Evidence map›Paper›PMID 40091430›Full record

ArticleJournal of extracellular vesicles2025

Human Transmembrane Serine Protease 2 (TMPRSS2) on Human Seminal Fluid Extracellular Vesicles Is Proteolytically Active.

Emile Verhulst, Michelle De Bruyn, Pascale Berckmans, Yani Sim, Koen Augustyns, Isabel Pintelon, Maya Berg, Pieter Van Wielendaele, Anne-Marie Lambeir, Yann G-J Sterckx and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of extracellular vesicles, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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.

Emile VerhulstLaboratory of Medical Biochemistry, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp, Wilrijk, Belgium.ORCID https://orcid.org/0000-0002-8798-2750
Michelle De BruynLaboratory of Medical Biochemistry, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp, Wilrijk, Belgium.
Pascale BerckmansHealth Unit, Flemish Institute for Technological Research, Mol, Belgium.
Yani SimLaboratory of Medical Biochemistry, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp, Wilrijk, Belgium.
Koen AugustynsLaboratory of Medicinal Chemistry, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp, Wilrijk, Belgium.
Isabel PintelonLaboratory of Cell Biology and Histology, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp, Wilrijk, Belgium.
Maya BergInfla-Med Centre of Excellence, University of Antwerp, Wilrijk, Belgium.
Pieter Van WielendaeleLaboratory of Medical Biochemistry, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp, Wilrijk, Belgium.
Anne-Marie LambeirLaboratory of Medical Biochemistry, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp, Wilrijk, Belgium.
Yann G-J SterckxLaboratory of Medical Biochemistry, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp, Wilrijk, Belgium.
Inge NelissenHealth Unit, Flemish Institute for Technological Research, Mol, Belgium.
Ingrid De MeesterLaboratory of Medical Biochemistry, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp, Wilrijk, Belgium.

Funding

University Research Council (BOF) Antwerp 45146VITO NV
6 · The paper itself

Abstract

Human transmembrane serine protease 2 (TMPRSS2) has garnered substantial interest due to its clinical significance in various pathologies, notably its pivotal role in viral entry into host cells. The development of effective strategies to target TMPRSS2 is a current area of intense research and necessitates a consistent source of active TMPRSS2 with sufficient stability. Here, we comprehensively characterised human seminal-fluid extracellular vesicles (SF-EVs, also referred to as prostasomes), bearing a native source of surface-exposed, enzymatically active TMPRSS2 as demonstrated by high-sensitivity flow cytometry and a fluorometric activity assay. Additionally, we recombinantly produced human TMPRSS2 ectodomain in mammalian cells adopting a directed activation strategy. We observed comparable catalytic parameters and inhibition characteristics for both native SF-EV-associated and recombinant TMPRSS2 when exposed to serine protease inhibitor Nafamostat mesylate. Leveraging these findings, we developed a robust in vitro biochemical assay based on these SF-EVs for the screening of TMPRSS2-targeting compounds. Our results will accelerate the discovery and advancement of efficacious therapeutic approaches targeting TMPRSS2 and propel further exploration into the biological role of SF-EV-associated active TMPRSS2.

Indexed as

Extracellular VesiclesSemenSerine EndopeptidasesBenzamidinesGuanidinesHumansMaleProteolysisSerine Proteinase InhibitorsBenzamidinesGuanidinesnafamostatSerine EndopeptidasesSerine Proteinase InhibitorsTMPRSS2 protein, humanCD26high‐sensitivity flow cytometry (HS‐FCM)nafamostat mesylateprostasomesSARS‐ CoV‐2seminal fluid extracellular vesicles (SF‐EVs)transmembrane serine protease 2 (TMPRSS2)

Identifiers

PMID40091430
PMCPMC11911546

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.