skip to main content
Idioma:
Primo Search
Clear Search Box
Search in: Busca Geral
Busca Avançada
Busca por Índices

Identification and Characterization of a Na+-independent Neutral Amino Acid Transporter That Associates with the 4F2 Heavy Chain and Exhibits Substrate Selectivity for Small Neutral d- and l-Amino Acids

Fukasawa, Yoshiki ; Segawa, Hiroko ; Kim, Ju Young ; Chairoungdua, Arthit ; Kim, Do Kyung ; Matsuo, Hirotaka ; Cha, Seok Ho ; Endou, Hitoshi ; Kanai, Yoshikatsu

The Journal of biological chemistry, 2000-03, Vol.275 (13), p.9690-9698 [Periódico revisado por pares]

United States: Elsevier Inc

Texto completo disponível

Citações Citado por
  • Título:
    Identification and Characterization of a Na+-independent Neutral Amino Acid Transporter That Associates with the 4F2 Heavy Chain and Exhibits Substrate Selectivity for Small Neutral d- and l-Amino Acids
  • Autor: Fukasawa, Yoshiki ; Segawa, Hiroko ; Kim, Ju Young ; Chairoungdua, Arthit ; Kim, Do Kyung ; Matsuo, Hirotaka ; Cha, Seok Ho ; Endou, Hitoshi ; Kanai, Yoshikatsu
  • Assuntos: Amino Acid Sequence ; Amino Acid Transport Systems ; Amino Acids - metabolism ; Animals ; Biological Transport ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; DNA, Complementary ; Hydrogen-Ion Concentration ; Mice ; Molecular Sequence Data ; Rats ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Sequence Homology, Amino Acid ; Sodium - metabolism ; Substrate Specificity ; Xenopus
  • É parte de: The Journal of biological chemistry, 2000-03, Vol.275 (13), p.9690-9698
  • Descrição: A cDNA was isolated from the mouse brain that encodes a novel Na+-independent neutral amino acid transporter. The encoded protein, designated as Asc-1 (asc-type amino acid transporter 1), was found to be structurally related to recently identified mammalian amino acid transporters for the transport systems L, y+L, xC−, and b0,+, which are linked, via a disulfide bond, to the type II membrane glycoproteins, 4F2 heavy chain (4F2hc), or rBAT (related to b0,+ amino acid transporter). Asc-1 required 4F2hc for its functional expression. In Western blot analysis in the nonreducing condition, a 118-kDa band, which seems to correspond to the heterodimeric complex of Asc-1 and 4F2hc, was detected in the mouse brain. The band shifted to 33 kDa in the reducing condition, confirming that Asc-1 and 4F2hc are linked via a disulfide bond. Asc-1-mediated transport was not dependent on the presence of Na+ or Cl−. Although Asc-1 showed a high sequence homology (66% identity at the amino acid level) to the Na+-independent broad scope neutral amino acid transporter LAT2 (Segawa, H., Fukasawa, Y., Miyamoto, K., Takeda, E., Endou, H., and Kanai, Y. (1999)J. Biol. Chem. 274, 19745–19751), Asc-1 also exhibited distinctive substrate selectivity and transport properties. Asc-1 preferred small neutral amino acids such as Gly,l-Ala, l-Ser, l-Thr, andl-Cys, and α-aminoisobutyric acid as substrates. Asc-1 also transported d-isomers of the small neutral amino acids, in particular d-Ser, a putative endogenous modulator of N-methyl-d-aspartate-type glutamate receptors, with high affinity. Asc-1 operated preferentially, although not exclusively, in an exchange mode. Asc-1 mRNA was detected in the brain, lung, small intestine, and placenta. The functional properties of Asc-1 seem to be consistent with those of a transporter subserving the Na+-independent small neutral amino acid transport system asc.
  • Editor: United States: Elsevier Inc
  • Idioma: Inglês
Links
Voltar para lista de resultados

  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

Buscando em bases de dados remotas. Favor aguardar.