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- Table of Contents
Facts about Alpha-1-antichymotrypsin.
Human | |
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Gene Name: | SERPINA3 |
Uniprot: | P01011 |
Entrez: | 12 |
Belongs to: |
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serpin family |
AACTMGC88254; ACTGIG25; alpha 1-Antichymotrypsin; alpha-1-antichymotrypsin; antitrypsin), member 3; Cell growth-inhibiting gene 24/25 protein; growth-inhibiting protein 24; growth-inhibiting protein 25; member 3; serine (or cysteine) proteinase inhibitor, clade A (alpha-1 antiproteinase; serine (or cysteine) proteinase inhibitor, clade A, member 3; Serpin A3; serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin)
Mass (kDA):
47.651 kDA
Human | |
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Location: | 14q32.13 |
Sequence: | 14; NC_000014.9 (94612391..94624053) |
Plasma. Synthesized in the liver. Like the related alpha-1-antitrypsin, its concentration increases in the acute phase of inflammation or infection. Found in the amyloid plaques from the hippocampus of Alzheimer disease brains.
Secreted.
You might be curious what SERPINA3 means. This serine protease inhibit has been implicated in a variety of biological processes, including upregulating EZH2 and promoting non-TNBC cell growth. It's also been implicated in apoptosis in T-47D cells. These findings need to be confirmed by further studies.
The SERPINA3 protein is a histone methyltransferase that has been associated with the development of cancer. Its expression has been linked to the presence of EMT, malignant invasion of a wide variety of human tumors. The SERPINA3 Protein is also a mediator in various activities in cancer cell cells and may play an important role for tumor cell proliferation. Numerous studies have looked into the possible role of SERPINA3 for the prevention and progression cancer.
SERPINA3 blocks the activity of a variety of important serine protases, including complement, chymotrypsin and cathepsin G. It regulates lipid metabolism, wound healing, and apoptosis. Many of these agents have been proven to be effective in treating solid tumors.
The CDS fragment was amplified with PCR to create a SERPINA3 gene. The PCR products were purified and inserted into the XhoI site of a pcDNA3.1(-) expression vector. Sangon Biotech sequenced this plasmid to confirm its integrity. The SERPINA3 gene was successfully transfected to MDA-MB-231 cell lines. The result was a high level of expression.
In a titration test, serpinA3 was able to inhibit KLK9 by as much 80%. However, the effect of serpinA3 was reduced to 6% in matKLK9 solution. The new KLK9 ELISA test was used to detect serpinA3 and KLK9 complexes during the titration. The sample was then diluted in 6% BSA, and the reaction was carried out as per the protocol.
These preliminary studies are still too early to draw conclusions. Further research is needed to determine if serpinA3 inhibits tumour growth. SerpinA3 reduced tumour growth, but did not alter the invasiveness of CRC cell lines. This study shows the therapeutic benefits of serine protease inhibitors and is a major step towards more effective CRC treatment.
In a mouse model for TNBC, a new gene, SERPINA3, was discovered. In this study, SERPINA3 was expressed in TNBC cell lines from MDA-MB-231 and BT-549. The overexpression of this gene promoted proliferation and had no effect whatsoever on cell cycle or apoptosis. These data suggest SERPINA3 promotes TNBC cells growth.
We previously showed that SERPINA3 blocks TNBC cell migration. This study also confirmed that SERPINA3 overexpression is associated with aggressive phenotypes of TNBC. The mechanism behind the inhibition of ADAM9 gene expression is not yet clear. Cells expressing this gene show strong migratory responses to EGF. This could be due to the culture process.
To test the effect of SERPINA3 on the sensitivity of TNBC cells to cisplatin, Boster Bio used transfection of SERPINA3-overexpression plasmid in MCF-7 cells. The plasmids could be transfected into TNBC-derived cell lines and cisplatin (uM), was added based upon their IC50 values. To determine the drug that had the greatest effect on the cells' sensitivity, the cells were analysed using the CCK-8 detection method.
