Analysis of Cationic Amino Acid Transport Activity in Canine Lens Epithelial Cells

Ochiai, Hideharu; Moriyama, Jun; Kanemaki, Nobuyuki; Sato, Reiichiro; Onda, Ken

doi:10.1538/expanim.62.311

Cited by 3 publications

(3 citation statements)

References 26 publications

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“…Regarding ocular tissues, CAT-1 and CAT-2 have been localized in healthy lacrimal glands, conjunctiva, cornea, and nasolacrimal ducts [ 45 ]. Physiologically, CAT-1 has been found to be responsible for molecular or nutrient transport in ocular surfaces [ 37 ], across lens epithelial cells [ 46 ], and the inner blood-retinal barrier [ 31 , 47 ]. Owing to the transport ability of CATs, it has also been suggested that amino acid prodrugs utilizing CAT transport may improve the solubility of poorly aqueous soluble compounds [ 38 , 48 ].…”

Section: Discussionmentioning

confidence: 99%

Expression Profile of Cationic Amino Acid Transporters in Rats with Endotoxin-Induced Uveitis

Hsu

Chang

Yang

et al. 2016

Mediators of Inflammation

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Purpose. The transcellular arginine transportation via cationic amino acid transporter (CAT) is the rate-limiting step in nitric oxide (NO) synthesis, which is crucial in intraocular inflammation. In this study, CAT isoforms and inducible nitric oxide synthase (iNOS) expression was investigated in endotoxin-induced uveitis (EIU). Methods. EIU was induced in Lewis rats by lipopolysaccharide (LPS) injection. In the treatment group, the rats were injected intraperitoneally with the proteasome inhibitor bortezomib before EIU induction. After 24 hours, leukocyte quantification, NO measurement of the aqueous humor, and histopathological examination were evaluated. The expression of CAT isoforms and iNOS was determined by reverse transcription-polymerase chain reaction, western blotting, and immunofluorescence staining. Nuclear factor-kappa B (NF-κB) binding activity was evaluated by electrophoretic mobility shift assay. The mouse macrophage cell line RAW 264.7 was used to validate the in vivo findings. Results. LPS significantly stimulated iNOS, CAT-2A, and CAT-2B mRNA and protein expression but did not affect CAT-1 in EIU rats and RAW 264.7 cells. Bortezomib attenuated inflammation and inhibited iNOS, CAT-2A, and CAT-2B expression through NF-κB inhibition. Conclusions. CAT-2 and iNOS, but not CAT-1, are specifically involved in EIU. NF-κB is essential in the induction of CAT-2 and iNOS in EIU.

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Section: Discussionmentioning

confidence: 99%

Expression Profile of Cationic Amino Acid Transporters in Rats with Endotoxin-Induced Uveitis

Hsu

Chang

Yang

et al. 2016

Mediators of Inflammation

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“…Intestinal epithelial cell (IEC) lines used in nutrient absorption experiments mostly were derived from colonic adenocarcinoma (e.g., Caco-2) [6,9]. However, these cell lines may not be suitable models for nutrient transport analysis, as they had undergone changes and selection to facilitate long-term growth in vitro.…”

Section: Introductionmentioning

confidence: 99%

Uptake of Manganese from the Manganese-Lysine Complex in Primary Chicken Intestinal Epithelial Cells

