Evidence map›Paper›PMID 27571934›Full record

ArticleRedox report : communications in free radical research2017

Modification of cysteine 457 in plakoglobin modulates the proliferation and migration of colorectal cancer cells by altering binding to E-cadherin/catenins.

Suhee Kim, Sun Hee Ahn, Hee-Young Yang, Jin-Sil Lee, Hyang-Gi Choi, Young-Kyu Park, Tae-Hoon Lee

Open access · bronzeAbstract read
In one paragraph

Article in Redox report : communications in free radical research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

7 authors at 2 institutions in 1 country.

Suhee Kima Department of Oral Biochemistry , Dental Science Research Institute, Medical Research Center for Biomineralization Disorders, School of Dentistry, Chonnam National University , Gwangju , Republic of Korea.ORCID http://orcid.org/0000-0002-9315-0360
Sun Hee Ahna Department of Oral Biochemistry , Dental Science Research Institute, Medical Research Center for Biomineralization Disorders, School of Dentistry, Chonnam National University , Gwangju , Republic of Korea.ORCID http://orcid.org/0000-0002-0772-9588
Hee-Young Yanga Department of Oral Biochemistry , Dental Science Research Institute, Medical Research Center for Biomineralization Disorders, School of Dentistry, Chonnam National University , Gwangju , Republic of Korea.ORCID http://orcid.org/0000-0001-7654-8708
Jin-Sil Leea Department of Oral Biochemistry , Dental Science Research Institute, Medical Research Center for Biomineralization Disorders, School of Dentistry, Chonnam National University , Gwangju , Republic of Korea.ORCID http://orcid.org/0000-0002-9795-3128
Hyang-Gi Choia Department of Oral Biochemistry , Dental Science Research Institute, Medical Research Center for Biomineralization Disorders, School of Dentistry, Chonnam National University , Gwangju , Republic of Korea.ORCID http://orcid.org/0000-0001-7487-4585
Young-Kyu Parkc Department of Surgery , Chonnam National University Hwasun Hospital , Hwasun , Republic of Korea.ORCID http://orcid.org/0000-0002-3009-404X
Tae-Hoon Leea Department of Oral Biochemistry , Dental Science Research Institute, Medical Research Center for Biomineralization Disorders, School of Dentistry, Chonnam National University , Gwangju , Republic of Korea.ORCID http://orcid.org/0000-0003-0105-1750
Chonnam National University · KRChonnam National University Hwasun Hospital · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectivesIn tissue samples from patients with colorectal cancer (CRC), oxidation of C420 and C457 of plakoglobin (Pg) within tumor tissue was identified by proteomic analysis. The aim of this study was to identify the roles of Pg C420 and C457.

methodsHuman CRC tissues, CRC and breast cancer cells, and normal mouse colon were prepared to validate Pg oxidation. MC38 cells were co-transfected with E-cadherin plus wild type (WT) or mutant (C420S or C457S) Pg to evaluate protein interactions and cellular localization, proliferation, and migration.

resultsPg was more oxidized in stage III CRC tumor tissue than in non-tumor tissue. Similar oxidation of Pg was elicited by H DISCUSSION: Pg appears to be redox-sensitive in cancer, and the C457 modification may impair cell migration and proliferation by affecting its interaction with the E-cadherin/catenin axis. Our findings suggest that redox-sensitive cysteines of Pg may be the targets for CRC therapy.

Indexed as

AnimalsCadherinsCateninsCell MovementCell ProliferationColorectal NeoplasmsFemalegamma CateninHumansHydrogen PeroxideIn Vitro TechniquesMaleMiceProtein BindingCadherinsCateninsgamma CateninHydrogen PeroxideColorectal cancercysteineE-cadherinoxidationplakoglobin

Identifiers

PMID27571934
PMCPMC6837414
OpenAlexW2510710740

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.