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Facts about Retinal dehydrogenase 1.
May get a broader specificity and oxidize other aldehydes in vivo (PubMed:19296407, PubMed:26373694, PubMed:25450233). .
Human | |
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Gene Name: | ALDH1A1 |
Uniprot: | P00352 |
Entrez: | 216 |
Belongs to: |
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aldehyde dehydrogenase family |
acetaldehyde dehydrogenase 1; ALDC; aldehyde dehydrogenase 1 family, member A1; aldehyde dehydrogenase 1, soluble; Aldehyde Dehydrogenase 1A1; Aldehyde Dehydrogenase 1-A1; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; aldehyde dehydrogenase, liver cytosolic; ALDH class 1; ALDH1; ALDH11; ALDH1A1; ALDH-E1; ALHDII; EC 1.2.1; EC 1.2.1.36; MGC2318; PUMB1; RALDH 1; RALDH1; retinal dehydrogenase 1; retinaldehyde dehydrogenase 1
Mass (kDA):
54.862 kDA
Human | |
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Location: | 9q21.13 |
Sequence: | 9; NC_000009.12 (72900671..72953053, complement) |
Cytoplasm, cytosol.
You may be wondering if ALDh2A1 is a good CSC marker. In this article, we will examine whether ALDh2A1 regulates cell function and promotes the development of stem cells. In addition, we will also discuss its possible uses in cancer research. As we can see ALDh2A1 is much more than a stemness indicator. It promotes stem-cell development and regulates cells functions.
ALDh2A1's enzymatic activity is important, even though it can be used as a CSC marker based only on cell morphology. ALDh2A1 expression in tumor tissues is common, so high levels can be used as a reliable CSC indicator. ALDh2A1 is also expressed in tumor tissues, consistent with the CSC concept, which emphasizes multipotent differentiation.
In this study, researchers used a fluorescence-activated cell sorting method to identify human PCa cell lines expressing ALDh2A1 and found that these cells have important CSC properties, such as tumorigenicity in vitro and in vivo, and the ability to self-renew. These cells were also sparsely expressed in the basal prostate glands. This was also associated with poor survival. In the end, CD133 and ALDh2A1 expression were associated both with higher cancer progression rates and poorer prognosis.
ALDh2A1 may not be a reliable CSC marker but it is useful in tumor diagnosis. ALDh2A1 activity has been shown to correlate with stage, survival, and metastasis. This does not mean that ALDh2A1 will be an effective CSC marker but it does prove its potential for use in tumor biopsy.
Cojoc, along with colleagues, published a paper that was published in Cancer Research. It suggested that the ALDH proteins may be a therapeutic target. Inhibiting ALDh2A1 might reverse radioresistant CSCs, as it plays an important role in CSC signaling. Should ALDh2A1 be considered as a CSC marker
ALDh2A1 a molecule that is involved in the conversion from acetaldehyde and acetic acids. The acetaldehyde-acetic acid conversion can be used as a measure of the activity ALDh2A1 proteins. For this purpose, cells were cultured as described above, scraped into 600 ml lysis buffer, containing 100 mM Tris-HCl pH 8.0, 10 mM DTT, 20% glycerol, and 1% Triton X-100. After that, acetaldehyde (10mM) was added into the cuvette and the activity ALDh2A1 enzymes were measured.
ALDh2A1 is implicated in drug resistance in cancer. Increased sensitivity to chemotherapy can be achieved by blocking ALDh2B1. It also inhibits OS cell growth and colony formation. In addition, it may be a prognostic marker for cancer. More research is needed to confirm this association. ALDh2B1 expression, however, is an important biomarker in OS patients.
To test whether ALDh2A1 inhibits cellular function, lentiviral vectors were designed against UBQLN1 (a protein encoded by ALDh2A1) and SAOS, respectively. These vectors then were transfected into cells with serum-free culture medium. Cells were scored using quantitative RTPCR analysis and immunoblotting after transfection.
After 24 h of incubation in DMEM containing 10% FBS, cells were plated onto coverslips. They were stained by DAPI and inspected every seven days for a total of 28 days. The tumors were also photographed every seven days for a total of 28 days. After the injection of the luciferin, the tumor samples were fixed in paraffin. If the tumor growth was greater than expected, the antibody could be reversed.
The Cell Signaling Technology protocol was used to measure the extent and intensity of staining in ALDh2B1. Sections from human OS tissue microarrays had to be paraffinized with alcohol and rehydrated in graded alcohol. The sections were then placed into boiling citrate buffer and left to set for 20 minutes. This completes the antigen retrieval procedure. The sections were then incubated overnight with ALDh2B1 antibodies. Finally, the samples were washed in PBS three times and analyzed by log-rank analysis.
The superfamily includes enzymes that detoxify many aldehydes. The ALDh2A1 genome is part of this superfamily. These enzymes play an important role in the biosynthesis of vitamin A and other molecular regulators that regulate cellular function. ALDH is becoming a popular marker for stem cells. Evidence suggests that it controls cell functions like self-renewal. differentiation and resistance to drugs.
