Evidence map›Paper›PMID 24808173›Full record

ArticleThe Journal of biological chemistry2014

Tenascin-C-derived peptide TNIIIA2 highly enhances cell survival and platelet-derived growth factor (PDGF)-dependent cell proliferation through potentiated and sustained activation of integrin α5β1.

Rika Tanaka, Yutaka Seki, Yohei Saito, Sadahiro Kamiya, Motomichi Fujita, Hiroaki Okutsu, Takuya Iyoda, Tatsuya Takai, Toshiyuki Owaki, Hirofumi Yajima and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

27 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  7. Advances on the roles of tenascin-C in cancer.Journal of cell science · 2022
    Article
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  18. Combining peptide TNIIIA2 with all-American journal of cancer research · 2019
    Article
  19. 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

15 authors at 3 institutions in 1 country.

Rika TanakaFrom the Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Chiba 278-8510, Japan.
Yutaka SekiFrom the Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Chiba 278-8510, Japan.
Yohei SaitoFrom the Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Chiba 278-8510, Japan.
Sadahiro KamiyaDepartment of Drug Informatics, Faculty of Pharmaceutical Sciences, Josai International University, 1 Gumyo, Togane-shi, Chiba 283-8555, Japan.
Motomichi FujitaFrom the Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Chiba 278-8510, Japan.
Hiroaki OkutsuFrom the Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Chiba 278-8510, Japan.
Takuya IyodaFrom the Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Chiba 278-8510, Japan.
Tatsuya TakaiFrom the Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Chiba 278-8510, Japan.
Toshiyuki OwakiFrom the Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Chiba 278-8510, Japan.
Hirofumi YajimaDepartment of Applied Chemistry, Faculty of Science, Tokyo University of Science, Tokyo 162-8601, Japan.
Junichi TairaDepartment of Chemistry, Kurume University School of Medicine, Kurume 830-0011, Japan.
Ryo HayashiFaculty of Science and Engineering, Saga University, Saga 849-0922, Japan, and.
Hiroaki KodamaFaculty of Science and Engineering, Saga University, Saga 849-0922, Japan, and.
Takuya MatsunagaFrom the Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Chiba 278-8510, Japan.
Fumio FukaiFrom the Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Chiba 278-8510, Japan, fukai@rs.noda.tus.ac.jp.
Josai International University · JPKurume University · JPTokyo University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tenascin-C is an adhesion modulatory matrix protein that is highly expressed in tumors; however, its biochemical activity involved in tumorigenesis is not fully understood. On the other hand, increasing evidence indicates the importance of integrin α5β1 in cancer development. We previously demonstrated that tenascin-C harbors a functional site that can be released as a proadhesive peptide such as TNIIIA2. Peptide TNIIIA2 is capable of inducing activation of β1-integrins including α5β1 via syndecan-4. In this study the proadhesive effect of TNIIIA2 was characterized by potentiated and sustained activation of integrin α5β1. Based on this effect, TNIIIA2 rendered nontransformed fibroblasts (NIH3T3) resistant to serum deprivation-elicited anoikis through activation of the Akt/Bcl-2 pathway. Moreover, TNIIIA2 hyperstimulated PDGF-dependent proliferation of NIH3T3 by activating integrin α5β1. Tenascin-C, a parental protein of TNIIIA2, also stimulated PDGF-dependent proliferation, which was blocked by a matrix metalloproteinase-2/9 inhibitor and an anti-TNIIIA2 function-blocking antibody, suggesting proteolytic exposure of the proadhesive effect of TNIIIA2. Mechanistic analyses revealed that TNIIIA2 induced a lateral association of PDGF receptor β with the molecular complex of activated integrin α5β1 and syndecan-4 in the membrane microdomains enriched with cholesterol/caveolin-1, resulting in prolonged activation of PDGF receptor β and the subsequent Ras/mitogen-activated protein kinase pathway in a PDGF-dependent manner. Of note, TNIIIA2 induced continuous proliferation in NIH3T3 in an integrin α5β1-dependent manner even after they formed a confluent monolayer. Thus, it was proposed that tenascin-C might be involved in deregulated cell growth through potentiated and sustained activation of integrin α5β1 after exposure of the proadhesive effect of TNIIIA2.

Indexed as

AnimalsCell ProliferationCell SurvivalHumansK562 CellsMembrane MicrodomainsMiceNIH 3T3 CellsPeptidesPlatelet-Derived Growth FactorReceptor, Platelet-Derived Growth Factor betaReceptors, VitronectinSyndecan-4Tenascinintegrin alphavbeta1PeptidesPlatelet-Derived Growth FactorReceptor, Platelet-Derived Growth Factor betaReceptors, VitronectinSDC4 protein, humanSdc4 protein, mouseSyndecan-4TenascinCell AdhesionCell ProliferationExtracellular MatrixIntegrinPDGFTenascin

Identifiers

PMID24808173
PMCPMC4067204
OpenAlexW2045039781

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.