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- Table of Contents
Facts about Serine protease HTRA3.
May act as a tumor suppressor. Negatively regulates, in vitro, trophoblast invasion during placental development and may be involved in the development of the placenta in vivo.
Mouse | |
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Gene Name: | Htra3 |
Uniprot: | Q9D236 |
Entrez: | 78558 |
Belongs to: |
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peptidase S1C family |
EC 3.4.21; EC 3.4.21.-; EC 3.4.21.108; High-temperature requirement factor A3; HTRA 3; HtrA serine peptidase 3; HTRA3; Pregnancy-related serine protease; probable serine protease HTRA3; Prsp; serine protease HTRA3; Tasp
Mass (kDA):
49.149 kDA
Mouse | |
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Location: | 5|5 B3 |
Sequence: | 5; |
Highest level of isoform 1 in maternal part of the placenta, moderate level in heart, testis and ovary, low level in muscle and lung. High expression found in granulosa cells of the ovary. Expressed in bone matrix, particularly in articular chondrocytes. Very low level of isoform 2 expressed in placenta. Expressed in the bone matrix, particularly in articular chondrocytes.
The HTRA3 Marker is one of the Serine proteases that cleaves beta-casein/CSN2. This protein is essential for placental development and may play a role in tumor suppression. Boster Bio has antibodies to this protein that react with many types of animal samples, including human, mouse, and rabbit. Among other things, HTRA3 acts as a tumor suppressor and may be involved in placental development.
Several studies have shown that serine protienases play a role in the development of various cancers. Among them, HtrA1 and HtrA2 play dual roles in cancer, mediating cellular survival and death. HtrA3 is a tumor suppressor, implicated in the negative regulation of TGF-b signaling. HtrA4 shows inhibitory activity against various cancers, by inducing cell cycle arrest and apoptosis.
The expression of HTRA3 in tumor tissues correlated with the presence of immune infiltrates and the stage of the disease. Further analysis of its role in GC progression and prognosis showed a significant correlation between HTRA3 and TP53 status, a marker of T-stage tumors. Despite its limited clinical relevance, HTRA3 may be a useful marker in predicting prognosis of patients with gastric cancer.
Although it is unclear whether Helicobacter pylori is a bacterium, the protein it produces is important in regulating bacterial stress responses. In particular, Helicobacter pylori secretes HtrA into the extracellular environment where it cleaves off the ectodomain of the tumor suppressor E-cadherin.
Inhibitors of serine proteases can stabilize HtrA3 by inhibiting its own proteolytic activity. Four-amidinophenyl-methane sulfonyl-fluoride (APMSF) is a commonly used serine protease inhibitor. The inhibitor APMSF was added to 17degC synthesis at various concentrations, but it had no effect on the stability of HtrA3-L and HtrA3-S. Further, higher concentration of inhibitor is required for HtrA3 to be stable.
In the present study, the protein levels in the OC differentiation phase were measured by quantitative PCR (qPCR) and mass spectrometry. Htra1 and MMP9 were upregulated during OC differentiation. Oscar was also identified by western blot analysis. Using these data, these proteins were linked to the development of OCs. Although it is difficult to determine exactly which genes are involved in OC differentiation, a significant percentage of OA patients have elevated levels of HTRA3.
The gene encoding HTRA3 encodes a protein that cleaves beta-casein/Csn2 and several ECM proteoglycans. The enzyme also inhibits signaling from TGF-beta family proteins and fibronectin. Its function is unknown, but it may be involved in placental development, ovarian development, granulosa cell differentiation and luteinization.
High-temperature requirement factor A3 (HTRA3) is a serine protease involved in a variety of processes, including cell signaling and apoptosis. It is also a potent inhibitor of signaling by TGF-beta family proteins and negatively regulates trophoblast invasion during placental development. In addition, it has been implicated in ovarian development.
The expression of HTRA3 was correlated with the relative abundance of 24 immune cell types in the tumor microenvironment. Relative abundance of HTRA3 was compared to the expression of genes found in published signature gene lists, which included 509 genes. HTRA3 correlated with immune cell infiltration in tumors and was associated with specific expression groups. To examine the association between HTRA3 and immune cell infiltration, we used a Spearman correlation.
The extended binding patch lacks major residues from the conserved binding groove. When a peptide binds to this site, it causes alterations in regulatory loops, resulting in a catalytically favorable active site. Using this biochemical method, Boster Bio has identified a peptide that cleaves extracellular matrix proteoglycans.
High expression of HTRA3 in tumor cells is associated with an increased risk of developing cancer. Its expression correlates with the occurrence of thyroid cancer and the acquisition of invasive phenotypes in oral squamous cell carcinoma and colorectal cancer. High expression of HTRA3 is associated with a decreased five-year overall survival rate.
Researchers say that the presence of HTRA3 in the tumour samples provides a more detailed understanding of the protein's role in gastric cancer. Although the study has significant clinical implications, it does not address the question of whether HTRA3 is a predictive biomarker of GC or a therapeutic target. It is still early in the development of a definitive treatment for GC.
Although the activity of the enzyme is not completely understood, a comprehensive investigation of the interaction of HtrA3 with its substrates suggests that multiple pathways are involved in the protein's proteolytic activity. A detailed analysis of the HtrA3 N-SPD revealed that it cleaves b-casein and XIAP, but cyt-deficient mutants exhibited minimal activity.
PMID: 12728021 by Nie G.Y., et al. A novel serine protease of the mammalian HtrA family is up-regulated in mouse uterus coinciding with placentation.
PMID: 15206957 by Tocharus J., et al. Developmentally regulated expression of mouse HtrA3 and its role as an inhibitor of TGF-beta signaling.