Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family.

Détails

ID Serval
serval:BIB_12375
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family.
Périodique
EMBO Journal
Auteur(s)
Pfeiffer R., Rossier G., Spindler B., Meier C., Kühn L., Verrey F.
ISSN
0261-4189
Statut éditorial
Publié
Date de publication
1999
Volume
18
Numéro
1
Pages
49-57
Langue
anglais
Notes
Publication types: In Vitro
Résumé
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 approximately 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. The mRNA 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/secretion in many cell types, is the basolateral amino acid exchanger involved in transepithelial reabsorption of cationic amino acids; hence, its defect might be the cause of the human genetic disease lysinuric protein intolerance.
Mots-clé
Amino Acid Sequence, Amino Acid Transport Systems, Amino Acids/metabolism, Animals, Antigens, CD/chemistry, Antigens, CD/genetics, Antigens, CD98, Biological Transport, Active, Carrier Proteins/chemistry, Carrier Proteins/genetics, Dimerization, Female, Glycoproteins/chemistry, Glycoproteins/genetics, Humans, Mice, Molecular Sequence Data, Oocytes/metabolism, RNA, Messenger/genetics, RNA, Messenger/metabolism, Sequence Homology, Amino Acid, Tissue Distribution, Xenopus laevis
Pubmed
Web of science
Création de la notice
19/11/2007 13:03
Dernière modification de la notice
20/08/2019 13:40
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