SPSS 22.0 was used by the study authors to analyze quantitative and categorical data. They also used the KruskalWallis U and MannWhitney U tests to test for the relationship between the proteins and a variety clinicopathological factors. The Kaplan–Meier method was used in order to draw the DSS, PFS and DSS curves. A logrank test was used in order to compare the estimated curves with 95% confidence intervals. To determine the association between SALL4 AND ALDh2A, they used the Cox proportional danger regression model.
Researchers also found that ALDh2A1 expression was lower in cancer tissues than normal and SOC tissues. Researchers found that ALDh2A1 protein expression was significantly lower from SOC tissues than normal tissue samples. However, ALDh2A1 was more prominent in ovarian and benign breast cancers than in other types of cancer. Ultimately, the results are encouraging and suggest that ALDh2A1 may be a useful marker of stem cells in tumor tissue.
The study compared the expression levels of SALL4 (and ALDh2A1) in tumors and normal tissues. The researchers concluded that SALL4 and ALDh2A1 are not independent markers of CSC, but they do appear to interact with one another. More research is needed before the gene can be used as a marker for CSC. It's unclear whether ALDh2A1 is a marker for CSC in SOC.
ALDh2A1 is a gene recently identified as a marker of stem cells in malignant tumours. ALDh2A1 is responsible for the oxidation intracellular aldehydes, and converts retinol into RA. Retinol is an effective modulator of cell differentiation and proliferation and may contribute to the preservation of undifferentiated cells. ALDh2 can also be used to isolate human cells. In a recent study, Ginestier et al. identified ALDh2 as a stem cell marker in breast cancer and found a negative association with poor clinical outcomes.
ALDh2A1 gene expression can be found both in HSCs, and stromal tissues. These cells exhibit altered functions in many tissues and an increased sensitivity to damage to DNA. The ALDH genes is a critical regulator of many cellular functions involved in hematopoiesis. These include stem cell development, cancer progression, and regulation of stem cells. The ALDh2A1 gene could be a therapeutic target.
This gene has a dual role in regulating cancer stem cell differentiation. It has been shown to promote the growth and survival of primary human HSCs. ALDh2A1 is among 139 genes that are differentially expressed in human HSCs. It could also be useful for regenerative medicine. This protein is found in many normal tissues such as skin, bones, and nerves. It is also important in the promotion of vascular density in models of acute myocardial injury.
ALDh2A1 was also identified as a stem-cell marker. It has also been shown to be expressed by cancer cells. ALDh2A1 is a marker for stemness in lung and colorectal tumours. Its role in the development of cancer stem cells has not yet been fully understood. The ALDh2A1 gene marker may be a promising candidate in identifying cancer stem cell types in various types.
The ALDh2A1 protein, a marker for the activity of the enzyme ALDh2A, is expressed in breast cancer cells. This enzyme inhibits tumor immunity by causing MDSCs to grow and proliferate. This enzyme provides a novel vulnerability to the treatment of breast tumors. This enzyme also has other functions such as modulating tumor immunity and triggering chemokine dependent tumor angiogenesis.
The GEPIA2 database was used for comparing the mRNA expression levels in tumors and normal tissues of ALDh2A1 & SALL4. All expression analyses, including those of isoforms, could be done using the GEPIA2 online program. To identify potential CSC markers, we extracted and tracked 83 proteins markers. Cytoscape software was used to create PPI networks based upon the co-expressions of ALDh2A1 & SALL4 in human tumours.
ALDH-positive NSCLS cell lines have the highest self-renewal potential and differentiation potential in vitro. They also have the highest growth rates. ALDH-positive cells also possess the highest growth potentials in vivo. ALDH-positive NCI-1299 cells have an unmatched ability to self-renew or re-initiate serially-transplanted tumors.
The Wnt pathway regulates ALDh2A1 through its regulation. This promotes stemness and drug-resistance. TGFb downregulates ALDh2A1 using Smad4 signaling. ALDh2A1 is involved in Notch, Wnt, and PI3K/Akt signaling pathways. ALDh2A1 inhibition inhibits breast tumor growth by targeting the TAK1 enzyme.
Human seminoma cells express the ALDh2A1 protein. DSS is significantly enhanced by coexpressions of ALDh2A1/SALL4. This protein has recently been validated in a clinical trial involving human cancer patients. In the meantime, it is still a promising tool for treating cancer. However, it may not be enough to treat cancer. Boster Bio is exploring other applications for ALDh2A1 and its recombinant forms.
PMID: 2591967 by Hsu L.C., et al. Genomic structure of the human cytosolic aldehyde dehydrogenase gene.
PMID: 8214422 by Zheng C.F., et al. Cloning and expression of the full-length cDNAs encoding human liver class 1 and class 2 aldehyde dehydrogenase.
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