Evidence map›Paper›PMID 22334655›Full record

ArticleThe Journal of biological chemistry2012

β-Actin-binding complementarity-determining region 2 of variable heavy chain from monoclonal antibody C7 induces apoptosis in several human tumor cells and is protective against metastatic melanoma.

Denise C Arruda, Luana C P Santos, Filipe M Melo, Felipe V Pereira, Carlos R Figueiredo, Alisson L Matsuo, Renato A Mortara, Maria A Juliano, Elaine G Rodrigues, Andrey S Dobroff and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. From antimicrobial to anticancer: the pioneering works of Prof. Luiz Rodolpho Travassos on bioactive peptides.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Review
  3. A limitless Brazilian scientist: Professor Travassos and his contribution to cancer biology.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 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

12 authors at 3 institutions in 3 countries.

Denise C ArrudaExperimental Oncology Unit (UNONEX), Universidade Federal de São Paulo (UNIFESP), São Paulo SP 04023-062, Brazil.
Luana C P Santos
Filipe M Melo
Felipe V Pereira
Carlos R Figueiredo
Alisson L Matsuo
Renato A Mortara
Maria A Juliano
Elaine G Rodrigues
Andrey S Dobroff
Luciano Polonelli
Luiz R Travassos
Universidade Federal de São Paulo · BRThe University of Texas MD Anderson Cancer Center · USUniversity of Parma · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Complementarity-determining regions (CDRs) from monoclonal antibodies tested as synthetic peptides display anti-infective and antitumor activities, independent of the specificity of the native antibody. Previously, we have shown that the synthetic peptide C7H2, based on the heavy chain CDR 2 from monoclonal antibody C7, a mAb directed to a mannoprotein of Candida albicans, significantly reduced B16F10 melanoma growth and lung colony formation by triggering tumor apoptosis. The mechanism, however, by which C7H2 induced apoptosis in tumor cells remained unknown. Here, we demonstrate that C7H2 interacts with components of the tumor cells cytoskeleton, being rapidly internalized after binding to the tumor cell surface. Mass spectrometry analysis and in vitro validation revealed that β-actin is the receptor of C7H2 in the tumor cells. C7H2 induces β-actin polymerization and F-actin stabilization, linked with abundant generation of superoxide anions and apoptosis. Major phenotypes following peptide binding were chromatin condensation, DNA fragmentation, annexin V binding, lamin disruption, caspase 8 and 3 activation, and organelle alterations. Finally, we evaluated the cytotoxic efficacy of C7H2 in a panel of human tumor cell lines. All tumor cell lines studied were equally susceptible to C7H2 in vitro. The C7H2 amide without further derivatization significantly reduced lung metastasis of mice endovenously challenged with B16F10-Nex2 melanoma cells. No significant cytotoxicity was observed toward nontumorigenic cell lines on short incubation in vitro or in naïve mice injected with a high dose of the peptide. We believe that C7H2 is a promising peptide to be developed as an anticancer drug.

Indexed as

ActinsAnimalsAntibodies, Monoclonal, Murine-DerivedAntibodies, NeoplasmAntineoplastic AgentsApoptosisCandida albicansCaspase 3Caspase 8Cell Line, TumorDNA FragmentationDNA, NeoplasmFungal ProteinsHumansImmunoglobulin Heavy ChainsImmunoglobulin Variable RegionActinsAntibodies, Monoclonal, Murine-DerivedAntibodies, NeoplasmAntineoplastic AgentsCASP3 protein, humanCasp3 protein, mouseCASP8 protein, humanCasp8 protein, mouseCaspase 3Caspase 8DNA, NeoplasmFungal ProteinsImmunoglobulin Heavy ChainsImmunoglobulin Variable RegionmannoproteinsMembrane GlycoproteinsNeoplasm Proteins

Identifiers

PMID22334655
PMCPMC3340220
OpenAlexW2012706912

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.