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Last update 08 May 2025

matriptase

Last update 08 May 2025

Basic Info

Synonyms

CAP3, channel–activating protein 3, epithin

+ [17]

Introduction

Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site (PubMed:10373424). Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing (PubMed:18843291). Proteolytically cleaves and therefore activates TMPRSS13 (PubMed:28710277).

Drugs associated with matriptase

A-11

Target

matriptase

Mechanism

matriptase inhibitors

Active Org.

The University of California, San Francisco

Originator Org.

The University of California, San Francisco

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

VE-2843

Target

matriptase

Mechanism

matriptase inhibitors

Active Org.

Verseon Corp.

Originator Org.

Verseon Corp.

Active Indication

Solid tumor

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

VE-1787

Target

matriptase

Mechanism

matriptase inhibitors

Active Org.

Verseon Corp.

Originator Org.

Verseon Corp.

Active Indication

Solid tumor

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with matriptase

100 Translational Medicine associated with matriptase

0 Patents (Medical) associated with matriptase

774

Literatures (Medical) associated with matriptase

01 Aug 2025·Journal of Biotechnology

Fragmentation of recombinant human interleukin-12 by matriptase in CHO cell culture

Article

Author: Ma, Fengfei ; Liu, Anita Ping-Wen ; Zhang, Yixiao ; Shah, Sunil S ; Tang, Tiffany ; Aapjeet, Fnu ; Gopalan, Aditya ; Pan, Jessica ; Liu, Ren ; Rivera, Shannon ; Kallappagoudar, Satish ; Juan, Veronica

During the development of a recombinant CHO cell line expressing human Interleukin-12 fused to human IgG1 Fc (rhIL-12), we observed a prominent proteolytic cleavage of the rhIL-12 in its p40 subunit between Lys260 and Arg261. Using class-specific protease inhibitors, we concluded that the serine hydrolase family was responsible for the clipping. To identify the specific serine proteases involved, we conducted transcriptomic and proteomic analyses and identified several potential candidates. By performing in-vitro enzyme digestion experiments with these proteases, we determined that matriptase was responsible for the observed p40 clipping. Further confirmation was obtained through the development of matriptase (St14) knockout cell lines in which rhIL-12 clipping was almost completely abolished. Armed with this knowledge, we devised several strategies including increasing culture pH to reduce matriptase activity and rhIL-12 clipping during the manufacturing process.

25 Apr 2025·ACS Sensors

Preliminary Observations of a Substrate-Based Radiotracer Biosensor for In Vivo Positron Emission Tomography Imaging of Tumor Transmembrane Protease ST14

Article

Author: Zhao, Haitao ; Peng, Tukang ; Liu, Jianjun

Imaging protease proteolysis with positron emission tomography (PET) has not been well documented in the literature, primarily due to the absence of suitable radiotracers. This study aims to develop a substrate-based radiotracer biosensor for ST14 protease to facilitate direct in vivo PET imaging of proteolysis. The design of the substrate-based radiotracer RQARK-DOTA-⁶⁸Ga is characterized by the inclusion of an ST14 substrate RQAR moiety and a Lys-DOTA-⁶⁸Ga moiety, linked via an ST14 cleavage site. The enzymatic cleavage of this radiotracer by ST14 protease was characterized in vitro, and the proteolysis of ST14 was further confirmed through in vivo PET imaging in tumors expressing ST14. RQARK-DOTA-⁶⁸Ga was specifically cleaved by ST14 protease to yield Lys-DOTA-⁶⁸Ga and RQAR moieties, whereas the d-isomer, rqark-DOTA-68Ga, was not susceptible to cleavage by ST14 protease. In vivo PET imaging demonstrated high tumor uptake of radioactive signal postinjection RQARK-DOTA-⁶⁸Ga in ST14-expressing AsPC-1 xenografts, with optimal accumulation observed 1 h postinjection. In contrast, the d-isomer radiotracer, rqark-DOTA-⁶⁸Ga, exhibited negligible tumor uptake, indicating a distinct preference for the substrate-based radiotracer in regions of ST14-mediated proteolysis. Radio-HPLC analysis following extraction from AsPC-1 tumors injected with RQARK-DOTA-⁶⁸Ga identified a radioactive peak corresponding to Lys-DOTA-⁶⁸Ga, confirming enzymatic cleavage and the generation of the anticipated radioactive product in the tumor tissue. Preliminary results indicate that a novel strategy for noninvasive in vivo positron emission tomography imaging of the transmembrane protease ST14 in tumors has been introduced through the development and application of a substrate-based radiotracer biosensor. The radiotracer RQARK-DOTA-⁶⁸Ga, capable of producing imaging signals through structural changes triggered by substrate cleavage, has proven its ST14-targeting potency in both in vitro enzymatic assays and in vivo PET imaging.

10 Apr 2025·Journal of Medicinal Chemistry

From N-0385 to N-0920: Unveiling a Host-Directed Protease Inhibitor with Picomolar Antiviral Efficacy against Prevalent SARS-CoV-2 Variants

Article

Author: Hassanzadeh, Malihe ; Désilets, Antoine ; Gravel-Trudeau, Alice ; Arrowsmith, Cheryl H. ; Jean, François ; Leduc, Richard ; Joushomme, Alexandre ; Boudreault, Pierre-Luc ; Fraser, Bryan J. ; Niikura, Masahiro ; Pérez-Vargas, Jimena ; Champagne, William ; Marouseau, Étienne ; Thompson, Connor A. H. ; Ennis, Siobhan ; Lepage, Matthieu ; Lemieux, Gabriel ; Villanueva, Ivan

The worldwide spread of new SARS-CoV-2 variants emphasizes the need to diversify existing therapeutic strategies. TMPRSS2, a host protease crucial for SARS-CoV-2 entry, has garnered significant research attention as a potential target for therapeutic intervention. Here, we optimized N-0385, a previously reported TMPRSS2 ketobenzothiazole-based peptidomimetic inhibitor, by screening 135 derivatives for target affinity and antiviral potency. Among the top candidates, N-0695 exhibited low nanomolar K_i values against three TTSPs associated with respiratory virus entry: TMPRSS2, matriptase, and TMPRSS13. Notably, N-0920 demonstrated exceptional potency in reducing SARS-CoV-2 variants EG.5.1 and JN.1 entry in Calu-3 cells, representing the first in cellulo picomolar inhibitor with EC₅₀ values of 300 and 90 pM, respectively. Additionally, molecular modeling provided insights into the binding interactions between the compounds and their targets. This study underscores the effectiveness of our screening approach in refining an existing peptidomimetic scaffold to enhance selectivity and antiviral activity.

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matriptase

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