Evidence map›Paper›PMID 20145119›Full record

ArticleCancer research2010

Tumor detection by imaging proteolytic activity.

Molly R Darragh, Eric L Schneider, Jianlong Lou, Paul J Phojanakong, Christopher J Farady, James D Marks, Byron C Hann, Charles S Craik

Open access · bronzeAbstract readEvaluation Study
In one paragraph

Article in Cancer research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Mapping Enzyme Activity on Tissue by Functional Mass Spectrometry Imaging.Angewandte Chemie (International ed. in English) · 2020
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  15. Imaging a functional tumorigenic biomarker in the transformed epithelium.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Article
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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

8 authors at 2 institutions in 1 country.

Molly R DarraghGraduate Group in Biophysics, Department of Pharmaceutical Chemistry, Helen Diller Family Comprehensive Cancer Center, University of California, San Francisco, San Francisco, California 94158, USA.
Eric L Schneider
Jianlong Lou
Paul J Phojanakong
Christopher J Farady
James D Marks
Byron C Hann
Charles S Craik
UCSF Helen Diller Family Comprehensive Cancer Center · USUniversity of California, San Francisco · US

Funding

PROTEASES--TUMOR BIOLOGYP01CA072006 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WERB, ZENA · 1997 to 2007
$10.8M
Molecular and Cellular Mechanisms in CancerT32CA108462 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GOGA, ANDREI · 2004 to 2024
$10.4M
A Technological Platform for the Identification of Serine Proteases in CancerR01CA128765 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2009 to 2011
$1.1M
NCI NIH HHS CA108462-04NCI NIH HHS CA128765NCI NIH HHS CA72006NCI NIH HHS P01 CA072006NCI NIH HHS R01 CA128765NCI NIH HHS T32 CA108462
6 · The paper itself

Abstract

The cell surface protease membrane-type serine protease-1 (MT-SP1), also known as matriptase, is often upregulated in epithelial cancers. We hypothesized that dysregulation of MT-SP1 with regard to its cognate inhibitor hepatocyte growth factor activator inhibitor-1 (HAI-1), a situation that increases proteolytic activity, might be exploited for imaging purposes to differentiate malignant from normal tissue. In this study, we show that MT-SP1 is active on cancer cells and that its activity may be targeted in vivo for tumor detection. A proteolytic activity assay with several MT-SP1-positive human cancer cell lines showed that MT-SP1 antibodies that inhibit recombinant enzyme activity in vitro also bind and inhibit the full-length enzyme expressed on cells. In contrast, in the same assay, MT-SP1-negative cancer cell lines were inactive. Fluorescence microscopy confirmed the cell surface localization of labeled antibodies bound to MT-SP1-positive cells. To evaluate in vivo targeting capability, 0.7 to 2 nmoles of fluorescently labeled antibodies were administered to mice bearing tumors that were positive or negative for MT-SP1. Antibodies localized to MT-SP1-positive tumors (n = 3), permitting visualization of MT-SP1 activity, whereas MT-SP1-negative tumors (n = 2) were not visualized. Our findings define MT-SP1 activity as a useful biomarker to visualize epithelial cancers using a noninvasive antibody-based method.

Indexed as

Protein Processing, Post-TranslationalAnimalsAntibodiesAntibody SpecificityBiomarkers, TumorDiagnostic ImagingEnzyme ActivationEnzyme InhibitorsFemaleFluorescent Antibody TechniqueHT29 CellsHumansMiceMice, NudeNeoplasmsSerine EndopeptidasesAntibodiesBiomarkers, TumorEnzyme InhibitorsSerine EndopeptidasesST14 protein, human

Identifiers

PMID20145119
PMCPMC2823079
OpenAlexW2142846457

What OpenQuestion holds

Textmetadata
LicenceTDM
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.