| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10767740 | Biochemical and Biophysical Research Communications | 2005 | 5 Pages |
Abstract
Oligopeptides originating from ingested meal stimulate the secretion of various gastrointestinal hormones, but the mechanism is unknown. In this study, we show that transfection of oligopeptide transporter 1 (PEPT1) in STC-1 cells, a murine enteroendocrine cell line, evokes di-peptide-stimulated hormone secretion in a pH-dependent manner. Measurement of membrane potentials shows that PEPT1- transfected STC-1 cells are depolarized by di-peptide glycyl-glycine but not by glycine monomer. Glycyl-glycine stimulation induces a rise in the intracellular calcium concentration in PEPT1-transfected STC-1 cells. The secretion induced by glycyl-glycine in PEPT1-transfected STC-1 cells was blocked by nifedipine, a Ca2+ channel blocker, suggesting that the secretion is triggered by Ca2+ influx through L-type voltage-dependent Ca2+ channels. These data suggest that PEPT1 mediates oligopeptide-induced hormone secretion in enteroendocrine cells.
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Authors
Kimio Matsumura, Takashi Miki, Takahito Jhomori, Tohru Gonoi, Susumu Seino,