Immunolocalization and pharmacological relevance of oligopeptide transporter PepT1 in intestinal absorption of β‐lactam antibiotics

FEBS Letters

Hayashi, Kiyomi¹  Sumikawa, Hiromi¹  Iseki, Shoichi²  Sai, Yoshimichi¹  Nakanishi, Takeo¹  Tamai, Ikumi¹  Tsuji, Akira¹  Numata, Masayuki²  Amano, Osamu² 

[1] Department of Pharmaceutics, Faculty of Pharmaceutical Sciences, Kanazawa University, 13-1 Takara-machi, Kanazawa, Ishikawa 920, Japan;Department of Anatomy, School of Medicine, Kanazawa University, 13-1 Takara-machi, Kanazawa, Ishikawa 920, Japan

关键词: Peptide transport;    β-Lactam antibiotic;    Intracellular localization;    Basolateral membrane;    Xenopus oocyte;    Hybrid depletion;    BBM;    brush-border membrane;    BLM;    basolateral membrane;   

DOI  :  10.1016/0014-5793(96)00778-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A polyclonal antibody (anti-PepT1/C) was raised against the rabbit intestinal H⁺-coupled oligopeptide transporter, PepT1. Anti-PepT1/C detected 70–80-kDa protein in crude membranes obtained from rabbit duodenum, jejunum and ileum. PepT1 was localized in the brush-border of the absorptive epithelial cells by subcellular fractionation of membranes on a sucrose density gradient and by immunohistochemistry using light and electron microscopy. Transport activity for cephalosporins and dipeptide expressed in Xenopus laevis oocytes injected with total mRNA obtained from rabbit small intestine was eliminated completely by prehybridization of the mRNA with antisense oligonucleotide against the 5′-coding region of rabbit PepT1 cDNA.

【 授权许可】

Unknown