ArticleThe Journal of biological chemistry2015
Aldo-keto Reductase 1B15 (AKR1B15): a mitochondrial human aldo-keto reductase with activity toward steroids and 3-keto-acyl-CoA conjugates.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Aldo-Keto Reductase 1B10 (AKR1B10) Restrains Trophoblast Cell Invasion via the ERK Signaling Pathway.International journal of molecular sciences · 2026Article
- Smoking-induced dysregulation of transposable elements in the small airway epithelium.Respiratory research · 2026Article
- Development of a prognostic model for thyroid cancer based on mitochondrial metabolism-related genes and immune profiling.World journal of surgical oncology · 2026Article
- Transcriptome Analysis, Machine Learning, and Experimental Identification of CDK7 Affecting the Progression of Pregnancy-induced Hypertension by Influencing Macrophage Polarization.Current molecular medicine · 2026Article
- Article
- Identification of M0 macrophage associated lipid metabolism genes for prognostic and immunotherapeutic response prediction in hepatocellular carcinoma.Discover oncology · 2025Article
- RNA-seq analysis of mitochondria-related genes regulated by AMPK in the human trophoblast cell line BeWo.Animal models and experimental medicine · 2025Article
- Predicting the prognosis of hepatocellular carcinoma based on genes related to polyamine metabolism.PeerJ · 2025Article
- Aldo-keto reductase (AKR) superfamily website and database: An update.Chemico-biological interactions · 2024Article
- Cancer to Cataracts: The Mechanistic Impact of Aldo-Keto Reductases in Chronic Diseases.The Yale journal of biology and medicine · 2024Review
- AKR1B10 and digestive tumors development: a review.Frontiers in immunology · 2024Review
- The pan-cancer landscape of aldo-keto reductase1B10 reveals that its expression is diminished in gastric cancer.Frontiers in immunology · 2024Article
- Estrogen-related genes influence immune cell infiltration and immunotherapy response in Hepatocellular Carcinoma.Frontiers in immunology · 2023Article
- The Role of AKR1B10 in Physiology and Pathophysiology.Metabolites · 2021Review
- Role of aldo-keto reductase family 1 member B1 (AKR1B1) in the cancer process and its therapeutic potential.Journal of cellular and molecular medicine · 2020Review
- The Biosynthesis of Enzymatically Oxidized Lipids.Frontiers in endocrinology · 2020Review
- Structural and Functional Biology of Aldo-Keto Reductase Steroid-Transforming Enzymes.Endocrine reviews · 2019Review
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- Aldo-Keto Reductases 1B in Adrenal Cortex Physiology.Frontiers in endocrinology · 2016Review
- Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Aldo-keto reductases (AKRs) comprise a superfamily of proteins involved in the reduction and oxidation of biogenic and xenobiotic carbonyls. In humans, at least 15 AKR superfamily members have been identified so far. One of these is a newly identified gene locus, AKR1B15, which clusters on chromosome 7 with the other human AKR1B subfamily members (i.e. AKR1B1 and AKR1B10). We show that alternative splicing of the AKR1B15 gene transcript gives rise to two protein isoforms with different N termini: AKR1B15.1 is a 316-amino acid protein with 91% amino acid identity to AKR1B10; AKR1B15.2 has a prolonged N terminus and consists of 344 amino acid residues. The two gene products differ in their expression level, subcellular localization, and activity. In contrast with other AKR enzymes, which are mostly cytosolic, AKR1B15.1 co-localizes with the mitochondria. Kinetic studies show that AKR1B15.1 is predominantly a reductive enzyme that catalyzes the reduction of androgens and estrogens with high positional selectivity (17β-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoA conjugates and exhibits strong cofactor selectivity toward NADP(H). In accordance with its substrate spectrum, the enzyme is expressed at the highest levels in steroid-sensitive tissues, namely placenta, testis, and adipose tissue. Placental and adipose expression could be reproduced in the BeWo and SGBS cell lines, respectively. In contrast, AKR1B15.2 localizes to the cytosol and displays no enzymatic activity with the substrates tested. Collectively, these results demonstrate the existence of a novel catalytically active AKR, which is associated with mitochondria and expressed mainly in steroid-sensitive tissues.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.