http://www.cnr.it/ontology/cnr/individuo/prodotto/ID196940

Unsaturated long-chain N-acyl-vanillyl-amides (N-AVAMs): Vanilloid receptor ligands that inhibit anandamide-facilitated transport and bind to CB1 cannabinoid receptors (Articolo in rivista)

Type

Articolo in rivista (Classe)
Prodotto della ricerca (Classe)

Label

Unsaturated long-chain N-acyl-vanillyl-amides (N-AVAMs): Vanilloid receptor ligands that inhibit anandamide-facilitated transport and bind to CB1 cannabinoid receptors (Articolo in rivista) (literal)

Anno

1999-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

10.1006/bbrc.1999.1105 (literal)

Alternative label

Melck D, Bisogno T, De Petrocellis L, Chuang H, Julius D, Bifulco M, Di Marzo V. (1999)
Unsaturated long-chain N-acyl-vanillyl-amides (N-AVAMs): Vanilloid receptor ligands that inhibit anandamide-facilitated transport and bind to CB1 cannabinoid receptors
in Biochemical and biophysical research communications (Print); Academic Press, San Diego (Stati Uniti d'America)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Melck D, Bisogno T, De Petrocellis L, Chuang H, Julius D, Bifulco M, Di Marzo V. (literal)

Pagina inizio

275 (literal)

Pagina fine

284 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

262 (literal)

Rivista

Biochemical and biophysical research communications (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

1 (literal)

Note

ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

1. CNR, Ist Chim Mol Interesse Biol, Natl Inst Chem Biol Syst, I-80072 Arco Felice, Napoli, Italy 2. CNR, Ist Cibernetica, I-80072 Arco Felice, Napoli, Italy 3. Univ Calif San Francisco, Dept Mol & Cellular Pharmacol, San Francisco, CA 94143 USA 4. Univ Naples, CNR, CEOS, I-80131 Naples, Italy 5. Univ Naples, Dipartimento Biol & Patol Cellulare & Mol, I-80131 Naples, Italy (literal)

Titolo

Unsaturated long-chain N-acyl-vanillyl-amides (N-AVAMs): Vanilloid receptor ligands that inhibit anandamide-facilitated transport and bind to CB1 cannabinoid receptors (literal)

Abstract

We investigated the effect of changing the length and degree of unsaturation of the fatty acyl chain of N-(3-methoxy-4-hydroxy)-benzyl-cis-9-octadecenoamide (olvanil), a ligand of vanilloid receptors, on its capability to: (i) inhibit anandamide-facilitated transport into cells and enzymatic hydrolysis, (ii) bind to CB1 and CB2 cannabinoid receptors, and (iii) activate the VR1 vanilloid receptor. Potent inhibition of [C-14]anandamide accumulation into cells was achieved with C20:4 n-6, C18:3 n-6 and n-3, and C18:2 n-6 N-acyl-vanillyl-amides (N-AVAMs). The saturated analogues and Delta(9)-trans-olvanil were inactive. Activity in CB1 binding assays increased when increasing the number of cis-double bonds in a n-6 fatty acyl chain and, in saturated N-AVAMs, was not greatly sensitive to decreasing the chain length, The C20:4 n-6 analogue (arvanil) was a potent inhibitor of anandamide accumulation (IC50 = 3.6 mu M) and was 4-fold more potent than anandamide on CB1 receptors (Ki = 0.25-0.52 mu M), whereas the C18:3 n-3 N-AVAM was more selective than arvanil for the uptake (IC50 = 8.0 mu M) vs CB1 receptors (Ki = 3.4 mu M). None of the compounds efficiently inhibited [C-14]anandamide hydrolysis or bound to CB2 receptors, All N-AVAMs activated the cation currents coupled to VR1 receptors overexpressed in Xenopus oocytes, In a simple, intact cell model of both vanilloid- and anandamide-like activity, i.e., the inhibition of human breast cancer cell (HBCC) proliferation, arvanil was shown to behave as a \"hybrid\" activator of cannabinoid and vanilloid receptors. (literal)

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