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- Table of Contents
Facts about Branched-chain-amino-acid aminotransferase, mitochondrial.
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Human | |
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Gene Name: | BCAT2 |
Uniprot: | O15382 |
Entrez: | 587 |
Belongs to: |
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class-IV pyridoxal-phosphate-dependent aminotransferase family |
BCAM; BCAT(m); BCAT2; BCATM; BCT2; BCT2EC 2.6.1.42; branched chain amino-acid transaminase 2, mitochondrial; branched chain aminotransferase 2, mitochondrial; branched-chain-amino-acid aminotransferase, mitochondrial; Eca40; Placental protein 18; PP18
Mass (kDA):
44.288 kDA
Human | |
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Location: | 19q13.33 |
Sequence: | 19; NC_000019.10 (48795064..48811029, complement) |
Ubiquitous.
[Isoform A]: Mitochondrion.; [Isoform B]: Cytoplasm.
If you're looking for more information about the BCAT2 gene, you've come to the right place. Boster has a wealth and variety of gene infographics available to assist you in making your decision. The informational content of the website covers every gene found in human and mouse cells. The site features a search bar that makes it easy to quickly find any gene you are interested in. The site also includes gene infographics and a comprehensive list with clinical applications.
Boster Bio BCAT2 gene informationgraphics provide basic information on the various genes found within human and mouse tissues. In addition, Boster offers a search bar to find any gene of interest. This information is extremely useful in understanding a disease or condition's biology. Scientists using gene infographics to determine whether a particular treatment is effective can find them very useful.
The BosterBio HSPD1 Picoband antibody Picoband is a monoclonal, highly specific antibody made from E. coli derived products. It is available in multiple formats and is supplied with high-quality lysis buffers. Boster Bio offers both ELISA Kits and Antibodies for Research. Boster Bio's antibodies are available through tebubio. When using Boster Bio antibodies, make sure to thoroughly read the label and ensure that the antibody is the correct one for the intended application.
Although BCAT2's functions in cells are still unclear, it is known to play a significant role regulation ferroptosis. It is linked with the BCAT family, which catalyzes the reversible oxidation of BCAAs into glutamate. Glutamate is an important metabolic pathway in ferroptosis regulation. It is also linked to system Xc–, which exchanges glutamate with cystine 1:1. High levels in glutamate can cause system Xc to be less active and promote ferroptosis.
Functionally, BCAT2 must be present in order to synthesize myoblasts. When cells are BCAT2-deficient, they show an impaired differentiation process. Depletion of BCAT2 significantly reduces mTORC1 signaling, which is required for myofibrillar protein synthesis. Depletion of BCAT2 also results in impaired differentiation, but these are still preliminary findings. Further studies are needed to understand the role of BCAT2 in muscle cell differentiation.
BCAT2 reduces S6 phosphorylation in myoblasts. BCAT2 contributes to the formation of myotubes in muscle tissue. Despite the increased number of cells, BCAT2 depletion led to a marked decrease in cell numbers. Further, depletion of BCAT2 leads to accumulation of differentiation-incompetent cells and increased apoptosis.
Depletion of BCAT2 prevented differentiation and reduced myoblast production in the study. Glutamin-containing proteins were not able to rescue myotube differentiation. This further supports the idea that BCAT2 is essential for myotube formation. It may interact with other proteins that inhibit myotube formation. If you have a BCAT2 mutation in your blood, you might be interested in its role in human cancer.
Besides predicting response to sorafenib, a small molecule called sorafenib inhibits BCAT2 expression. A combination of these drugs inhibits the growth of cancer cells and promotes ferroptosis. Its unique role as a cancer therapy treatment strategy could make it an innovative option. This novel molecule could be used by clinicians to target resistance to sorafenib.
It has been shown that allelic variation at BCAT2 is responsible for natural variation in seed BCAA levels. Complementation analysis has revealed that BCAT2 is also involved in glutamate recycling and free amino acid homeostasis. Seed-specific mutants have demonstrated the functionality of null alleles for bcat2. In addition, it is associated with mitochondrial localization.
BCAT enzymes can be used in a variety of applications. As such, they are potentially relevant for metabolic reprogramming in eukaryotic cells. Boster Bio's Gene Infographics offers more information. This site provides gene informationgraphics that cover all known human genes and mouse genes. A search bar allows users to narrow down their choices based upon the gene's location and name.
Using BCAT2 as a marker can be incredibly useful, particularly in the context of cell culture and tissue engineering. The expression levels of BCAT enzymes can be seen in the protein's sequence data. BCAT enzymes are also active when the ERG240 molecule is present. The BCAT2 indicator is being used in its most effective uses. Here are some examples of its usefulness.
The gene BCAT is a key regulator of cell proliferation and is linked to numerous cancers. It is upregulated via several signaling molecules, such as c-Myc, which is a transcription factor that regulates BCAT expression. BCAT1 has been shown to be associated with many types of cancer, including breast cancer and Burkitt's lymphoma.
Researchers used western blotting as well as immunohistochemical staining in order to assess the biological significance and expression of BCAT1 in HCC tissues. In the study, BCAT1 expression was significantly higher in HCC tissues than in adjacent non-cancerous tissues. BCAT1 protein expression was also linked to c-Myc expression suggesting that this protein could be an important biomarker in HCC treatment.
The BCAT2 marker has already been identified as a biomarker of cancer. Its expression is decreased by chemotherapy drugs like sorafenib and sulfasalazine. BCAT2 expression levels were also associated with tumor grade and other ferroptosis markers. The BCAT2 marker may provide a sensitive biomarker for advanced liver cancer.
AICAR, a powerful AMPK inhibitor, was shown to reduce BCAT2 expression in pancreatic carcinoma cells. This effect was reversed when the inhibitor was used. Compound C, a p53 inhibitor, also suppressed BCAT2 in pancreatic cancer cell lines. Additionally, ferroptosis inhibitors inhibited BCAT2 expression while erastin led to a reduction in tumor size of 36%.
Both the cytoplasmic as well as the mitochondria of a cell are home to the BCAT2 genes. It is present in both the organelles and is essential for cellular respiration. BCAT2 enzyme activities were determined by using a mitochondria isolation kit, MITO-ISO1, from Sigma-Aldrich. Afterwards, the samples were stained with mouse rabbit-BCAT2 (Abcam, #ab95976, 1:200). The MultiSkan Spectrum allowed for the quantification of BCAT2 activities. The final results were then calculated as the average of all visual field.
The mouse's BCAT2 gene can be found in exons 1 through 4. The mutation in the mouse Bcat2 gene mRNA was homozygous. It is T/C. Bcat2 EX-1 or EX-3 are heterozygous. The mutation was found both in the parents. RTPCR amplifications of BCAT2 mRNA in human tissues yields a truncated protof of about 350 bp (WT), while the affected tissue displays a truncated protofofof of approximately 230 bp.
Several mammalian expression plasmids are available in the market. One of the most popular types is FC-324 from Fubio Company. Its cloned genetic DNA is located at Suzhou in China. The BCAT2-overexpressing BCAT2 cells were then cultured in six well plates and grew to 70%, 80%, or both. The cells were then transfected with 10nM of shRNA against BCAT2 and a negative control.
PMID: 9165094 by Bledsoe R.K., et al. Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm).
PMID: 11170829 by Than N.G., et al. Molecular cloning and characterization of placental tissue protein 18 (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its novel alternatively spliced PP18b variant.