Bai

Zhang

Ding

et al. 2019

Animals

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Organic manganese (Mn) sources can replace inorganic Mn as dietary Mn supplements in poultry. To compare the uptake of Mn from the Mn-lysine complex (MnLys) and MnSO4, we first established the primary chicken intestinal epithelial cells (IECs) model and used it to determine Mn uptake. The MnLys increased the uptake of Mn compared to MnSO4. The uptake of Mn decreased in the IECs with Fe addition in the medium regardless of the Mn sources. The MnLys decreased the Mn2+ efflux transporter ferroportin 1 (FPN1) mRNA level but did not influence the Mn2+ influx transporter divalent metal transporter 1 (DMT1) mRNA expression when compared to MnSO4. The results above indicated that the increase of Mn accumulation for MnLys at least partly was due to the decrease of Mn efflux by reduced FPN1 expression. The addition of N-ethylmaleimide, an L-lysine transport system y+ inhibitor, decreased the uptake of Mn from MnLys but did not affect the uptake of Mn from MnSO4. The cycloheximide, as an L-lysine transport system b0,+ activator, increased the uptake of Mn from MnLys, whereas they did not influence the uptake of Mn from MnSO4. The MnLys increased the system y+ members cationic amino acid transporter (CAT) 1 and CAT2, and system b0,+ components rBAT and b0,+AT mRNA expression when compared to MnSO4. These results suggested that the uptake of MnLys complex might be transported by CAT1/2 and system b0,+, which was different from the ionized Mn2+ uptake pathway. In conclusion, the uptake of Mn from MnLys complex not only might be uptake through the ionized Mn2+ pathway, but also appeared to be transported through the CAT1/2 and system b0,+ in primary chicken IECs.

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“…The epithelial cell lines used in nutrient absorption experiments were derived from colonic adenocarcinoma (e.g. Caco‐2) and the intestine of suckling animals (Thomas and Oates, ; Li et al., ; Ochiai et al., ). These normal or transformed cell lines may not be suitable models for the intact epithelium, as they had undergone changes and selection to facilitate long‐term growth in vitro .…”

Section: Introductionmentioning

confidence: 99%

Uptake of manganese from manganese–lysine complex in the primary rat intestinal epithelial cells

Zhang

Gilbert

Zhang

et al. 2015

Animal Physiology Nutrition

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This study was conducted to compare the differences of the uptake of Mn from Mn-lysine complex (MnLys) and MnSO and to determine the potential mechanisms of the uptake of Mn from MnLys. We first established the primary rat intestinal epithelial cell culture model and used it to determine the uptake of Mn from different Mn sources. The MnLys increased (p < 0.001) Mn uptake when compared to MnSO . The uptake of Mn decreased (p < 0.05) with added Fe concentration increasing in the medium regardless of Mn source. The MnLys decreased (p < 0.01) Mn efflux transporter ferroportin 1 (FPN1) mRNA level, but did not influence (p > 0.06) Mn influx transporter DMT1 mRNA expression when compared to MnSO . The results above indicated that the increase of Mn accumulation for MnLys at least partly was due to the decrease of Mn efflux by reduced FPN1 expression. The N-ethylmaleimide, as an l-lysine transport system y inhibitor, decreased (p < 0.001) the uptake of Mn from MnLys, but did not affect (p > 0.10) the uptake of Mn from MnSO . The cycloheximide, as an l-lysine transport system b activator, increased (p < 0.001) the uptake of Mn from MnLys, whereas also did not influence the uptake of Mn from MnSO . The MnLys increased (p < 0.01) the system y member cationic amino acid transporter (CAT) 1, and system b components rBAT and b AT mRNA expression when compared to MnSO . These results suggested that the uptake of Mn from MnLys complex might be transported by CAT1 and system b , which was different from ionized Mn uptake pathway. In conclusion, the uptake of MnLys complex not only might be absorbed as Mn , but also appeared to be transported through CAT1 and system b in the primary rat intestinal epithelial cells.

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Analysis of Cationic Amino Acid Transport Activity in Canine Lens Epithelial Cells

Cited by 3 publications

References 26 publications

Expression Profile of Cationic Amino Acid Transporters in Rats with Endotoxin-Induced Uveitis

Expression Profile of Cationic Amino Acid Transporters in Rats with Endotoxin-Induced Uveitis

Uptake of Manganese from the Manganese-Lysine Complex in Primary Chicken Intestinal Epithelial Cells

Uptake of manganese from manganese–lysine complex in the primary rat intestinal epithelial cells

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