Evidence map›Paper›PMID 21148558›Full record

ArticleThe Journal of biological chemistry2011

Transport via the transcytotic pathway makes prostasin available as a substrate for matriptase.

Stine Friis, Sine Godiksen, Jette Bornholdt, Joanna Selzer-Plon, Hanne Borger Rasmussen, Thomas H Bugge, Chen-Yong Lin, Lotte K Vogel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.1field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 42 citations in OpenAlex.

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  9. Alpha-1 Antitrypsin-Deficient Macrophages Have Increased Matriptase-Mediated Proteolytic Activity.American journal of respiratory cell and molecular biology · 2017
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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 3 institutions in 2 countries.

Stine FriisDepartment of Cellular and Molecular Medicine, University of Copenhagen, 2200 Copenhagen, Denmark.
Sine Godiksen
Jette Bornholdt
Joanna Selzer-Plon
Hanne Borger Rasmussen
Thomas H Bugge
Chen-Yong Lin
Lotte K Vogel
University of Copenhagen · DKNational Institute of Dental and Craniofacial Research · USUniversity of Maryland, Baltimore · US

Funding

Cell surface serine proteases in development, tissue repair, and malignancyZIADE000699 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI BUGGE, THOMAS H · 2009 to 2025
$34.1M
Mechanisms of Deregulation of Matriptase in Breast CancerR01CA123223 · NCI · GEORGETOWN UNIVERSITY · PI JOHNSON, MICHAEL D, LIN, CHEN-YONG · 2010 to 2014
$1.6M
Intramural NIH HHSNCI NIH HHS R01 CA123223NCI NIH HHS R01-CA-123223
6 · The paper itself

Abstract

The matriptase-prostasin proteolytic cascade is essential for epidermal tight junction formation and terminal epidermal differentiation. This proteolytic pathway may also be operative in a variety of other epithelia, as both matriptase and prostasin are involved in tight junction formation in epithelial monolayers. However, in polarized epithelial cells matriptase is mainly located on the basolateral plasma membrane whereas prostasin is mainly located on the apical plasma membrane. To determine how matriptase and prostasin interact, we mapped the subcellular itinerary of matriptase and prostasin in polarized colonic epithelial cells. We show that zymogen matriptase is activated on the basolateral plasma membrane where it is able to cleave relevant substrates. After activation, matriptase forms a complex with the cognate matriptase inhibitor, hepatocyte growth factor activator inhibitor (HAI)-1 and is efficiently endocytosed. The majority of prostasin is located on the apical plasma membrane albeit a minor fraction of prostasin is present on the basolateral plasma membrane. Basolateral prostasin is endocytosed and transcytosed to the apical plasma membrane where a long retention time causes an accumulation of prostasin. Furthermore, we show that prostasin on the basolateral membrane is activated before it is transcytosed. This study shows that matriptase and prostasin co-localize for a brief period of time at the basolateral plasma membrane after which prostasin is transported to the apical membrane as an active protease. This study suggests a possible explanation for how matriptase or other basolateral serine proteases activate prostasin on its way to its apical destination.

Indexed as

Caco-2 CellsCell MembraneCell PolarityColonEnzyme ActivationEpithelial CellsHumansProstasinProtein TransportSerine EndopeptidasesProstasinSerine EndopeptidasesST14 protein, human

Identifiers

PMID21148558
PMCPMC3037692
OpenAlexW2080252542

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.