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Titolo:
Amino acid transport of y(+)L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family
Autore:
Pfeiffer, R; Rossier, G; Spindler, B; Meier, C; Kuhn, L; Verrey, F;
Indirizzi:
Univ Zurich, Inst Physiol, CH-8057 Zurich, Switzerland Univ Zurich Zurich Switzerland CH-8057 siol, CH-8057 Zurich, Switzerland Swiss Inst Expt Canc Res, CH-1066 Epalinges, Switzerland Swiss Inst Expt Canc Res Epalinges Switzerland CH-1066 nges, Switzerland
Titolo Testata:
EMBO JOURNAL
fascicolo: 1, volume: 18, anno: 1999,
pagine: 49 - 57
SICI:
0261-4189(19990104)18:1<49:AATOYB>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
XENOPUS-LAEVIS OOCYTES; ECOTROPIC RETROVIRUS RECEPTOR; MONOCLONAL-ANTIBODY 4F2; CELL-SURFACE ANTIGEN; HUMAN ERYTHROCYTES; HEAVY-CHAIN; SYSTEM Y(+)L; RAT-KIDNEY; EXPRESSION; MEMBRANE;
Keywords:
amino acid exchanger; epithelial transport; lysinuric protein intolerance; Xenopus oocytes;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Verrey, F Univ Zurich, Inst Physiol, Winterthurerstr 190, CH-8057 Zurich, Switzerland Univ Zurich Winterthurerstr 190 Zurich Switzerland CH-8057 land
Citazione:
R. Pfeiffer et al., "Amino acid transport of y(+)L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family", EMBO J, 18(1), 1999, pp. 49-57

Abstract

Amino acid transport across cellular membranes is mediated by multiple transporters with overlapping specificities. We recently have identified the vertebrate proteins which mediate Na+-independent exchange of large neutral amino acids corresponding to transport system L. This transporter consists of a novel amino acid permease-related protein (LAT1 or AmAT-L-lc) which for surface expression and function requires formation of disulfide-linked heterodimers with the glycosylated heavy chain of the h4F2/CD98 surface antigen. We show that h4F2hc also associates with other mammalian light chains, e.g. y(+)LAT1 from mouse and human which are similar to 48% identical with LAT1 and thus belong to the same family of glycoprotein-associated amino acid transporters. The novel heterodimers form exchangers which mediate the cellular efflux of cationic amino acids and the Na+-dependent uptake of large neutral amino acids. These transport characteristics and kinetic and pharmacological fingerprints identify them as y(+)L-type transport systems. ThemRNA encoding my(+)LAT1 is detectable in most adult tissues and expressed at high levels in kidney cortex and intestine, This suggests that the y(+)LAT1-4F2hc heterodimer, besides participating in amino acid uptake/secretionin many cell types, is the basolateral amino acid exchanger involved in transepithelial reabsorption of cationic amino acids; hence, its defect mightbe the cause of the human genetic disease lysinuric protein intolerance.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/01/21 alle ore 07:50:36