Evidence map›Paper›PMID 26081835›Full record

ArticleMolecular & cellular proteomics : MCP2015

Proteomic Identification of Cysteine Cathepsin Substrates Shed from the Surface of Cancer Cells.

Barbara Sobotič, Matej Vizovišek, Robert Vidmar, Petra Van Damme, Vasilena Gocheva, Johanna A Joyce, Kris Gevaert, Vito Turk, Boris Turk, Marko Fonović

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 133 citations in OpenAlex.

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  12. Inhibitory prodrug mechanism for cysteine cathepsin-targeted self-controlled drug release.Journal of enzyme inhibition and medicinal chemistry · 2022
    Article
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  15. Helicobacter pylori and gastric cancer: a lysosomal protease perspective.Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association · 2022
    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

10 authors at 5 institutions in 3 countries.

Barbara SobotičFrom the ‡Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, Jamova cesta 39, SI-1000 Ljubljana, Slovenia; §International Postgraduate School Jozef Stefan, Jamova 39, SI-1000 Ljubljana, Slovenia;
Matej VizovišekFrom the ‡Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, Jamova cesta 39, SI-1000 Ljubljana, Slovenia; §International Postgraduate School Jozef Stefan, Jamova 39, SI-1000 Ljubljana, Slovenia;
Robert VidmarFrom the ‡Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, Jamova cesta 39, SI-1000 Ljubljana, Slovenia; §International Postgraduate School Jozef Stefan, Jamova 39, SI-1000 Ljubljana, Slovenia;
Petra Van Damme¶Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium; ‖Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium;
Vasilena Gocheva**Cancer Biology and Genetics Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065;
Johanna A Joyce**Cancer Biology and Genetics Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065;
Kris Gevaert¶Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium; ‖Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium;
Vito TurkFrom the ‡Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, Jamova cesta 39, SI-1000 Ljubljana, Slovenia; §International Postgraduate School Jozef Stefan, Jamova 39, SI-1000 Ljubljana, Slovenia; ‡‡Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins, Jamova cesta 39, SI-1000 Ljubljana, Slovenia;
Boris TurkFrom the ‡Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, Jamova cesta 39, SI-1000 Ljubljana, Slovenia; ‡‡Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins, Jamova cesta 39, SI-1000 Ljubljana, Slovenia; §§Center of Excellence NIN, Ljubljana, Slovenia; ¶¶Faculty of Chemistry and Chemical Technology, University of Ljubljana, Slovenia.
Marko FonovićFrom the ‡Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, Jamova cesta 39, SI-1000 Ljubljana, Slovenia; ‡‡Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins, Jamova cesta 39, SI-1000 Ljubljana, Slovenia; marko.fonovic@ijs.si.
Jožef Stefan Institute · SIGhent University · BEJožef Stefan International Postgraduate School · SIMemorial Sloan Kettering Cancer Center · USCentre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins · SI

Funding

Dissecting the Function of Cysteine Cathepsins in the Tumor MicroenvironmentR01CA125162 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI JOYCE, JOHANNA · 2007 to 2011
$1.8M
NCI NIH HHS NIH R01CA125162NCI NIH HHS R01 CA125162
6 · The paper itself

Abstract

Extracellular cysteine cathepsins are known to drive cancer progression, but besides degradation of extracellular matrix proteins little is known about their physiological substrates and thus the molecular mechanisms they deploy. One of the major mechanisms used by other extracellular proteases to facilitate cancer progression is proteolytic release of the extracellular domains of transmembrane proteins or ectodomain shedding. Here we show using a mass spectrometry-based approach that cathepsins L and S act as sheddases and cleave extracellular domains of CAM adhesion proteins and transmembrane receptors from the surface of cancer cells. In cathepsin S-deficient mouse pancreatic cancers, processing of these cathepsin substrates is highly reduced, pointing to an essential role of cathepsins in extracellular shedding. In addition to influencing cell migration and invasion, shedding of surface proteins by extracellular cathepsins impacts intracellular signaling as demonstrated for regulation of Ras GTPase activity, thereby providing a putative mechanistic link between extracellular cathepsin activity and cancer progression. The MS data is available via ProteomeXchange with identifier PXD002192.

Indexed as

AnimalsCarcinogenesisCathepsin BCathepsin LCathepsinsCell Line, TumorCell MembraneCell MovementHumansMacrophagesMembrane ProteinsMiceNeoplasm InvasivenessNeoplasmsProtein Processing, Post-TranslationalProteomicsCathepsin BCathepsin Lcathepsin SCathepsinsMembrane Proteinsras Proteins

Identifiers

PMID26081835
PMCPMC4528248
OpenAlexW2110063674

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.