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- Table of Contents
Facts about Aldehyde dehydrogenase family 3 member A2.
Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid (PubMed:22633490). .
Human | |
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Gene Name: | ALDH3A2 |
Uniprot: | P51648 |
Entrez: | 224 |
Belongs to: |
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aldehyde dehydrogenase family |
Aldehyde dehydrogenase 10; aldehyde dehydrogenase 3 family, member A2; Aldehyde dehydrogenase family 3 member A2; ALDH10FLJ20851; EC 1.2.1; EC 1.2.1.3; FALDHDKFZp686E23276; fatty aldehyde dehydrogenase; Microsomal aldehyde dehydrogenase; SLS
Mass (kDA):
54.848 kDA
Human | |
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Location: | 17p11.2 |
Sequence: | 17; NC_000017.11 (19648150..19677596) |
Detected in liver (at protein level).
Microsome membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side.
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The ALDH superfamily has many members. In addition to ALDH3A2, the group includes ALDH genes. The ALDH superfamily may be evolutionary stable, or it may have undergone changes during evolution. Molecular biology uses of the ALDH3A2 marker may help answer this question. Molecular biology uses of the ALDH3A2 marker are growing in number and importance. This article summarizes some of these uses.
The ALDH3A2 gene is encoded by a nucleotide sequence starting with the first ATG codon. Depending on the length of the protein, the gene may have skipped a premature termination codon or been suppressed. While protein synthesis termination is not 100% efficient, several methods exist to prolong the reading frame by circumventing the stop codon. These include translational bypassing, in-frame suppression, and ribosomal frame shifting.
The ALDH3A2 gene is found in a variety of tissues and is part of the ALDH superfamily. The ALDH gene produces an enzyme called fatty aldehyde dehydrogenase. This enzyme oxidizes aldehydes to carboxylic acids, a form used by the body for energy. ALDH3A2 is found in most tissues, but is most abundant in the liver. The enzyme is found in the endoplasmic reticulum, a structure that plays a role in protein processing.
Copy number variants of ALDH3A2 are defined as changes in DNA sequences that are not rearranged. For example, human ALDH3A2 contains six unique peptides. The sequences of these amino acids are included in Supplementary Materials. These amino acids are used as markers for various types of ALDHs. They can be used to confirm gene-duplications in many cases.
The ALDH3A2 enzyme has recently gained much attention in cancer research, where it has been confirmed as a new marker of stem cells in various solid tumors. While targeted treatments have been developed for this enzyme, they have had limited success in improving patient outcomes in the clinic. Because there are 19 isoforms of ALDH, different isoforms may exhibit similar biological functions in cancer. Therefore, the ALDH enzyme has a wide variety of applications in cancer research.
The ALDH enzyme is made up of dimeric and tetrameric forms. Dimeric ALDH is red, while tetrameric ALDHs are cyan. The dimeric form of ALDH3A2 has an extended C-terminal tail, which contributes to its tetrameric assembly and protein stability. It wraps the opposing monomer and forms hydrogen bonds and salt bridges. In contrast, ALDH2 is gray.
ALDH3A2 is related to glioma research. It is known that ALDH may influence the development of GC, which can affect patient survival. Additionally, it may influence immune checkpoints such as CTLA4 and PDCD1.
The ALDH3A2 enzyme is also associated with a variety of biological processes, including cell cycle, proliferation, and response to stimulus. Its high expression phenotype is enriched in signaling pathways that are involved in b-alanine, butanoate, and isoleucine metabolism. This information is useful in diagnosing a range of diseases. Although this marker may not be universally applicable, its use in clinical research is expected to improve diagnostics and monitoring in various medical settings.
In addition to the use of the ALDH3A2 marker in clinical research, studies of ALDH-related diseases have also been undertaken. In addition, the ALDH enzyme has been associated with the development of several human diseases. Several studies, including those by Chao et al., have shown that patients with this enzyme may have a higher risk for developing cancer, diabetes, or kidney stones.
Molecular profiling of ALDH3A1 enzyme is a key component in tumor immunotherapy. ALDH3A1 is involved in the regulation of signaling molecules from EMT and inflammation. It also plays a role in PD-L1 expression and the release of immunosuppressive cytokines. Additionally, ALDH3A1 activity is associated with the cytoprotective role of ALDh2 in normal tissues. Furthermore, ALDH3A1 promotes stem cell development, differentiation, and release of immune suppressive cytokines.
ALDH3A1 is overexpressed in cancer cell lines, revealing incipient stem-like properties. Furthermore, high-level expression of ALDH3A1 induced a significant alteration in the redox proteome and genes. ALDH3A1-deficient cells exhibit a reduced capacity to form tumorspheres, whereas ALDH3A1-high spheres display a significant increase in these markers.
ALDH3A2 is a protein that is enriched in hepatic cells. When elevated in human cells, it can be used to identify cancer cells. However, it is less clear whether ALDH3A2 is present in human blood or urine. Moreover, ALDH3A2 is expressed in various cancer cells, including lung adenocarcinoma and skin melanoma.
In melanoma and non-small cell lung cancer, ALDH3A2 might influence the infiltration of immune cells. These findings also have implications for immunotherapy. For instance, ALDH3A2 could affect the levels of COX-2 and PD-L1 proteins, two of which are involved in tumor-related inflammation. These findings could be helpful for the design of experiments that aim to uncover the mechanism of enzyme action.
The ALDH3A2 gene is a candidate for cancer diagnosis, as it is involved in the metabolism of fats and carbohydrates. Boster has developed a reagent that will test for the presence of this gene in a variety of tissues, including brain, liver, and kidney. The reagent is highly sensitive and will provide the necessary information for the most accurate results. Best uses of the ALDH3A2 marker in cancer research include tumorigenesis, vascular disease, diabetes, hepatitis, and prostate cancer.
This reagent is a versatile tool in the diagnosis of various types of cancer, including skin melanoma and lung adenocarcinomas. The ALDH3A1 marker has been found to alter the redox state of tumor cells, indicating their reprogramming status. Additionally, it correlates with several markers of stemness, including Oct4 and Sox2.
In this study, ALDH3A2 expression was knocked down with siRNA interference in HGC-27 and MGC-803 cells. Results were analyzed by Western blotting and quantitative PCR. ALDH3A2 knockdown significantly increased mRNA expression of PDCD1, PDCD1LG2, and CTLA-4. Detailed analyses of the results are included in Figure S3.
PMID: 8528251 by de Laurenzi V., et al. Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene.
PMID: 9027499 by Rogers G.R., et al. Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH).