Differential influence of the 4F2 heavy chain and the protein related to b0,+ amino acid transport on substrate affinity of the heteromeric b0,+ amino acid transporter

D. Prasanna Rajan, Wei Huang, Ramesh Kekuda, Ronald L. George, Jian Wang, Simon J. Conway, Lawrence D Devoe, Frederick H. Leibach, Puttur D Prasad, Vadivel Ganapathy

Research output: Contribution to journalArticle

44 Scopus citations

Abstract

We provide evidence here that b0,+ amino acid transporter (b0,+ AT) interacts with 4F2 heavy chain (4F2hc) as well as with the protein related to b amino acid transporter (rBAT) to constitute functionally competent b0,+-like amino acid transport systems. This evidence has been obtained by co-expression of b0,+ AT and 4F2hc or b0,+AT and rBAT in human retinal pigment epithelial cells and in COS-1 cells. The ability to interact with 4F2hc and rBAT is demonstrable with mouse b0,+AT as well as with human b0,+AT. Even though both the 4F2hc.b0,+AT complex and the rBAT·b0,+ AT complex exhibit substrate specificity that is characteristic of system b0,+, these two complexes differ significantly in substrate affinity. The 4F2hc·b0,+AT complex has higher substrate affinity than the rBAT·b0,+AT complex. In situ hybridization studies demonstrate that the regional distribution pattern of mRNA in the kidney is identical for b0,+ AT and 4F2hc. The pattern of rBAT mRNA expression is different from that of b0,+AT mRNA and 4F2hc mRNA, but there are regions in the kidney where b0,+AT mRNA expression overlaps with rBAT mRNA expression as well as with 4F2hc mRNA expression.

Original languageEnglish (US)
Pages (from-to)14331-14335
Number of pages5
JournalJournal of Biological Chemistry
Volume275
Issue number19
DOIs
StatePublished - May 12 2000

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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