TY - JOUR
T1 - Transport of bestatin in rat renal brush-border membrane vesicles
AU - Ryohei, Hori
AU - Yoshiko, Tomita
AU - Toshiya, Katsura
AU - Masato, Yasuhara
AU - Ken-Ichi, Inui
AU - Mikihisa, Takano
PY - 1993/5/5
Y1 - 1993/5/5
N2 - Bestatin [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-l-leucine] is a dipeptide, comprising l-leucine and an unusual β-ammo acid. We studied its transport mechanism in rat renal brush-border membrane vesicles. Uptake of cephradine, an aminocephalosporin, by isolated brush-border membrane vesicles was trans-stimulated and cis-inhibited by bestatin, indicating that these drugs are transported via the same transport system(s). The uptake of bestatin was trans-stimulated by preloading the vesicles with glycylsarcosine, and was cis-inhibited by substrates for the H+/dipeptide cotransport system. Bestatin inhibited tetraethylammonium (an organic cation) uptake, and bestatin uptake was cis-inhibited by substrates for the H+/organic cation antiport system. In addition, bestatin uptake was stimulated by an outward H+ gradient (the driving force for the H+/organic cation antiport system). These findings suggest that bestatin, in spite of being a dipeptide, is transported via not only the H+/dipeptide cotransport system but also the H+/organic cation antiport system in rat renal brush-border membrane.
AB - Bestatin [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-l-leucine] is a dipeptide, comprising l-leucine and an unusual β-ammo acid. We studied its transport mechanism in rat renal brush-border membrane vesicles. Uptake of cephradine, an aminocephalosporin, by isolated brush-border membrane vesicles was trans-stimulated and cis-inhibited by bestatin, indicating that these drugs are transported via the same transport system(s). The uptake of bestatin was trans-stimulated by preloading the vesicles with glycylsarcosine, and was cis-inhibited by substrates for the H+/dipeptide cotransport system. Bestatin inhibited tetraethylammonium (an organic cation) uptake, and bestatin uptake was cis-inhibited by substrates for the H+/organic cation antiport system. In addition, bestatin uptake was stimulated by an outward H+ gradient (the driving force for the H+/organic cation antiport system). These findings suggest that bestatin, in spite of being a dipeptide, is transported via not only the H+/dipeptide cotransport system but also the H+/organic cation antiport system in rat renal brush-border membrane.
UR - https://www.scopus.com/pages/publications/0027324899
U2 - 10.1016/0006-2952(93)90431-U
DO - 10.1016/0006-2952(93)90431-U
M3 - 記事
C2 - 8494534
AN - SCOPUS:0027324899
SN - 0006-2952
VL - 45
SP - 1763
EP - 1768
JO - Biochemical Pharmacology
JF - Biochemical Pharmacology
IS - 9
ER -