Evidence map›Paper›PMID 33580460›Full record

ArticleMolecular biology reports2021

Role of p53 in transcriptional repression of SVCT2.

Eun Ho Kim, Dong-In Koh, Yea Seong Ryu, Sang-Soo Park, Seung-Woo Hong, Jai-Hee Moon, Jae-Sik Shin, Mi Jin Kim, Do Yeon Kim, Jun Ki Hong and 7 more

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular biology reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 34% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. TCOF1 promotes the colorectal cancer progression by stabilizing β-catenin.Medical oncology (Northwood, London, England) · 2023
    Article
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

17 authors at 3 institutions in 1 country.

Eun Ho Kim *Asan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Dong-In Koh *Asan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Yea Seong RyuAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Sang-Soo ParkAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Seung-Woo HongAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Jai-Hee MoonAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Jae-Sik ShinAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Mi Jin KimAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Do Yeon KimAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Jun Ki HongAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Hong-Rae JeongAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Hyeseon YunAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Joo-Yeon ShinAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Joseph KimAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Yoon Sun ParkAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Dong Min KimAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea.
Dong-Hoon JinAsan Institute for Life Science, Asan Medical Center, Seoul, Republic of Korea. inno183@amc.seoul.kr.
Asan Medical Center · KRUniversity of Ulsan · KRUlsan College · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SVCT2, Sodium-dependent Vitamin C Transporter 2, uniquely transports ascorbic acid (also known as vitamin C and ascorbate) into all types of cells. Vitamin C is an essential nutrient that must be obtained through the diet and plasma levels are tightly regulated by transporter activity. Vitamin C plays an important role in antioxidant defenses and is a cofactor for many enzymes that enable hormone synthesis, oxygen sensing, collagen synthesis and epigenetic pathways. Although SVCT2 has various functions, regulation of its expression/activity remains poorly understood. We found a p53-binding site, within the SVCT2 promoter, using a transcription factor binding-site prediction tool. In this study, we show that p53 can directly repress SVCT2 transcription by binding a proximal- (~-185 to -171 bp) and a distal- (~-1800 to -1787 bp) p53-responsive element (PRE), Chromatin immunoprecipitation assays showed that PRE-bound p53 interacts with the corepressor-histone deacetylase 3 (HDAC3), resulting in deacetylation of histones Ac-H4, at the proximal promoter, resulting in transcriptional silencing of SVCT2. Overall, our data suggests that p53 is a potent transcriptional repressor of SVCT2, a critical transporter of diet-derived ascorbic acid, across the plasma membranes of numerous essential tissue cell types.

Indexed as

AnimalsAntioxidantsAscorbic AcidBinding SitesChromatinFibroblastsHep G2 CellsHistone Deacetylase 3Histone DeacetylasesHumansMiceProtein BindingRepressor ProteinsSodium-Coupled Vitamin C TransportersTumor Suppressor Protein p53AntioxidantsAscorbic AcidChromatinHistone Deacetylase 3Histone DeacetylasesRepressor ProteinsSLC23A2 protein, humanSodium-Coupled Vitamin C TransportersTP53 protein, humanTumor Suppressor Protein p53BiomarkerCorepressorHDAC3p53p53R175HSVCT2Vitamin C

Identifiers

PMID33580460
OpenAlexW3128637702

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.