TMPRSS2
GeneName
TMPRSS2
Summary
TMPRSS2, also known as transmembrane protease serine 2, is a 54 kDa serine protease that is expressed in various tissues, including the respiratory and urogenital tracts. It is localised to the plasma membrane and extracellular regions, and plays a critical role in the processing of viral proteins, particularly as an entry receptor for viruses such as SARS-CoV-2. TMPRSS2 facilitates the cleavage of viral glycoproteins, which is essential for viral entry into host cells. Additionally, it is involved in protein autoprocessing and proteolytic activities that contribute to various physiological processes.
Importance
TMPRSS2 is relevant to: - Viral pathogenesis, particularly in the context of respiratory viruses, as it mediates entry into host cells - Cancer biology, due to its role in the progression of prostate cancer and potential as a therapeutic target - Understanding host-pathogen interactions, which can inform vaccine development and antiviral strategies - The modulation of immune responses, given its involvement in proteolytic processing of various proteins
Top Products
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Abcam Product Citation Summary
The data indicates that the TMPRSS2 target was investigated in the context of SMYD2 inhibition using human cell lines, specifically Caco-2, Calu-3, and HT-29. All experiments employed western blotting as the application method, highlighting the relevance of TMPRSS2 in this biological study.
Abcam Product Citation Table
Function
Plasma membrane-anchored serine protease that cleaves at arginine residues (PubMed:32703818, PubMed:35676539, PubMed:37990007, PubMed:38964328). Participates in proteolytic cascades of relevance for the normal physiologic function of the prostate (PubMed:25122198). Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells (PubMed:15537383, PubMed:25122198, PubMed:26018085). In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia (By similarity).
(Microbial infection) Facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via two independent mechanisms, proteolytic cleavage of ACE2 receptor which promotes viral uptake, and cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry (PubMed:24227843, PubMed:32142651, PubMed:32404436, PubMed:33051876, PubMed:34159616, PubMed:35676539, PubMed:37990007). The cleavage of SARS-COV2 spike glycoprotein occurs between the S2 and S2' site (PubMed:32703818). Upon SARS-CoV-2 infection, increases syncytia formation by accelerating the fusion process (PubMed:33051876, PubMed:34159616, PubMed:35676539). Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.
(Microbial infection) Receptor for human coronavirus HKU1-CoV, acts synergistically with disialoside glycans to facilitate the entry of the virus. After binding to cell-surface disialoside glycans, the viral S protein interacts with the inactive form of TMPRSS2 and inhibits its protease activity.
Post-translational modifications
Proteolytically processed; by an autocatalytic mechanism. Autocleavage induces active conformation.
Sequence Similarities
Belongs to the peptidase S1 family.
Tissue Specificity
Expressed in several tissues that comprise large populations of epithelial cells with the highest level of transcripts measured in the prostate gland. Expressed in type II pneumocytes in the lung (at protein level). Expressed strongly in small intestine. Also expressed in colon, stomach and salivary gland. Coexpressed with ACE2 within lung type II pneumocytes, ileal absorptive enterocytes, intestinal epithelial cells, cornea, gallbladder and nasal goblet secretory cells (Ref.21).
Cellular localization
- Cell membrane
- Single-pass type II membrane protein
- Transmembrane protease serine 2 catalytic chain
- Secreted
- Activated by cleavage and secreted.
Alternative names
PRSS10, TMPRSS2, Transmembrane protease serine 2, Serine protease 10
Database links
swissprot:O15393 entrezGene:7113 omim:602060
Other research areas
- Oncology