Evidence map›Paper›PMID 26562785›Full record

ArticlePloS one2015

Imaging Sites of Inhibition of Proteolysis in Pathomimetic Human Breast Cancer Cultures by Light-Activated Ruthenium Compound.

Suelem D Ramalho, Rajgopal Sharma, Jessica K White, Neha Aggarwal, Anita Chalasani, Mansoureh Sameni, Kamiar Moin, Paulo C Vieira, Claudia Turro, Jeremy J Kodanko and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

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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

11 authors at 4 institutions in 2 countries.

Suelem D RamalhoDepartment of Chemistry, Federal University of São Carlos, São Carlos, São Paulo, Brazil.
Rajgopal SharmaDepartment of Chemistry, Wayne State University, Detroit, Michigan, United States of America.
Jessica K WhiteDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, United States of America.
Neha AggarwalDepartment of Physiology, School of Medicine, Wayne State University, Detroit, Michigan, United States of America.
Anita ChalasaniDepartment of Pharmacology, School of Medicine, Wayne State University, Detroit, Michigan, United States of America.
Mansoureh SameniDepartment of Pharmacology, School of Medicine, Wayne State University, Detroit, Michigan, United States of America.
Kamiar MoinDepartment of Pharmacology, School of Medicine, Wayne State University, Detroit, Michigan, United States of America.
Paulo C VieiraDepartment of Chemistry, Federal University of São Carlos, São Carlos, São Paulo, Brazil.
Claudia TurroDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, United States of America.
Jeremy J KodankoDepartment of Chemistry, Wayne State University, Detroit, Michigan, United States of America.
Bonnie F SloaneDepartment of Pharmacology, School of Medicine, Wayne State University, Detroit, Michigan, United States of America.
Michigan United · USThe Ohio State University · USUniversidade Federal de São Carlos · BRWayne State University · US

Funding

Tumor Biology and Microenvironment (Program 1)P30CA022453 · NCI · WAYNE STATE UNIVERSITY · PI PAUL M STEMMER · 1985 to 2026
$68.4M
Proteolytic Pathways in Progression of Pre-Malignant Breast DiseaseR01CA131990 · NCI · WAYNE STATE UNIVERSITY · PI MATTINGLY, RAYMOND R, SLOANE, BONNIE F · 2008 to 2013
$1.9M
Light Activation of Enzyme InhibitionR01EB016072 · NIBIB · WAYNE STATE UNIVERSITY · PI KODANKO, JEREMY · 2013 to 2016
$1.5M
NCI NIH HHS P30 CA022453NCI NIH HHS R01 CA131990NIBIB NIH HHS R01 EB016072NIBIB NIH HHS R01EB016072
6 · The paper itself

Abstract

The cysteine protease cathepsin B has been causally linked to progression and metastasis of breast cancers. We demonstrate inhibition by a dipeptidyl nitrile inhibitor (compound 1) of cathepsin B activity and also of pericellular degradation of dye-quenched collagen IV by living breast cancer cells. To image, localize and quantify collagen IV degradation in real-time we used 3D pathomimetic breast cancer models designed to mimic the in vivo microenvironment of breast cancers. We further report the synthesis and characterization of a caged version of compound 1, [Ru(bpy)2(1)2](BF4)2 (compound 2), which can be photoactivated with visible light. Upon light activation, compound 2, like compound 1, inhibited cathepsin B activity and pericellular collagen IV degradation by the 3D pathomimetic models of living breast cancer cells, without causing toxicity. We suggest that caged inhibitor 2 is a prototype for cathepsin B inhibitors that can control both the site and timing of inhibition in cancer.

Indexed as

BiocatalysisCathepsin BCell Culture TechniquesCell Line, TumorCell SurvivalCollagen Type IVCysteine Proteinase InhibitorsDiagnostic ImagingDose-Response Relationship, DrugHumansLightMicroscopy, ConfocalMolecular StructurePhotochemical ProcessesProteolysisRuthenium CompoundsCathepsin BCollagen Type IVCysteine Proteinase InhibitorsRuthenium Compounds

Identifiers

PMID26562785
PMCPMC4643019
OpenAlexW2412235604

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.