The favorable prognosis for breast cancer patients was associated with the LINC01140 gene, while LINC01578 (negatively correlated with poor prognosis) and LINC00667 (positively correlated with poor prognosis). The gene is expressed in tumor cells in two different regions: the lung and breast. Both the LINC gene as well as the miR200 are involved with stemness and EMT. This gene blocks the cyclin D1/Akt1 pathway.
BCL2 is included in the ncRNA/mRNA Network. It is possible that BCL2 may be the most important target for treating TNBC. The MUC14 gene belongs to this network. It plays an important function in cancer biology because it is multifunctional. BCL2 & EP300 are also oncogenic, which could be a therapeutic target.
The SERPINA3 gene product can be used as a biomarker for human cancers. It is expressed by a percent recovery KLK9 compared with control. It was the first time that any other gene product had been recognized in human tumors. It is now possible to identify tumor cells easily with the SERPINA3 ELISA Kits. However, it is important that you understand the best uses of SERPINA3 for tumor research.
Boster bio SERPINA3 markers are linked to the tumorigenesis T-47D cell lines and other cancers like colorectal (hepatocellular) and liver hepatocellular carcinoma. SERPINA3 activates the PI3Kd signals, which drive cell proliferation, in HCC. SERPINA3 may also promote the growth of invasive GBM cell lines through the ECM and inhibit apoptosis.
In order to determine whether SERPINA3 promoted apoptosis in T-48D cells, the authors assessed the expression of the gene GAPDH. They also did statistical analysis, normalizing the data to GAPDH. This study was done using a nested-PCR method and the two-dimensional cellular variation (DDCt).
The immune response against tumor cells is influenced in large part by the PD-1 signaling pathway. The development of new drugs to combat cancer may be possible if the PD-1-L1 signaling pathway is blocked. PD-1 blocking drug, which targets tumor-infiltrating t-cells with a particular molecule, is one such example.
After transfection with gRNAs in T-47D cell lines, Boster Bio SERPINA3 gene transcription was significantly increased. The injected cells were compared with untransduced controls. The nucleus of live cells was green while the nucleus of dead cells was red. The same was true in cells expressing Boster bio SERPINA3 marker.
BC tissues had higher levels of SERPINA3. Overexpression of this protein resulted in increased proliferation, migration, invasion, and knockdown of SERPINA3 had an opposite effect. Overexpression increased the ability of TNBC cells to invade the medium and induced epithelial-mesenchymal transition, while knockdown reduced the sensitivity to cisplatin. These results suggest that SERPINA3 may regulate BC development and could be a target for clinical treatment.
The SERPINA3 marker was first used to test the invasion capability of breast cancer cells. This was followed by IHC staining with a specific fluorescent dye, 3,3'-diaminobenzidine. The images were taken using Nikon Eclipse80i microscopes. The SERPINA3 expression has been preliminarily tested in clinical specimens with a two-level scale system.
The Cell Bank of Chinese Academy of Sciences has human HR+ and HR-negative cells for breast cancer. The cells were grown in RPMI/DMEM/high glucose media containing 10% fetal bovine serum. The samples were incubated at 37 degC in a humidified incubator with 5% CO2. The upper chamber was then washed twice in 4% paraformaldehyde, and stained with 0.5% of crystal violet. An inverted light microscope was used to count the number of cells in each field.
Recent research has shown that the SERPINA3 protein is a prognostic factor for glioma. It is also a promising target when it comes to gliomatherapy. High levels of this protein are associated with larger tumors and a lower WHO grade. Patients with high SERPINA3 level have shorter survival times than patients with low levels.
PMID: 6606438 by Chandra T., et al. Sequence homology between human alpha 1-antichymotrypsin, alpha 1- antitrypsin, and antithrombin III.
PMID: 8244391 by Poller W., et al. A leucine-to-proline substitution causes a defective alpha 1- antichymotrypsin allele associated with familial obstructive lung disease.