The Experts below are selected from a list of 1251 Experts worldwide ranked by ideXlab platform
Ryohei Hori - One of the best experts on this subject based on the ideXlab platform.
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Bestatin transport in rabbit intestinal brush border membrane vesicles
Biochemical Pharmacology, 1994Co-Authors: Mikihisa Takano, Toshiya Katsura, Ken-ichi Inui, Yoshiko Tomita, Masato Yasuhara, Ryohei HoriAbstract:The effect of papain treatment on Bestatin uptake by rabbit intestinal brush-border membrane vesicles (BBMVs) was studied. Papain treatment of BBMVs effectively diminished aminopeptidase activity but not Bestatin uptake by a H+/dipeptide cotransporter. Bestatin uptake by BBMVs was composed of two saturable components, and after papain treatment the high-affinity component disappeared while the low-affinity component was retained. These findings suggest that high- and low-affinity components represent Bestatin binding to aminopeptidase and the true uptake by the H+/dipeptide cotransporter, respectively.
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h coupled active transport of Bestatin via the dipeptide transport system in rabbit intestinal brush border membranes
Journal of Pharmacology and Experimental Therapeutics, 1992Co-Authors: Ken-ichi Inui, Mikihisa Takano, Toshiya Katsura, Yoshiko Tomita, Tomonobu Okano, Ryohei HoriAbstract:Bestatin [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-leucine], a dipeptide containing an unusual amino acid, has been used clinically as an anticancer agent in p.o. dosage form. We examined the transport characteristics of [3H]Bestatin by rabbit intestinal brush-border membrane vesicles. Bestatin uptake was stimulated by an inward H+ gradient (overshoot phenomenon) and by an interior-negative membrane potential. About half of the apparent Bestatin uptake at 1 mM by brush-border membrane vesicles was estimated as binding to the membranes. The affinity constant for the Bestatin transport was 0.52 mM. The uptake of Bestatin by brush-border membrane vesicles was inhibited by p.o. cephalosporins and dipeptides, but not by amino acids. In vesicles preloaded with either Bestatin, cephradine or glycylsarcosine, the uptake of [3H]Bestatin was stimulated markedly (countertransport effect). These results indicate that Bestatin is transported via the H+/dipeptide transport system in rabbit intestinal brush-border membranes.
Ken-ichi Inui - One of the best experts on this subject based on the ideXlab platform.
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Bestatin transport in rabbit intestinal brush border membrane vesicles
Biochemical Pharmacology, 1994Co-Authors: Mikihisa Takano, Toshiya Katsura, Ken-ichi Inui, Yoshiko Tomita, Masato Yasuhara, Ryohei HoriAbstract:The effect of papain treatment on Bestatin uptake by rabbit intestinal brush-border membrane vesicles (BBMVs) was studied. Papain treatment of BBMVs effectively diminished aminopeptidase activity but not Bestatin uptake by a H+/dipeptide cotransporter. Bestatin uptake by BBMVs was composed of two saturable components, and after papain treatment the high-affinity component disappeared while the low-affinity component was retained. These findings suggest that high- and low-affinity components represent Bestatin binding to aminopeptidase and the true uptake by the H+/dipeptide cotransporter, respectively.
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h coupled active transport of Bestatin via the dipeptide transport system in rabbit intestinal brush border membranes
Journal of Pharmacology and Experimental Therapeutics, 1992Co-Authors: Ken-ichi Inui, Mikihisa Takano, Toshiya Katsura, Yoshiko Tomita, Tomonobu Okano, Ryohei HoriAbstract:Bestatin [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-leucine], a dipeptide containing an unusual amino acid, has been used clinically as an anticancer agent in p.o. dosage form. We examined the transport characteristics of [3H]Bestatin by rabbit intestinal brush-border membrane vesicles. Bestatin uptake was stimulated by an inward H+ gradient (overshoot phenomenon) and by an interior-negative membrane potential. About half of the apparent Bestatin uptake at 1 mM by brush-border membrane vesicles was estimated as binding to the membranes. The affinity constant for the Bestatin transport was 0.52 mM. The uptake of Bestatin by brush-border membrane vesicles was inhibited by p.o. cephalosporins and dipeptides, but not by amino acids. In vesicles preloaded with either Bestatin, cephradine or glycylsarcosine, the uptake of [3H]Bestatin was stimulated markedly (countertransport effect). These results indicate that Bestatin is transported via the H+/dipeptide transport system in rabbit intestinal brush-border membranes.
Mikihisa Takano - One of the best experts on this subject based on the ideXlab platform.
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Bestatin transport in rabbit intestinal brush border membrane vesicles
Biochemical Pharmacology, 1994Co-Authors: Mikihisa Takano, Toshiya Katsura, Ken-ichi Inui, Yoshiko Tomita, Masato Yasuhara, Ryohei HoriAbstract:The effect of papain treatment on Bestatin uptake by rabbit intestinal brush-border membrane vesicles (BBMVs) was studied. Papain treatment of BBMVs effectively diminished aminopeptidase activity but not Bestatin uptake by a H+/dipeptide cotransporter. Bestatin uptake by BBMVs was composed of two saturable components, and after papain treatment the high-affinity component disappeared while the low-affinity component was retained. These findings suggest that high- and low-affinity components represent Bestatin binding to aminopeptidase and the true uptake by the H+/dipeptide cotransporter, respectively.
