Vitamin C transport and SVCT1 transporter expression in chick renal proximal tubule cells in culture

Johnston, Lauren; Laverty, Gary

doi:10.1016/j.cbpa.2006.11.025

Cited by 8 publications

(10 citation statements)

References 25 publications

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“…Experiments show that SLC23A1 mediates ascorbate uptake across the apical membrane into the cell (Kuo et al. ; Johnston and Laverty ; Luo et al. ).…”

Section: Introductionmentioning

confidence: 99%

“…Reabsorption of ascorbic acid across the polarized renal epithelial cell requires at least two events: uptake from the tubular lumen across the apical membrane into the tubule cell, followed by release across the basolateral membrane into the circulation. Experiments show that SLC23A1 mediates ascorbate uptake across the apical membrane into the cell Johnston and Laverty 2007;Luo et al 2008). What is unknown is the mechanism of ascorbic acid efflux from the renal epithelial cell, across the basolateral membrane.…”

Section: Introductionmentioning

confidence: 99%

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The human sodium-dependent ascorbic acid transporters SLC23A1 and SLC23A2 do not mediate ascorbic acid release in the proximal renal epithelial cell

et al. 2013

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Sodium-dependent ascorbic acid membrane transporters SLC23A1 and SLC23A2 mediate ascorbic acid (vitamin C) transport into cells. However, it is unknown how ascorbic acid undergoes cellular release, or efflux. We hypothesized that SLC23A1 and SLC23A2 could serve a dual role, mediating ascorbic acid cellular efflux as well as uptake. Renal reabsorption is required for maintaining systemic vitamin C concentrations. Because efflux from nephron cells is necessary for reabsorption, we studied whether SLC23A1 and SLC23A2 mediate efflux of ascorbic acid in the human renal nephron. We found high gene expression of SLC23A1 but no expression of SLC23A2 in the proximal convoluted and straight tubules of humans. These data rule out SLC23A2 as the ascorbic acid release protein in the renal proximal tubular epithelia cell. We utilized a novel dual transporter-based Xenopus laevis oocyte system to investigate the function of the SLC23A1 protein, and found that no ascorbate release was mediated by SLC23A1. These findings were confirmed in mammalian cells overexpressing SLC23A1. Taken together, the data for SLC23A1 show that it too does not have a role in cellular release of ascorbic acid across the basolateral membrane of the proximal tubular epithelial cell, and that SLC23A1 alone is responsible for ascorbic acid uptake across the apical membrane. These findings reiterate the physiological importance of proper functioning of SLC23A1 in maintaining vitamin C levels for health and disease prevention. The ascorbate efflux mechanism in the proximal tubule of the kidney remains to be characterized.

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“…Experiments show that SLC23A1 mediates ascorbate uptake across the apical membrane into the cell (Kuo et al. ; Johnston and Laverty ; Luo et al. ).…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The human sodium-dependent ascorbic acid transporters SLC23A1 and SLC23A2 do not mediate ascorbic acid release in the proximal renal epithelial cell

et al. 2013

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“…The hepatocytes were plated (5.0 × 10 5 cells/60‐mm collagen‐coated dish) with an incubation medium (Basal Medium Eagle supplemented with essential amino acids), containing 75 U/ml penicillin and 75 U/ml streptomycin, 1 µg/ml insulin, 10 −12 M dexamethasone, 5 µg/ml transferrin, 10 −8 M 3,5,3′‐triiodi‐ L ‐thyronine (T3), and 5% calf serum, and incubated for 4 h at 37°C in 5% CO 2 . In the previous studies, primary cultured chicken hepatocytes [Sasaki et al, 2000; Hou et al, 2001; Lee et al, 2006a, 2006b], cultured cells from the ovarian surface epithelium (OSE) layer of the hen [Giles et al, 2006], and chicken renal proximal cells [Johnston and Laverty, 2007] were cultured at 37°C. In our preliminary studies to determine the temperature of culture since chickens have higher body temperature than mammals, we compared difference between 37 and 40°C.…”

Section: Methodsmentioning

confidence: 99%

High glucose induced translocation of Aquaporin8 to chicken hepatocyte plasma membrane: Involvement of cAMP, PI3K/Akt, PKC, MAPKs, and microtubule

