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Titolo:
DISSOCIATION OF THE VESICULAR ACETYLCHOLINE TRANSPORTER DOMAINS IMPORTANT FOR HIGH-AFFINITY TRANSPORT RECOGNITION, BINDING OF VESAMICOL ANDTARGETING TO SYNAPTIC VESICLES
Autore:
VAROQUI H; ERICKSON JD;
Indirizzi:
LOUISIANA STATE UNIV,SCH MED,CTR NEUROSCI,2020 GRAVIER ST,SUITE D NEWORLEANS LA 70112 LOUISIANA STATE UNIV,SCH MED,DEPT PHARMACOL NEW ORLEANS LA 70112
Titolo Testata:
JOURNAL OF PHYSIOLOGY-PARIS
fascicolo: 2, volume: 92, anno: 1998,
pagine: 141 - 144
SICI:
0928-4257(1998)92:2<141:DOTVAT>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
TORPEDO; EXPRESSION;
Keywords:
VESICULAR ACETYLCHOLINE TRANSPORTER (VACHT); NEURONAL ISOFORM OF THE VESICULAR MONOAMINE TRANSPORTER (VMAT2); ACETYLCHOLINE; VESAMICOL; SYNAPTIC VESICLES; TARGETING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
13
Recensione:
Indirizzi per estratti:
Citazione:
H. Varoqui e J.D. Erickson, "DISSOCIATION OF THE VESICULAR ACETYLCHOLINE TRANSPORTER DOMAINS IMPORTANT FOR HIGH-AFFINITY TRANSPORT RECOGNITION, BINDING OF VESAMICOL ANDTARGETING TO SYNAPTIC VESICLES", J PHYSL-PAR, 92(2), 1998, pp. 141-144

Abstract

Chimeras between the human vesicular acetylcholine transporter (hVAChT) and the neuronal isoform of the human vesicular monoamine transporter (hVMAT2) have been constructed and stably expressed in a rat pheochromocytoma cell line (PC12) in an effort to identify cholinergic-specific domains of VAChT. Examination of the transport properties of a chimera in which the N-terminal portion (up to putative transmembrane domain II and including the lumenal glycosylated loop) of hVAChT was replaced with hVMAT2 sequences (2/V@NheI) revealed that its apparent affinity for acetylcholine (ACh) was reduced approximately seven-fold compared to wild-type. However, the affinity of this chimera for vesamicol did not significantly differ from hVAChT. Similarly, the 2/V@NheI chimera retained its preferential targeting to the small synaptic-like vesicles found in PC12 cells in agreement with our recently reported observations that the synaptic vesicle targeting domain resides in the cytoplasmic tail of VAChT. ((C) Elsevier, Paris).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/04/20 alle ore 03:59:35