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h coupled active transport of Bestatin via the dipeptide transport system in rabbit intestinal brush border membranes
Journal of Pharmacology and Experimental Therapeutics, 1992Co-Authors: Ken-ichi Inui, Mikihisa Takano, Toshiya Katsura, Yoshiko Tomita, Tomonobu Okano, Ryohei HoriAbstract:Bestatin [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-leucine], a dipeptide containing an unusual amino acid, has been used clinically as an anticancer agent in p.o. dosage form. We examined the transport characteristics of [3H]Bestatin by rabbit intestinal brush-border membrane vesicles. Bestatin uptake was stimulated by an inward H+ gradient (overshoot phenomenon) and by an interior-negative membrane potential. About half of the apparent Bestatin uptake at 1 mM by brush-border membrane vesicles was estimated as binding to the membranes. The affinity constant for the Bestatin transport was 0.52 mM. The uptake of Bestatin by brush-border membrane vesicles was inhibited by p.o. cephalosporins and dipeptides, but not by amino acids. In vesicles preloaded with either Bestatin, cephradine or glycylsarcosine, the uptake of [3H]Bestatin was stimulated markedly (countertransport effect). These results indicate that Bestatin is transported via the H+/dipeptide transport system in rabbit intestinal brush-border membranes.
Toshiya Katsura - One of the best experts on this subject based on the ideXlab platform.
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Bestatin transport in rabbit intestinal brush border membrane vesicles
Biochemical Pharmacology, 1994Co-Authors: Mikihisa Takano, Toshiya Katsura, Ken-ichi Inui, Yoshiko Tomita, Masato Yasuhara, Ryohei HoriAbstract:The effect of papain treatment on Bestatin uptake by rabbit intestinal brush-border membrane vesicles (BBMVs) was studied. Papain treatment of BBMVs effectively diminished aminopeptidase activity but not Bestatin uptake by a H+/dipeptide cotransporter. Bestatin uptake by BBMVs was composed of two saturable components, and after papain treatment the high-affinity component disappeared while the low-affinity component was retained. These findings suggest that high- and low-affinity components represent Bestatin binding to aminopeptidase and the true uptake by the H+/dipeptide cotransporter, respectively.
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h coupled active transport of Bestatin via the dipeptide transport system in rabbit intestinal brush border membranes
Journal of Pharmacology and Experimental Therapeutics, 1992Co-Authors: Ken-ichi Inui, Mikihisa Takano, Toshiya Katsura, Yoshiko Tomita, Tomonobu Okano, Ryohei HoriAbstract:Bestatin [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-leucine], a dipeptide containing an unusual amino acid, has been used clinically as an anticancer agent in p.o. dosage form. We examined the transport characteristics of [3H]Bestatin by rabbit intestinal brush-border membrane vesicles. Bestatin uptake was stimulated by an inward H+ gradient (overshoot phenomenon) and by an interior-negative membrane potential. About half of the apparent Bestatin uptake at 1 mM by brush-border membrane vesicles was estimated as binding to the membranes. The affinity constant for the Bestatin transport was 0.52 mM. The uptake of Bestatin by brush-border membrane vesicles was inhibited by p.o. cephalosporins and dipeptides, but not by amino acids. In vesicles preloaded with either Bestatin, cephradine or glycylsarcosine, the uptake of [3H]Bestatin was stimulated markedly (countertransport effect). These results indicate that Bestatin is transported via the H+/dipeptide transport system in rabbit intestinal brush-border membranes.
Yoshiko Tomita - One of the best experts on this subject based on the ideXlab platform.
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Bestatin transport in rabbit intestinal brush border membrane vesicles
Biochemical Pharmacology, 1994Co-Authors: Mikihisa Takano, Toshiya Katsura, Ken-ichi Inui, Yoshiko Tomita, Masato Yasuhara, Ryohei HoriAbstract:The effect of papain treatment on Bestatin uptake by rabbit intestinal brush-border membrane vesicles (BBMVs) was studied. Papain treatment of BBMVs effectively diminished aminopeptidase activity but not Bestatin uptake by a H+/dipeptide cotransporter. Bestatin uptake by BBMVs was composed of two saturable components, and after papain treatment the high-affinity component disappeared while the low-affinity component was retained. These findings suggest that high- and low-affinity components represent Bestatin binding to aminopeptidase and the true uptake by the H+/dipeptide cotransporter, respectively.
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h coupled active transport of Bestatin via the dipeptide transport system in rabbit intestinal brush border membranes
Journal of Pharmacology and Experimental Therapeutics, 1992Co-Authors: Ken-ichi Inui, Mikihisa Takano, Toshiya Katsura, Yoshiko Tomita, Tomonobu Okano, Ryohei HoriAbstract:Bestatin [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-leucine], a dipeptide containing an unusual amino acid, has been used clinically as an anticancer agent in p.o. dosage form. We examined the transport characteristics of [3H]Bestatin by rabbit intestinal brush-border membrane vesicles. Bestatin uptake was stimulated by an inward H+ gradient (overshoot phenomenon) and by an interior-negative membrane potential. About half of the apparent Bestatin uptake at 1 mM by brush-border membrane vesicles was estimated as binding to the membranes. The affinity constant for the Bestatin transport was 0.52 mM. The uptake of Bestatin by brush-border membrane vesicles was inhibited by p.o. cephalosporins and dipeptides, but not by amino acids. In vesicles preloaded with either Bestatin, cephradine or glycylsarcosine, the uptake of [3H]Bestatin was stimulated markedly (countertransport effect). These results indicate that Bestatin is transported via the H+/dipeptide transport system in rabbit intestinal brush-border membranes.