Evidence map›Paper›PMID 18417304›Full record

ArticleInternational journal of pharmaceutics2008

Activity of a sodium-dependent vitamin C transporter (SVCT) in MDCK-MDR1 cells and mechanism of ascorbate uptake.

Shuanghui Luo, Zhiying Wang, Viral Kansara, Dhananjay Pal, Ashim K Mitra

Open access · greenAbstract read
In one paragraph

Article in International journal of pharmaceutics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.4field-weighted citation impact, top 31% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 33 citations in OpenAlex.

  1. Role of vitamin C and SVCT2 in neurogenesis.Frontiers in neuroscience · 2023
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Shuanghui LuoDivision of Pharmaceutical Science, School of Pharmacy, University of Missouri-Kansas City, 5005 Rockhill Road, Kansas City, MO 64110-2499, USA.
Zhiying Wang
Viral Kansara
Dhananjay Pal
Ashim K Mitra
University of Missouri–Kansas City · US

Funding

Protease Inhibitor Analogues for Enhanced Transport Across Blood-Brain InterfacesR01AI071199 · NIAID · UNIVERSITY OF MISSOURI KANSAS CITY · PI MITRA, ASHIM K. · 2008 to 2011
$1.5M
Cellular Efflux and Metabolism of Protease InhibitorsR01GM064320 · NIGMS · UNIVERSITY OF MISSOURI KANSAS CITY · PI MITRA, ASHIM K · 2002 to 2004
$609k
NIAID NIH HHS R01 AI 071199NIGMS NIH HHS R01 GM064320
6 · The paper itself

Abstract

The objective of this research was to functionally characterize sodium-dependent vitamin C transporter (SVCT) in MDCK-MDR1 cells and to study the effect of substituted benzene derivatives on the intracellular accumulation of ascorbic acid (AA). Mechanism of AA uptake and transport was delineated. Uptake of [(14)C]ascorbic acid ([(14)C]AA) was studied in the absence and presence of excess unlabelled AA, anion transporter inhibitors, and a series of mono- and di-substituted benzenes. Transepithelial transport of [(14)C]AA across polarized cell membrane has been studied for the first time. Role of cellular protein kinase-mediated pathways on the regulation of AA uptake has been investigated. The cellular localizations of SVCTs were observed using confocal microscopy. Uptake of AA was found to be saturable with a K(m) of 83.2muM and V(max) of 94.2pmol/min/mg protein for SVCT1. The process was pH, sodium, temperature, and energy-dependent. It was under the regulation of cellular protein kinase C (PKC) and Ca(2+)/CaM mediated pathways. [(14)C]AA uptake was significantly inhibited in the presence of excess unlabelled AA and a series of electron-withdrawing group, i.e., halogen- and nitro-substituted benzene derivatives. AA appears to translocate across polarized cell membrane from apical to basal side (A-B) as well as basal to apical side (B-A) at a similar permeability. It appears that SVCT1 was mainly expressed on the apical side and SVCT2 may be located on both apical and basal sides. In conclusion, SVCT has been functionally characterized in MDCK-MDR1 cells. The interference of a series of electrophile-substituted benzenes on the AA uptake process may be explained by their structural similarity. SVCT may be targeted to facilitate the delivery of drugs with low bioavailability by conjugating with AA and its structural analogs. MDCK-MDR1 cell line may be utilized as an in vitro model to study the permeability of AA conjugated prodrugs.

Indexed as

AnimalsAscorbic AcidATP Binding Cassette Transporter, Subfamily BATP Binding Cassette Transporter, Subfamily B, Member 1Biological Transport, ActiveCell LineCell Membrane PermeabilityData Interpretation, StatisticalDogsEnergy MetabolismHumansHydrogen-Ion ConcentrationMicroscopy, ConfocalOrganic Anion Transporters, Sodium-DependentSignal TransductionSodiumABCB1 protein, humanAscorbic AcidATP Binding Cassette Transporter, Subfamily BATP Binding Cassette Transporter, Subfamily B, Member 1Organic Anion Transporters, Sodium-DependentSLC23A1 protein, humanSLC23A2 protein, humanSodiumSodium-Coupled Vitamin C TransportersSymporters

Identifiers

PMID18417304
PMCPMC2492580
OpenAlexW2074778919

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.