Effects of Cys mutation on taurocholic acid transport by mouse ileal and hepatic sodium-dependent bile acid transporters.
All cysteines of mouse ileal and hepatic sodium-dependent bile acid transporters (Isbt and Ntcp, respectively) were individually replaced by alanine. Replacement of Cys106 in Isbt and Cys96 in Ntcp, which are located closely in alignment, decreased taurocholate uptake. Although Cys51 in Isbt is conserved in Ntcp, the replacement spoiled Isbt only. Both similarity and difference in the arrangement of functional sites are suggested.
Saeki
Tohru
T
Department of Biological Resource Chemistry, Faculty of Agriculture, Kyoto Prefectural University, Japan. tsaeki@kpu.ac.jp
Kuroda
Toshinori
T
Matsumoto
Makiko
M
Kanamoto
Ryuhei
R
Iwami
Kimikazu
K
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003545:Cysteine / Q000235:genetics*; D006913:Hydroxysteroid Dehydrogenases; D007082:Ileum / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D008562:Membrane Glycoproteins; D051379:Mice; D008969:Molecular Sequence Data; D009154:Mutation; D017386:Sequence Homology, Amino Acid; D012964:Sodium / Q000378:metabolism*; D013656:Taurocholic Acid / Q000378:metabolism*; D045002:3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)
D002352:Carrier Proteins; D003545:Cysteine; D006913:Hydroxysteroid Dehydrogenases; D008562:Membrane Glycoproteins; D012964:Sodium; D013656:Taurocholic Acid; C037643:bile acid binding proteins; C435496:AKR1C2 protein, human; D045002:3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)