Interaction of Peptide Transporter 1 With d-Glucose and l-Glutamic Acid; Possible Involvement of Taste Receptors

Arakawa, Hiroshi; Ohmachi, Taichi; Ichiba, Kiko; Kamioka, Hiroki; Tomono, Takumi; Kanagawa, Masahiko; Idota, Yoko; Hatano, Yasuko; Yano, Kentarô; Morimoto, Kaori; Ogihara, Takuo

doi:10.1016/j.xphs.2015.11.024

Cited by 6 publications

(1 citation statement)

References 21 publications

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“…Because HCF is characterized by high porosity, the synergetic effect of co-culture of different types of cells is enhanced compared with conventional TEM inserts. Although only a few studies on cell-cell communication in pharmacokinetic studies have been reported, [30][31][32][33] cell-cell communication is potentially important for precise analysis of cell function. For example, the functions of cerebral microvessels, which constitute the blood-brain barrier, are regulated by astrocytes, which interact with brain capillary endothelial cells.…”

Section: Discussionmentioning

confidence: 99%

Drug Transcellular Transport Assay Using a High Porosity Honeycomb Film

Nakazono

Arakawa

Nishino

et al. 2021

Biological & Pharmaceutical Bulletin

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In vitro transport studies across cells grown on culture inserts are widely used for evaluating pharmacokinetic characteristics such as intestinal membrane permeability. However, measurements of the apparent permeability coefficient of highly lipophilic compounds are often limited by transport across the membrane filters, not by transport across the cultured cells. To overcome this concern, we have investigated the utility of a high-porosity membrane honeycomb film (HCF) for transcellular transport studies. Using the HCF inserts, the apparent permeability coefficient (P app ) of the drugs tested in LLC-PK1 and Caco-2 cells tended to increase with an increase in lipophilicity, reaching a maximum P app value at Log D higher than 2. In contrast, using the commercially available Track-Etched membrane (TEM) inserts, a maximum value was observed at Log D higher than 1. The basolateral to apical transport permeability P app(BL→AP) of rhodamine 123 across LLC-PK1 cells that express P-glycoprotein (P-gp) cultured on HCF inserts and TEM inserts was 2.33 and 2.39 times higher than the reverse directional P app(AP→BL) permeability, respectively. The efflux ratio (P app(B-A) / P app(A-B) ) of rhodamine 123 in LLC-PK1 expressing P-gp cells using HCF inserts was comparable to that obtained using TEM inserts, whereas the transported amount in both directions was significantly higher when using the HCF inserts. Accordingly, due to the higher permeability and high porosity of HCF membranes, it is expected that transcellular transport of high lipophilic as well as hydrophilic compounds and substrate recognition of transporters can be evaluated more accurately by using HCF inserts.

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Section: Discussionmentioning

confidence: 99%

Drug Transcellular Transport Assay Using a High Porosity Honeycomb Film

Nakazono

Arakawa

Nishino

et al. 2021

Biological & Pharmaceutical Bulletin

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Proton Coupled Oligopeptide Transporter 1 (PepT1) Function, Regulation, and Influence on the Intestinal Homeostasis

Spanier

Rohm

2018

Comprehensive Physiology

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As the organ with one of the largest surface areas facing the environment and responsible for nutrient uptake, the small intestine expresses numerous transport proteins in its brush-border membrane for efficient absorption and supply of dietary macro- and micronutrients. The understanding of regulation and functional interplay of these nutrient transporters is of emerging interest in nutrition and medical physiology research in respect to development of diabetes, obesity, and inflammatory bowel disease worldwide. The peptide transporter 1 (PepT1, SLC15A1) is abundantly expressed particularly in the intestinal tract and provides highly effective transport of amino acids in the form of di- and tripeptides and features a substantial acceptance for structurally related compounds and drugs. These characteristics bring PepT1 into focus for nutritional and medical/pharmaceutical approaches, as it is the essential hub responsible for oral bioavailability of dietary protein/peptide supplements and peptide-like drugs in eukaryotic organisms. Detailed analysis of molecular processes regulating PepT1 expression and function achieved in the last two decades has helped to define and use adjusting tools and to better integrate the transporter's role in cell and organ physiology. In this article, we provide an overview of the current knowledge on PepT1 function in health and disease, and on regulatory factors modulating its gene and protein expression as well as transport activity. © 2018 American Physiological Society. Compr Physiol 8:843-869, 2018.

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Effects of Ghrelin on intestinal cell proliferation, the expression of protein absorption and metabolism factors in juvenile grass carp (Ctenopharyngodon idella)

Interaction of Peptide Transporter 1 With d-Glucose and l-Glutamic Acid; Possible Involvement of Taste Receptors

Cited by 6 publications

References 21 publications

Drug Transcellular Transport Assay Using a High Porosity Honeycomb Film

Drug Transcellular Transport Assay Using a High Porosity Honeycomb Film

Proton Coupled Oligopeptide Transporter 1 (PepT1) Function, Regulation, and Influence on the Intestinal Homeostasis

Effects of Ghrelin on intestinal cell proliferation, the expression of protein absorption and metabolism factors in juvenile grass carp (Ctenopharyngodon idella)

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