Abstract 1425 Membrane-anchored serine protease (MASP) regulation of protease-activated receptor-2 (PAR-2) signaling in ovarian cancer

Ovarian cancer (OvCa) is the most lethal gynecological cancer. Dysregulation of protease activity has been shown to play a significant role in OvCa progression. Testisin and matriptase are membrane-anchored serine proteases (MASPs) that activate protease-activated receptor-2 (PAR-2), all of which have been shown to be aberrantly upregulated in OvCa. PAR-2 is a G-protein coupled receptor (GPCR) that regulates inflammation, pain and tumor progression. Testisin and matriptase are two MASPs that proteolytically cleave PAR-2 at the same canonical cleavage site, Arg36, which unmasks an endogenous tethered ligand (TL).

Authors

Institutions

Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.108654
Primary Topic
Blood Coagulation and Thrombosis Mechanisms
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Abstract 1425 Membrane-anchored serine protease (MASP) regulation of protease-activated receptor-2 (PAR-2) signaling in ovarian cancer

Toni Antalis, Marguerite S. Buzza, Amando A. Strong
Journal of Biological Chemistry
Blood Coagulation and Thrombosis Mechanisms
article

Abstract 1425 Membrane-anchored serine protease (MASP) regulation of protease-activated receptor-2 (PAR-2) signaling in ovarian cancer

Toni Antalis, Marguerite S. Buzza, Amando A. Strong
article en

Abstract

Ovarian cancer (OvCa) is the most lethal gynecological cancer. Dysregulation of protease activity has been shown to play a significant role in OvCa progression. Testisin and matriptase are membrane-anchored serine proteases (MASPs) that activate protease-activated receptor-2 (PAR-2), all of which have been shown to be aberrantly upregulated in OvCa. PAR-2 is a G-protein coupled receptor (GPCR) that regulates inflammation, pain and tumor progression. Testisin and matriptase are two MASPs that proteolytically cleave PAR-2 at the same canonical cleavage site, Arg36, which unmasks an endogenous tethered ligand (TL).

Journal of Biological ChemistryVol. 301(5)
University of Maryland, Baltimore (US), Louisiana State University Health Sciences Center New Orleans (US)
Zero hunger
Openalex Percentile: Top 83%
Blood Coagulation and Thrombosis Mechanisms
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.