The novel endogenous cannabinoid 2-arachidonoylglycerol is inactivated by neuronal- and basophil-like cells: connections with anandamide (Articolo in rivista)

Type
Label
  • The novel endogenous cannabinoid 2-arachidonoylglycerol is inactivated by neuronal- and basophil-like cells: connections with anandamide (Articolo in rivista) (literal)
Anno
  • 1998-01-01T00:00:00+01:00 (literal)
Alternative label
  • Di Marzo V, Bisogno T, Sugiura T, Melck D, De Petrocellis L. (1998)
    The novel endogenous cannabinoid 2-arachidonoylglycerol is inactivated by neuronal- and basophil-like cells: connections with anandamide
    in Biochemical journal (Lond., 1984); PORTLAND PRESS,, LONDON W1N 3AJ ENGLAND (Regno Unito)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Di Marzo V, Bisogno T, Sugiura T, Melck D, De Petrocellis L. (literal)
Pagina inizio
  • 15 (literal)
Pagina fine
  • 19 (literal)
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  • 331 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
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  • 1. CNR, Ist Chim Mol Interesse Biol, I-80072 Arco Felice, Napoli, Italy 2. Teikyo Univ, Fac Pharmaceut Sci, Kanagawa, Japan 3. CNR, Ist Cibernet, I-80072 Arco Felice, Napoli, Italy 4. CNR, Natl Inst Chem Biol Syst, I-00185 Rome, Italy (literal)
Titolo
  • The novel endogenous cannabinoid 2-arachidonoylglycerol is inactivated by neuronal- and basophil-like cells: connections with anandamide (literal)
Abstract
  • The novel endogenous cannabinoid 2-arachidonoylglycerol (2-AG) was rapidly inactivated by intact rat basophilic leukaemia (RBL-2H3) and mouse neuroblastoma (N18TG2) cells through diffusion/hydrolysis/reacylation processes. 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 hydrolysis of the other 'endocannabinoid', anandamide (AEA). No evidence for a facilitated-diffusion process was found. A 2-AG-hydrolysing activity was detected in homogenates from both cell lines, with the highest levels in membrane fractions. It exhibited an optimal pH at 10, and recognized both 2- and 1(3)- isomers of monoarachidonoylglycerol with similar efficiencies. The apparent K-m and V-max valuer for [H-3]2-AG hydrolysis were 91 mu M and 29 mu M and 2.4 and 1.8 nmol.min(-1).mg of protein(-1) respectively in N18TG2 and RBL-2H3 cells. [H-3]2-AG hydrolysis was inhibited by Cu2+, Zn2+ and p-hydroxymercuribenzoate, and by 2- or 1(3)-monolinoleoyl- and -linolenoyl-glycerols, but not by the oleoyl, palmitoyl and myristoyl congeners. Purified fractions from solubilized membrane proteins catalysed, at pH 9.5, the hydrolysis of 2-AG as well as AEA. Accordingly, AEA as well as FAAH inhibitors, including arachidonoyltrifluoromethyl ketone (ATFMK), blocked [H-3]2-AG hydrolysis by N18TG2 and RBL-2H3 membranes, whereas 2-AG inhibited [C-14]AEA hydrolysis. FAAH blockade by ATFMK preserved from inactivation the 2-AG synthesized ne novo by intact N18TG2 cells stimulated with ionomycin. These data suggest that FAAH may be one of the enzymes deputed to the physiological inactivation of 2-AG, and create intriguing possibilities for the cross-regulation of 2-AG and AEA levels. (literal)
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