title: Transepithelial transport of oligopeptides in the human intestinal cell, Caco-2.
abstract: The transepithelial transport of oligopeptides (of more than 4 residues) was studied by using human intestinal Caco-2 cell monolyers. The susceptibility to the brush-border peptidases was observed to be one of the primary factors which decide the transport rate. The apical-to-basolateral transport mechanism was investigated by using bradykinin and GGYR which were resistant to cellular peptidases. The intracellular pathway, probably the adsorptive transcytosis, was suggested to be involved in the transport of bradykinin and its analogues, the transport rate being particularly dependent on the hydrophobic properties of the peptides. On the other hand, the tetrapeptide such as GGYR was suggested to be transported mainly via the paracellular pathway.
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Japan. ams316@hongo.ecc.u-tokyo.ac.jp
authors.forename: M
authors.initials: M
authors.lastname: Shimizu
authors.forename: M
authors.initials: M
authors.lastname: Tsunogai
authors.forename: S
authors.initials: S
authors.lastname: Arai
mesh_terms: D001692:Biological Transport / Q000187:drug effects; D001920:Bradykinin / Q000037:antagonists & inhibitors / Q000378:metabolism; D018938:Caco-2 Cells / Q000378:metabolism*; D004527:Egg Proteins / Q000378:metabolism; D004723:Endorphins / Q000378:metabolism; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism*; D009842:Oligopeptides / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D013329:Structure-Activity Relationship; D013997:Time Factors
chemical_list: D004527:Egg Proteins; D004723:Endorphins; D009842:Oligopeptides; D010446:Peptide Fragments; C096585:ovokinin; C078237:glycyl-glycyl-tyrosyl-arginine; C021968:beta-casomorphins; D001920:Bradykinin