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• W1988491331 abstract "The sigma1 receptor is distinguished for its ability to bind various pharmacological agents including drugs of abuse such as cocaine and methamphetamine. Some endogenous ligands have been identified as putative sigma1 receptor regulators. High affinity ligands for the sigma1 receptor contain a nitrogen atom connected to long alkyl chains. We found that long alkyl chain primary amines including endogenous amines belonging to the sphingolipid family such as d -erythro-sphingosine and sphinganine bind with considerable affinity to the sigma1 receptor but not to the sigma2 receptor. The binding of d -erythro-sphingosine to the sigma1 receptor appears to be competitive in nature as assessed against the radioligand [ 3 H]-(+)-pentazocine. Interestingly, the well studied sphingolipid mediator sphingosine-1 phosphate did not bind to the sigma1 or the sigma2 receptor. Sphingosine is converted to sphingosine-1 phosphate by a family of sphingosine kinases that regulate the relative levels of these two bioactive lipids in the cell. The selective binding of sphingosine but not sphingosine-1 phosphate to the sigma1 receptor suggests a mechanism for regulation of sigma1 receptor activity by the sphingosine kinase. We have successfully reconstituted this hypothetical model in HEK-293 cells overexpressing both the sigma1 receptor and sphingosine kinase-1. The data presented here strongly supports sphingosine as an endogenous modulator of the sigma1 receptor." @default.
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• W1988491331 date "2009-05-01" @default.
• W1988491331 modified "2023-09-24" @default.
• W1988491331 title "The sigma1 receptor interacts with N-alkyl amines and endogenous sphingolipids" @default.
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• W1988491331 doi "https://doi.org/10.1016/j.ejphar.2009.03.003" @default.
• W1988491331 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3194046" @default.
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