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Titolo:
A new class of scorpion toxin binding sites related to an A-type K+ channel: pharmacological characterization and localization in rat brain
Autore:
Vacher, H; Romi-Lebrun, R; Mourre, C; Lebrun, B; Kourrich, S; Masmejean, F; Nakajima, T; Legros, C; Crest, M; Bougis, PE; Martin-Eauclaire, MF;
Indirizzi:
Univ Mediterranee, UMR 6560 CNRS, Inst Jean Roche, Fac Med Nord, F-13916 Marseille 20, France Univ Mediterranee Marseille France 20 Nord, F-13916 Marseille 20, France Univ Aix Marseille 1, UMR 6565 CNRS, Marseille, France Univ Aix Marseille 1 Marseille France UMR 6565 CNRS, Marseille, France Suntory Inst Bioorgan Res, Osaka, Japan Suntory Inst Bioorgan Res Osaka Japan y Inst Bioorgan Res, Osaka, Japan LNCF, CNRS, Marseille, France LNCF Marseille FranceLNCF, CNRS, Marseille, France Univ Hamburg, ZMNH, Inst Neurale Signalverarbeitung, Hamburg, Germany UnivHamburg Hamburg Germany urale Signalverarbeitung, Hamburg, Germany ITIS, FRE 2362, Marseille, France ITIS Marseille FranceITIS, FRE 2362, Marseille, France
Titolo Testata:
FEBS LETTERS
fascicolo: 1, volume: 501, anno: 2001,
pagine: 31 - 36
SICI:
0014-5793(20010713)501:1<31:ANCOST>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
POTASSIUM CHANNELS; BUTHUS-MARTENSI; MCD PEPTIDE; VENOM; CHARYBDOTOXIN; PURIFICATION; KALIOTOXIN; APAMIN; SEQUENCE; AFFINITY;
Keywords:
A-type K+ current; scorpion toxin; distribution in rat brain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Martin-Eauclaire, MF Univ Mediterranee, UMR 6560 CNRS, Inst Jean Roche, Fac Med Nord, Blvd Pierre Dramard, F-13916 Marseille 20, France Univ Mediterranee Blvd Pierre Dramard Marseille France 20
Citazione:
H. Vacher et al., "A new class of scorpion toxin binding sites related to an A-type K+ channel: pharmacological characterization and localization in rat brain", FEBS LETTER, 501(1), 2001, pp. 31-36

Abstract

A new scorpion toxin (3751.8 Da) was isolated from the Buthus martensi venom, sequenced and chemically synthesized (sBmTX3), The A-type current of striatum neurons in culture completely disappeared when 1 muM sBmTX3 was applied (K-d = 54 nM), whereas the sustained K+ current was unaffected. I-125-sBmTX3 specifically bound to rat brain synaptosomes (maximum binding = 14 fmol mg(-1) of protein, K-d = 0.21 nM). A panel of toxins yet described as specific ligands for K+ channels were unable to compete with I-125-sBmTX3. A high density of I-125-sBmTX3 binding sites was found in the striatum, hippocampus, superior colliculus, and cerebellum in the adult rat brain. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 01:06:27