Oligomeric structure of a renal cystine transporter: implications in cystinuria Academic Article uri icon

Overview

MeSH Major

  • Phospholipid Transfer Proteins

abstract

  • Homologous proteins (NBAT) which mediate sodium-independent transport of neutral as well as basic amino acids and cystine when expressed in Xenopus oocytes were recently cloned from mammalian kidneys. Mutations in human NBAT have been implicated in cystinuria. Here, we show that rat kidney and jejunal brush border membrane NBAT (85 kDa) is found in association with a 50 kDa protein. The association involves one or more interprotein disulfide bonds. Rabbit kidney brush border membranes and membranes of NBAT cRNA-injected Xenopus oocytes also contain such heterodimers. Our data suggest that the heterodimer is the minimal functional unit of NBAT-mediated amino acid transport and that the NBAT-associated 50 kDa protein could play a role in cystinuria.

publication date

  • July 17, 1995

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1016/0014-5793(95)00685-3

Additional Document Info

start page

  • 389

end page

  • 92

volume

  • 368

number

  • 2