Evidence map›Paper›PMID 24070417›Full record

ArticleThe American journal of pathology2013

Imbalanced matriptase pericellular proteolysis contributes to the pathogenesis of malignant B-cell lymphomas.

Feng-Pai Chou, Ya-Wen Chen, Xianfeng F Zhao, Zijun Y Xu-Monette, Ken H Young, Ronald B Gartenhaus, Jehng-Kang Wang, Hiroaki Kataoka, Annie H Zuo, Robert J Barndt and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The American journal of pathology, 2013. 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
1.8field-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

25 citing papers in PubMed, 39 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

12 authors at 6 institutions in 3 countries.

Feng-Pai ChouDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington, District of Columbia.
Ya-Wen Chen
Xianfeng F Zhao
Zijun Y Xu-Monette
Ken H Young
Ronald B Gartenhaus
Jehng-Kang Wang
Hiroaki Kataoka
Annie H Zuo
Robert J Barndt
Michael Johnson
Chen-Yong Lin
Georgetown University Medical Center · USGeorgetown University · USThe University of Texas MD Anderson Cancer Center · USUniversity of Maryland, Baltimore · USNational Defense Medical Center · TWUniversity of Miyazaki · JP

Funding

Tissue Culture Shared ResourceP30CA051008 · NCI · GEORGETOWN UNIVERSITY · PI STEPHEN W BYERS · 1990 to 2026
$71.5M
Georgetown-Howard Universities Center for Clinical and Translational Science (GHUUL1TR000101 · NCATS · GEORGETOWN UNIVERSITY · PI MELLMAN, THOMAS A, VERBALIS, JOSEPH G · 2012 to 2015
$19.3M
Mechanisms of Deregulation of Matriptase in Breast CancerR01CA123223 · NCI · GEORGETOWN UNIVERSITY · PI JOHNSON, MICHAEL D, LIN, CHEN-YONG · 2010 to 2014
$1.6M
NCATS NIH HHS UL1 TR000101NCI NIH HHS P30 CA051008NCI NIH HHS P30-CA051008NCI NIH HHS R01 CA 123223NCI NIH HHS R01 CA123223
6 · The paper itself

Abstract

Membrane-associated serine protease matriptase is widely expressed by epithelial/carcinoma cells in which its proteolytic activity is tightly controlled by the Kunitz-type protease inhibitor, hepatocyte growth factor activator inhibitor (HAI-1). We demonstrate that, although matriptase is not expressed in lymphoid hyperplasia, roughly half of the non-Hodgkin B-cell lymphomas analyzed express significant amounts of matriptase. Furthermore, a significant proportion of these tumors express matriptase in the absence of HAI-1. Aggressive Burkitt lymphoma was more likely than indolent follicular lymphoma to express matriptase alone (86% versus 36%). In the absence of significant HAI-1 expression, the lymphoma cells activate and shed active matriptase when the cells are stimulated with mildly acidic buffer or the hypoxia-mimicking agent, CoCl2. The shed active matriptase can initiate pericellular proteolytic cascades by activating urokinase-type plasminogen activator on the cell surface of monocytes, and it can activate prohepatocyte growth factor. In addition, matriptase knockdown suppressed proliferation and colony-forming ability of neoplastic B cells in culture and growth as tumor xenografts in mice. Furthermore, exogenous expression of HAI-1 significantly suppressed proliferation of neoplastic B cells. These studies suggest that dysregulated pericellular proteolysis as a result of unregulated matriptase expression with limited HAI-1 may contribute to the pathological characteristics of several human B-cell lymphomas through modulation of the tumor microenvironment and enhanced tumor growth.

Indexed as

ProteolysisAnimalsB-LymphocytesCell Line, TumorCell ProliferationFemaleHepatocyte Growth FactorHumansLymph NodesLymphoma, B-CellMiceMice, SCIDProteinase Inhibitory Proteins, SecretorySerine EndopeptidasesUrokinase-Type Plasminogen ActivatorXenograft Model Antitumor AssaysHepatocyte Growth FactormatriptaseProteinase Inhibitory Proteins, SecretorySerine EndopeptidasesSPINT1 protein, humanUrokinase-Type Plasminogen Activator

Identifiers

PMID24070417
PMCPMC3791685
OpenAlexW2037087223

What OpenQuestion holds

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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.