Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Identification and characterization of a lysosomal transporter for small neutral amino acids
Autore:
Sagne, C; Agulhon, C; Ravassard, P; Darmon, M; Hamon, M; El Mestikawy, S; Gasnier, B; Giros, B;
Indirizzi:
CHU Henri Mondor, INSERM, U513, F-94010 Creteil, France CHU Henri Mondor Creteil France F-94010 M, U513, F-94010 Creteil, France CHU Pitie Salpetriere, INSERM, U288, F-75634 Paris 13, France CHU Pitie Salpetriere Paris France 13 RM, U288, F-75634 Paris 13, France Hop La Pitie Salpetriere, CNRS, UMR 9923, F-75013 Paris, France Hop La Pitie Salpetriere Paris France F-75013 923, F-75013 Paris, France CNRS, UPR 1929, Inst Biol Physicochim, F-75005 Paris, France CNRS Paris France F-75005 , Inst Biol Physicochim, F-75005 Paris, France
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 13, volume: 98, anno: 2001,
pagine: 7206 - 7211
SICI:
0027-8424(20010619)98:13<7206:IACOAL>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
N-ACETYLNEURAMINIC ACID; ARABIDOPSIS-THALIANA; FIBROBLAST LYSOSOMES; MOLECULAR ANALYSIS; VESICULAR GABA; MEMBRANE; CLONING; EXPRESSION; DISORDERS; PERMEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Sagne, C CHU Henri Mondor, INSERM, U513, 8 Rue Gen Sarrail, F-94010 Creteil, France CHU Henri Mondor 8 Rue Gen Sarrail Creteil France F-94010 France
Citazione:
C. Sagne et al., "Identification and characterization of a lysosomal transporter for small neutral amino acids", P NAS US, 98(13), 2001, pp. 7206-7211

Abstract

In eukaryotic cells, lysosomes represent a major site for macromolecule degradation. Hydrolysis products are eventually exported from this acidic organelle into the cytosol through specific transporters. Impairment of this process at either the hydrolysis or the efflux step is responsible of several lysosomal storage diseases, However, most lysosomal transporters, although biochemically characterized, remain unknown at the molecular level. In this study, we report the molecular and functional characterization of a lysosomal amino acid transporter (LYAAT-1), remotely related to a family of H+-coupled plasma membrane and synaptic vesicle amino acid transporters. LYAAT-1 is expressed in most rat tissues, with highest levels in the brain whereit is present in neurons. Upon overexpression in COS-7 cells, the recombinant protein mediates the accumulation of neutral amino acids, such as gamma-aminobutyric acid, L-alanine, and L-proline, through an H+/amino acid symport. Confocal microscopy on brain sections revealed that this transporter colocalizes with cathepsin D, an established lysosomal marker. LYAAT-1 thusappears as a lysosomal transporter that actively exports neutral amino acids from lysosomes by chemiosmotic coupling to the HC-ATPase of these organelles. Homology searching in eukaryotic genomes suggests that LYAAT-1 defines a subgroup of lysosomal transporters in the amino acid/auxin permease family.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 06:01:52