scispace - formally typeset
L

L. De Petrocellis

Researcher at ARCO

Publications -  48
Citations -  4132

L. De Petrocellis is an academic researcher from ARCO. The author has contributed to research in topics: Anandamide & Endocannabinoid system. The author has an hindex of 26, co-authored 48 publications receiving 3946 citations. Previous affiliations of L. De Petrocellis include Olivetti & National Research Council.

Papers
More filters
Journal ArticleDOI

Immunohistochemical localization of cannabinoid type 1 and vanilloid transient receptor potential vanilloid type 1 receptors in the mouse brain

TL;DR: The hypothesis of a functional relationship between the two receptor types in the CNS is supported by using commercially available specific antibodies whose specificity was confirmed by data obtained with brains from cannabinoid type 1 (-/-) and transient receptor potential vanilloid type 1(-/-) mice.
Journal ArticleDOI

Biosynthesis, release and degradation of the novel endogenous cannabimimetic metabolite 2-arachidonoylglycerol in mouse neuroblastoma cells

TL;DR: The results suggest that the Ca2+-induced formation of 2-AG proceeds through the intermediacy of AcAGs but not necessarily through phospholipase C activation, and supports the hypothesis that this cannabimimetic monoacylglycerol might be a physiological neuromodulator.
Journal ArticleDOI

Cannabinoid actions at TRPV channels: effects on TRPV3 and TRPV4 and their potential relevance to gastrointestinal inflammation

TL;DR: This work investigated whether cannabinoids also activate/desensitize two other ‘thermo‐TRP’s’, the TRP channels of vanilloid type‐3 or ‐4 (TRPV3 or TRPV4), and if the TRpV‐inactive cannabichromene (CBC) modifies the expression of TRPv1–4 channels in the gastrointestinal tract.
Journal ArticleDOI

The novel endogenous cannabinoid 2-arachidonoylglycerol is inactivated by neuronal- and basophil-like cells: connections with anandamide.

TL;DR: The hydrolysis of 2-AG was inhibited by typical esterase inhibitors and by more specific blockers of 'fatty acid amide hydrolase' (FAAH), the enzyme catalysing the hydrolyses of the other 'endocannabinoid', anandamide (AEA).