signal transduction , biology , receptor , biochemistry , agonist , endocytosis
Cannabinoid receptor signaling is currently an active area of research due to therapeutic implications for analgesia, anxiety, appetite modulation, and regulation of immune responses. The long‐chain fatty acid amide anandamide (AEA) is an endogenous agonist for the central nervous system and peripheral cannabinoid receptors CB1 and CB2, respectively. AEA is a putative neurotransmitter, and as such, a mechanism must exist for synaptic inactivation of endogenous cannabinoid signaling. The primary mechanism for AEA inactivation is thought to be transport into cells, followed by metabolism by fatty acid amide hydrolase (FAAH). We have shown that AEA reuptake occurs via a protein carrier‐mediated caveolae‐related endocytic process. The current objective of our research is to identify specific proteins that play a role in this process. We have discovered that ERp57 localizes to caveolin‐rich membranes upon AEA treatment. Furthermore, we have identified ERp57 as a FAAH‐interacting protein. Finally, RNAi strategies have been used to knockdown ERp57 expression in order to explore its putative function in AEA uptake and FAAH activity. This research supported by grant R21 DA018844 from NIH.