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Titolo:
Transport mechanisms in acetylcholine and monoamine storage
Autore:
Parsons, SM;
Indirizzi:
Univ Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USAUniv Calif Santa Barbara Santa Barbara CA USA 93106 Barbara, CA 93106 USA Univ Calif Santa Barbara, Program Biochem & Mol Biol, Santa Barbara, CA 93106 USA Univ Calif Santa Barbara Santa Barbara CA USA 93106 Barbara, CA 93106 USA
Titolo Testata:
FASEB JOURNAL
fascicolo: 15, volume: 14, anno: 2000,
pagine: 2423 - 2434
SICI:
0892-6638(200012)14:15<2423:TMIAAM>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHOLINERGIC SYNAPTIC VESICLES; VESICULAR NEUROTRANSMITTER TRANSPORTERS; CHROMAFFIN GRANULE MEMBRANES; VESAMICOL RECEPTOR; AMINE TRANSPORTER; SUBSTRATE RECOGNITION; RESERPINE BINDING; ACTIVE-TRANSPORT; CATECHOLAMINE TRANSPORTER; RESIDUES CONTRIBUTE;
Keywords:
vesicular acetylcholine transporter; vesicular monoamine transporter neurotransmitter transport;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
84
Recensione:
Indirizzi per estratti:
Indirizzo: Parsons, SM Univ Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USA Univ Calif Santa Barbara Santa Barbara CA USA 93106 93106 USA
Citazione:
S.M. Parsons, "Transport mechanisms in acetylcholine and monoamine storage", FASEB J, 14(15), 2000, pp. 2423-2434

Abstract

Sequence-related vesicular acetylcholine transporter (VAChT) and vesicularmonoamine transporter (VMAT) transport neurotransmitter substrates into secretory vesicles. This review seeks to identify shared and differentiated aspects of the transport mechanisms. VAChT and VMAT exchange two protons persubstrate molecule with very similar initial velocity kinetics and pH dependencies. However, vesicular gradients of ACh in vivo are much smaller thanthe driving force for uptake and vesicular gradients of monoamines, suggesting the existence of a regulatory mechanism in ACh storage not found in monoamine storage, The importance of microscopic rather than macroscopic kinetics in structure-function analysis is described, Transporter regions affecting binding or translocation of substrates, inhibitors, and protons have been found with photoaffinity labeling, chimeras, and single-site mutations,VAChT and VMAT exhibit partial structural and mechanistic homology with lactose permease, which belongs to the same sequence-defined superfamily, despite opposite directions of substrate transport. The vesicular transporterstranslocate the first proton using homologous aspartates in putative transmembrane domain X (ten), but they translocate the second proton using unknown residues that might not be conserved between them. Comparative analysis of the VAChT and VMAT transport mechanisms will aid understanding of regulation in neurotransmitter storage.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/21 alle ore 04:10:29