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- Table of Contents
Facts about Aldo-keto reductase family 1 member D1.
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Human | |
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Gene Name: | AKR1D1 |
Uniprot: | P51857 |
Entrez: | 6718 |
Belongs to: |
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aldo/keto reductase family |
3o5bred; Aldo-keto reductase family 1 member D1,3-oxo-5-beta-steroid 4-dehydrogenase; aldo-keto reductase family 1, member D1 (delta4-3-ketosteroid-5-beta-reductase); CBAS2; Delta(4)-3-oxosteroid 5-beta-reductase; EC 1.3.1.3; SRD5B1beta polypeptide 1 (3-oxo-5 beta-steroid delta4-dehydrogenase beta 1)
Mass (kDA):
37.377 kDA
Human | |
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Location: | 7q33 |
Sequence: | 7; NC_000007.14 (138076459..138118305) |
Highly expressed in liver. Expressed in testis and weakly in colon.
Cytoplasm.
In this Boster Bio: Best Uses of the AKR1D1 Marker review, you will learn more about AKR1D1 gene polymorphisms, how they affect drug efficacy, and why these markers are important for scientists. Additionally, we'll cover the use of XF1729 and how this gene polymorphism may impact the efficacy of a drug. This review is applicable to scientists all over the world.
Using BAC libraries from 16 tissue types, we identified AKR1C gene polymorphismas. Of these, six expressed all five AKR1C genes; two, AKR1CL2 and AKR1C4, expressed in only the pancreas and liver, respectively. Only one, AKR1C2, was expressed in brain. The number of clones within these BAC libraries and the tissue type of the AKR1C gene polymorphisms correlated with gene expression.
The AKR1C gene is expressed at low levels in both HBEC-KT and A549 cells. AKR1C expression is detected by 1-acenaphthenol oxidation, while activity of p-nitrobenzaldehyde reductase was similar in both HBEC-KT and A549 cells.
AKR1C family members significantly reduced AR-dependent MMTV reporter activity. Both AKR1C1 and AKR1C2 significantly reduced AR-dependent MMTV reporter activity. AKR1C3 did not significantly affect AR-dependent MMTV reporter activity. This study provides further support for the importance of AKR1C gene polymorphisms in the treatment of breast cancer.
While HBEC-KT cells had reduced expression levels of AKR1C1, AKR1C2 expressed at 90-fold higher levels than P450 1A1 in A549 cancer cell line. TCDD-induced mRNA expression in HBEC-KT cells correlated with the P450 1A1 transcript level. TCDD-induced mRNA expression in both lung cell lines was comparable.
AKR1C is expressed in various human tissues, including liver and lung. It is overexpressed in non-small-cell lung cancer and is positively correlated with poor prognosis. AKR1C3 expression was found to increase five-fold in metastatic CRPC cells and was significantly higher than in primary PCa. The researchers also confirmed that increased AKR1C3 mRNA and protein levels were observed in the metastatic stage of CRPC.
AKR1C gene polymorphismal sequences were used for analysis of enzyme activity. The resulting amino acid sequences showed a high degree of homology to aldo-keto reductase enzymes. The homology between these enzymes is evident in their cofactor-binding residues. The resulting AKR1C gene polymorphisms in Boster Bio were analyzed by phylogenetic analysis.
Genetic variation in the metabolizing enzymes contributes to the variability of disease and drug response. Aldo-keto reductase type 1C is a subfamily of reductases that play important roles in biotransformation. They have been linked to breast cancer, obesity, and polycystic ovarian disease. However, the role of AKR in drug efficacy and disease risk is uncertain.
The AKR1C gene has been linked to the development of cancer and resistance to chemotherapy drugs. These polymorphisms may play an important role in drug efficacy, pharmacokinetics, and safety. Further studies are needed to refine our understanding of this association and develop a robust scientific foundation for its clinical application. A common denominator should be identified to avoid compromising patient safety.
Moreover, AKR1C gene polymorphismatic sequences were identified. While AKR1CL1 sequences were not identified in the BAC subclones, AKR1C4 promoter regions were amplified from sixteen human tissues. Six tissues expressed all five AKR1C genes, whereas four were only expressed in brain. The expression of each gene was correlated with the number of clones found in the EST libraries.
However, there were significant associations between the AKR genes and the cancer risk score. The risk score was higher in patients with AFP levels above 200ng/mL. AKR gene expression was higher in male patients, while it was lower in female patients. Furthermore, the expression of three critical AKR genes was significantly correlated with survival. This study has important implications for drug development and research.
Despite these important results, further research is required to understand how the gene affects drug efficacy. Mutations in one or more AKR1C genes reduce enzyme activity, while others enhance the risk of life-threatening diseases. Further, AKR1C gene polymorphisms are known to be associated with increased risk of cancer and other life-threatening diseases.
In the study, the AKR1C gene was found to be associated with lung cancer, squamous cell carcinoma, and gastroesophageal junction cancer. The authors also found that AKR1C gene polymorphisms were associated with increased resistance to radiation. Further, the gene has been implicated in CRPC. In endometriosis, it reduces PGD2 levels to 11b-PGF2a, which has similar affinity to the Prostaglandin receptor.
The XF1729 AKR1C Marker is a new member of the AKR13B1 family. The protein encodes a protein that is related to the superfamily of aldo-keto reductases and NADPH-dependent oxidoreductases. It was cloned onto the pET32Xa/LIC vector.
Mutations in the AKR1D1 gene result in a significant decrease in the amount of the active enzyme in the body. This deficiency may lead to bile acid deficiency syndrome. The AKR1D1 gene has a role in the metabolism of bile acid. When the enzyme is deficient, bile acid levels are low and the patient cannot produce bile acids.
PMID: 7508385 by Kondo K.-H., et al. Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta- reductase and substrate specificity of the expressed enzyme.
PMID: 11342103 by Charbonneau A., et al. Genomic organization of a human 5beta-reductase and its pseudogene and substrate selectivity of the expressed enzyme.