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Last update 08 May 2025

hepsin

Last update 08 May 2025

Basic Info

Synonyms

hepsin, HPN, Serine protease hepsin

+ [5]

Introduction

Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL (PubMed:15839837, PubMed:21875933). Plays a role in cell growth and maintenance of cell morphology (PubMed:21875933, PubMed:8346233). Plays a role in the proteolytic processing of ACE2 (PubMed:24227843). Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization (PubMed:26673890).

Drugs associated with hepsin

VD-4162

Target

HGFA x TMPRSS2 x hepsin

Mechanism

HGFA inhibitors [+2]

Active Org.

Washington University School of Medicine

Originator Org.

Washington University School of Medicine

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

VD-5123

Target

HGFA x TMPRSS2 x hepsin

Mechanism

HGFA inhibitors [+2]

Active Org.

Washington University School of Medicine

Originator Org.

Washington University School of Medicine

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Caramcillin

Target

HGFA x hepsin x matriptase

Mechanism

HGFA inhibitors [+2]

Active Org.-

Originator Org.-

Active Indication-

Inactive Indication

Bacterial Infections

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with hepsin

100 Translational Medicine associated with hepsin

0 Patents (Medical) associated with hepsin

354

Literatures (Medical) associated with hepsin

01 Jun 2025·Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy

Identifying Hepsin as a novel biomarker for human esophageal squamous cell carcinoma (ESCC) and its application in fluorescence imaging

Article

Author: Liu, Huifang ; Zhang, Jian ; Zhang, Dongjie ; Ren, Shenghan ; Xu, Xinyi ; Zheng, Yueting ; Liu, Siting ; Chen, Xueli

Human Esophageal squamous cell carcinoma (ESCC) represents a type of malignant tumor characterized by a high mortality rate and a generally poor surgical prognosis. The accurate labeling and high-specificity visualization of ESCC cells is extremely importance for its precise diagnosis and effective treatment. Fluorescence molecular imaging has emerged as one of the most critical modalities for cancer detection and therapeutic guidance, owing to its superior sensitivity, cost-effectiveness, portability, real-time imaging, and no damage. In this study, we initially verified that Hepsin, a protease, is highly expressed in ESCC through high-throughput immunocapture (HIC) and Western blot (WB) assays. Subsequently, we designed and synthesized an innovative activatable fluorescent probe, Ac-KQLR Rhodamine 110. It is specifically identified and cleaved by Hepsin, which is over-expressed in ESCC cells. Consequently, the Ac-KQLR Rhodamine 110 could be utilized for the activation fluorescence imaging of ESCC cells, providing a method for their precise visualization. In conclusion, this research highlights that the overexpression of Hepsin serves as a novel biomarker for ESCC. Based on Hepsin's high expression in ESCC, our team has developed a distinctive activation fluorescence imaging strategy that can be employed for the tracking and identification of ESCC. The implementation of this strategy could potentially revolutionize the current methodologies used for monitoring and treating cancer, thereby offering new hope and improved outcomes for patients diagnosed with ESCC.

01 Feb 2025·Archives of Biochemistry and Biophysics

Molecular characterization of the E2 conjugating enzyme LinfUbc13 in Leishmania infantum

Article

Author: Teixeira, Felipe Roberti ; Zanchetta Venancio, Mayla Gabriela ; Torres, Caroline ; Santana Travaglini Berti de Correia, Camila Rolemberg ; de Oliveira de Castro, Taissa ; Rodrigues da Silva, Eduardo Vagner ; Nemamiah Escolarique Ribeiro, Hariel ; Abdel Baqui, Munira Muhammad ; da Costa Mancin, Giovanna ; Gomes, Marcelo Damário

UBC13 is an orthologue of Homo sapiens ubiquitin-conjugation E2 enzymes described in Leishmania mexicana, a null mutant lacking this gene cannot be produced, suggesting essential functions in this parasite. Leishmania infantum is an etiological agent of visceral leishmaniasis, the most severe type of disease that is potentially fatal if untreated. The ubiquitination process has been targeted for leishmanicidal compounds, indicating its essential function in parasite homeostasis. Therefore, the molecular characterization of the ubiquitination process may provide a better understanding of the molecular and cellular basis of leishmaniasis. Here, we characterized the gene LINF_350017900 in Leishmania infantum, which was named LinfUBC13, an E2 orthologue of UBC13 in Leishmania mexicana and the UBE2D family in Homo sapiens, sharing 72-74 % identity with UBE2D1, UBE2D2, and UBE2D3. LinfUbc13 contains conserved catalytic residues, including Cys86 and the HPN motif, which are essential for ubiquitin-conjugating activity. Structural analysis revealed a high similarity between LinfUbc13 and human UBE2D proteins, with a root-mean-square deviation (RMSD) of 0.4 Å, suggesting conserved functions. Recombinant LinfUbc13 was expressed and shown to accept ubiquitin from E1, forming a thioester intermediate. Functional assays demonstrated that LinfUbc13 transfers ubiquitin to p53 through human HDM2 E3 ligase, confirming its role in ubiquitination. Subcellular localization showed that LinfUbc13 was distributed throughout the parasite cytoplasm. These findings highlight the conserved nature of the ubiquitin-proteasome system between Leishmania infantum and Homo sapiens, showing that LinfUbc13 is an E2 enzyme that plays a crucial role in parasitic development.

01 Jan 2025·Life Sciences

Intracellular autoactivation and surface location of hepsin, TMPRSS2, and TMPRSS13

Article

Author: Wang, Di ; Li, Hui ; Zhu, Rui ; Zhang, Ce ; Chen, Wenjun ; Shi, Lingyun ; Jin, Zili ; Zhang, Yue

AIMSHepsin (HPN), a Type II transmembrane serine protease (TTSP), is involved in hepatocyte metabolism and various diseases. It undergoes autoactivation on the surface of human hepatoma cells, a mechanism not observed in other cell types. This study aims to explore HPN activation and surface expression in endometrial epithelial cells.MATERIALS AND METHODSWe studied HPN zymogen activation and cell surface expression in human embryonic kidney 293 and endometrial epithelial AN3CA and Ishikawa cells using site-directed mutagenesis, Western blotting, flow cytometry, and immunostaining. Treatments with brefeldin A (BFA) and monensin, along with co-transfection assays, were employed to assess HPN activation and expression before reaching the cell surface. We also analyzed the activation and expression of TMPRSS2 and TMPRSS13 and examined the effect of the serine protease inhibitor HAI-1 on these proteases.KEY FINDINGSHPN zymogen autoactivates in the endoplasmic reticulum (ER) and Golgi apparatus. Its active form reduces cell surface expression through trans-autodegradation, a mechanism also applicable to in TMPRSS2 and TMPRSS13. Additionally, HAI-1 interacts with these TTSPs in different ways: it inhibits HPN activation and stabilizes its cell-surface expression; it inhibits TMPRSS2 activation without affecting its cell-surface expression; and it facilitates TMPRSS13 activation, protecting it from degradation and stabilizing its cell surface expression.SIGNIFICANCEThese results revealed an intracellular autoactivation and expression mechanism of HPN, TMPRSS2, and TMPRSS13, differing from the extracellular activated TTSPs. These findings provide new insights into the diverse mechanisms in regulating TTSP activation, potentially aiding in treating TTSP-related endometrial diseases.

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