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NAPEPLD is a phospholipase D type enzyme that catalyzes the release of N-acylethanolamine (NAE) from N-acyl-phosphatidylethanolamine (NAPE) in the second step of the biosynthesis of N-acylethanolamine (Okamoto et al., 2004 [PubMed 14634025]).[supplied by OMIM, Oct 2008].. Additionally we are shipping NAPEPLD Antibodies (37) and NAPEPLD Kits (4) and many more products for this protein.
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NAPE-PLD forms homodimers partly separated by an internal channel and uniquely adapted to associate with phospholipids.
our results do not support a clear role of FAAH (show FAAH Proteins), CNR1 (show CNR1 Proteins) and NAPE-PLD in BD and lithium response.
a major physiological role of NAPE-PLD
The differential expression of NAPE-PLD and FAAH (show FAAH Proteins) suggests that Anandamide could play an important role in the pathophysiology of preeclampsia.
NAPE-PLD expression increase steadily after infancy, peaking in adulthood.
The results of this study suggested that NAPEPLD was alterated in multip;e sclerosis.
a common haplotype in NAPEPLD, an enzyme involved in endocannabinoid synthesis, was protective against obesity.
During the menstrual cycle, NAPE-PLD immunoreactivity was down-regulated in the secretory epithelial gland compared to the proliferative epithelial gland and unaffected in the stroma.
The human NAPE-PLD was activated by phosphatidylethanolamine and inhibited by the beta-lactamase (show LACTB Proteins) substrate nitrocefin.
Data indicate that N-acyl phosphatidylethanolamine phospholipase D (NAPE-PLD) knockout mice showed a broad range of lipids that were differentially affected by lipid species and brain region.
Adipose tissue NAPE-PLD controls fat mass development by altering the browning process and gut (show GUSB Proteins) microbiota.
Authors demonstrated that phospholipase D and diacylglycerol lipase (show LIPG Proteins) were required for providing arachidonic acid for prostaglandin E(2) biosynthesis.
Phospholipase D is dispensable for superoxide production and degranulation in mouse neutrophils.
Suppression of NAPE-PLD expression and palmitoylethanolamide biosynthesis in peritoneal macrophage culture might contribute to an inflammatory response.
results confirm that overexpressed NAPE-PLD is capable of forming NAEs, including anandamide, in living cells
Inactivation of N-acyl phosphatidylethanolamine phospholipase D reveals multiple mechanisms for the biosynthesis of endocannabinoids.
Results support the existence of an N-acyl phosphatidylethanolamine (NAPE)-phospholipase D-independent route for N-acyl ethanolamine (NAE) biosynthesis and suggest that Abh4 (show ABHD4 Proteins) plays a role in this pathway by acting as a (lyso)NAPE-selective lipase (show LIPG Proteins).
We suggest that NAEs generated by NAPE-PLD in axons may act as anterograde synaptic signaling molecules that regulate the activity of postsynaptic neurons.
NAPEPLD is a phospholipase D type enzyme that catalyzes the release of N-acylethanolamine (NAE) from N-acyl-phosphatidylethanolamine (NAPE) in the second step of the biosynthesis of N-acylethanolamine (Okamoto et al., 2004
N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
, NAPE-hydrolyzing phospholipase D
, Metallo-beta-lactamase domain containing 1