Lee

Heo

Lee

et al. 2007

J of Cellular Biochemistry

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Aquaporin8 (AQP8) is a transmembrane water channel that is found mainly in hepatocytes. The direct involvement of AQP8 in high glucose condition has not been established. Therefore, this study examined the effects of high glucose on AQP8 and its related signal pathways in primary cultured chicken hepatocytes. High glucose increased the movement of AQP8 from the intracellular membrane to plasma membrane in a 30 mM glucose concentration and in a time- (> or =10 min) dependent manner. On the other hand, 30 mM mannitol did not affect the translocation of AQP8, which suggested the absence of osmotic effect. Thirty millimolar glucose increased intracellular cyclic adenosine 3, 5-monophosphate (cAMP) level. Moreover, high glucose level induced Akt phosphorylation, protein kinase C (PKC) activation, p44/42 mitogen-activated protein kinases (MAPKs), p38 MAPK, and c-jun NH2-terminal kinase (JNK) phosphorylation. On the other hand, inhibition of each pathway by SQ 22536 (adenylate cyclase inhibitor), LY 294002 (PI3-K phosphatidylinositol 3-kinase inhibitor), Akt inhibitor, staurosporine (PKC inhibitor), PD 98059 (MEK inhibitor), SB 203580 (p38 MAPK inhibitor), or SP 600125 (JNK inhibitor) blocked 30 mM glucose-induced AQP8 translocation, respectively. In addition, inhibition of microtubule movement with nocodazole blocked high glucose-induced AQP8 translocation. High glucose level also increased the level of kinesin light chain and dynein protein expression. In conclusion, high glucose level stimulates AQP8 via cAMP, PI3-K/Akt, PKC, and MAPKs pathways in primary cultured chicken hepatocytes.

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“…Πολλές μελέτες έχουν δείξει ότι η κουερσετίνη, μια φλαβονόλη με αντιοξειδωτικές ιδιότητες, είναι σημαντικός αναστολέας της πρόσληψης του ασκορβικού και του δεϋδροασκορβικού οξέος από τα κύτταρα [156,193,200,201]. Αυτή η αναστολή είναι αποτέλεσμα των δομικών χαρακτηριστικών της κουερσετίνης και όχι λόγω των αντιοξειδωτικών ιδιοτήτων της και επιπλέον, αυτή η αναστολή δεν ερμηνεύεται από την οξείδωση του ασκορβικού οξέος, γιατί η κουερσετίνη δε μειώνει τη σταθερότητα του ασκορβικού οξέος.…”

Section: διευκολυνόμενη διάχυση για το δεϋδροασκορβικό οξύ (Dha)unclassified

“…Οι SVCT 1 και SVCT 2 μοιάζουν λειτουργικά, έτσι δεν είναι δυνατό να αναγνωριστεί αν η πρόσληψη του ασκορβικού οξέος από τα μεσοθηλιακά κύτταρα γίνεται με τη μεσολάβηση και των δύο μεταφορέων ή του ενός από αυτούς [192,195,200]. Οι μεταφορείς αυτοί έχουν δομικές διαφορές σε γενετικό επίπεδο, έτσι για την ταυτοποίησή τους είναι απαραίτητη η εφαρμογή της RT-PCR [195].…”

Section: διευκολυνόμενη διάχυση για το δεϋδροασκορβικό οξύ (Dha)unclassified

Η Επίδραση Αντιοξειδωτικών Παραγόντων Στη Διαπερατότητα Του Υπεζωκότα Προβάτου

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Vitamin C transport and SVCT1 transporter expression in chick renal proximal tubule cells in culture

Cited by 8 publications

References 25 publications

The human sodium-dependent ascorbic acid transporters SLC23A1 and SLC23A2 do not mediate ascorbic acid release in the proximal renal epithelial cell

The human sodium-dependent ascorbic acid transporters SLC23A1 and SLC23A2 do not mediate ascorbic acid release in the proximal renal epithelial cell

High glucose induced translocation of Aquaporin8 to chicken hepatocyte plasma membrane: Involvement of cAMP, PI3K/Akt, PKC, MAPKs, and microtubule

Η Επίδραση Αντιοξειδωτικών Παραγόντων Στη Διαπερατότητα Του Υπεζωκότα Προβάτου

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