DOCSLIB.ORG

Product Datasheet Aldo-Keto Reductase 1B10/AKR1B10 Antibody

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Product Datasheet Aldo-Keto Reductase 1B10/AKR1B10 Antibody Product Datasheet Aldo-keto Reductase 1B10/AKR1B10 Antibody H00057016-A01 Unit Size: 0.05 ml Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles. Publications: 6 Protocols, Publications, Related Products, Reviews, Research Tools and Images at: www.novusbio.com/H00057016-A01 Updated 2/5/2017 v.20.1 Earn rewards for product reviews and publications. Submit a publication at www.novusbio.com/publications Submit a review at www.novusbio.com/reviews/destination/H00057016-A01 Page 1 of 3 v.20.1 Updated 2/5/2017 H00057016-A01 Aldo-keto Reductase 1B10/AKR1B10 Antibody Product Information Unit Size 0.05 ml Concentration This product is unpurified. The exact concentration of antibody is not quantifiable. Storage Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles. Clonality Polyclonal Preservative No Preservative Purity Unpurified Buffer Unpurified antisera so the specific antibody concentration is unknown. Contains 50% glycerol. Product Description Host Mouse Gene ID 57016 Gene Symbol AKR1B10 Species Human, Mouse Reactivity Notes Human, Mouse. Specificity/Sensitivity AKR1B10 - aldo-keto reductase family 1, member B10 (aldose reductase) Immunogen AKR1B10 (NP_064695, 76 a.a. ~ 144 a.a) partial recombinant protein with GST tag.VSKLWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKD DKGNAIGGKATFLDAWE Notes This product is produced by and distributed for Abnova, a company based in Taiwan. Product Application Details Applications Western Blot, ELISA Recommended Dilutions Western Blot 1:500, ELISA Application Notes Antibody reactive against cell lysate and recombinant protein for western blot. It has also been used for ELISA. Page 2 of 3 v.20.1 Updated 2/5/2017 Images Western Blot: Aldo-keto Reductase 1B10/AKR1B10 Antibody [H00057016-A01] - Analysis of AKR1B10 expression in K-562 (Cat # L009V1). Western Blot: Aldo-keto Reductase 1B10/AKR1B10 Antibody [H00057016-A01] - Analysis of AKR1B10 expression in NIH/3T3. Publications Jin GZ, Yu WL, Dong H et al. SUOX is a Promising Diagnostic and Prognostic Biomarker for Hepatocellular Carcinoma. J Hepatol 2013 May 08 [PMID: 23665285] (IHC-P, Human) Ebert B, Kisiela M, Wsol V et al. Proteasome inhibitors MG-132 and bortezomib induce AKR1C1; AKR1C3; AKR1B1; and AKR1B10 in human colon cancer cell lines SW-480 and HT-29. Chem Biol Interact 2011 Jan 06 [PMID: 21215737] (WB, Human) Loeffler-Ragg J, Mueller D, Gamerith G et al. Proteomic identification of aldo-keto reductase AKR1B10 induction after treatment of colorectal cancer cells with the proteasome inhibitor bortezomib. Mol Cancer Ther 2009 Jun 30 [PMID: 19567817] (IHC-P, WB, Human) Ebert B, Kisiela M, Wsol V et al. Proteasome inhibitors MG-132 and bortezomib induce AKR1C1; AKR1C3; AKR1B1; and AKR1B10 in human colon cancer cell lines SW-480 and HT-29. Chem Biol Interact. 2011 Jan 06 [PMID: 21215737] (WB, Human) Jin GZ, Yu WL, Dong H et al. SUOX is a Promising Diagnostic and Prognostic Biomarker for Hepatocellular Carcinoma. J Hepatol. 2013 May 08 [PMID: 23665285] (IHC-P, Human) Loeffler-Ragg J, Mueller D, Gamerith G et al. Proteomic identification of aldo-keto reductase AKR1B10 induction after treatment of colorectal cancer cells with the proteasome inhibitor bortezomib. Mol Cancer Ther 8(7):1995-2006. 2009 Jun 30 [PMID: 19567817] (IHC-P, WB, Human) Novus Biologicals USA Novus Biologicals Canada 10730 E. Briarwood Avenue 461 North Service Road West, Unit B37 Centennial, CO 80112 Oakville, ON L6M 2V5 USA Canada Phone: 303.730.1950 Phone: 905.827.6400 Toll Free: 1.888.506.6887 Toll Free: 855.668.8722 Fax: 303.730.1966 Fax: 905.827.6402 [email protected] [email protected] Novus Biologicals Europe General Contact Information 19 Barton Lane www.novusbio.com Abingdon Science Park Technical Support: [email protected] Abingdon, OX14 3NB, United Kingdom Orders: [email protected] Phone: (44) (0) 1235 529449 General: [email protected] Free Phone: 0800 37 34 15 Fax: (44) (0) 1235 533420 [email protected] Limitations This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt. For more information on our 100% guarantee, please visit www.novusbio.com/guarantee Earn gift cards/discounts by submitting a review: www.novusbio.com/reviews/submit/H00057016-A01 Earn gift cards/discounts by submitting a publication using this product: www.novusbio.com/publications.
Load more

Recommended publications
  • Development of Potent and Selective Inhibitors of Aldo−Keto Reductase
    Article pubs.acs.org/jmc Development of Potent and Selective Inhibitors of Aldo−Keto Reductase 1C3 (Type 5 17β-Hydroxysteroid Dehydrogenase) Based on N-Phenyl-Aminobenzoates and Their Structure−Activity Relationships † § ‡ § † † † ‡ Adegoke O. Adeniji, , Barry M. Twenter, , Michael C. Byrns, Yi Jin, Mo Chen, Jeffrey D. Winkler,*, † and Trevor M. Penning*, † Department of Pharmacology and Center of Excellence in Environmental Toxicology, Perelman School of Medicine, University of Pennsylvania, 130C John Morgan Building, 3620 Hamilton Walk, Philadelphia, Pennsylvania 19104-6084, United States ‡ Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104, United States *S Supporting Information ABSTRACT: Aldo−keto reductase 1C3 (AKR1C3; type 5 17β-hydroxy- steroid dehydrogenase) is overexpressed in castration resistant prostate cancer (CRPC) and is implicated in the intratumoral biosynthesis of testosterone and 5α-dihydrotestosterone. Selective AKR1C3 inhibitors are required because compounds should not inhibit the highly related AKR1C1 and AKR1C2 isoforms which are involved in the inactivation of 5α-dihydrotestosterone. NSAIDs, N-phenylanthranilates in particular, are potent but nonselective AKR1C3 inhibitors. Using flufenamic acid, 2-{[3-(trifluoromethyl)phenyl]amino}- benzoic acid, as lead compound, five classes of structural analogues were synthesized and evaluated for AKR1C3 inhibitory potency and selectivity. Structure−activity relationship (SAR) studies revealed that a meta-carboxylic acid group relative to the amine conferred pronounced AKR1C3 selectivity without loss of potency, while electron withdrawing groups on the phenylamino B-ring were optimal for AKR1C3 inhibition. Lead compounds did not inhibit COX-1 or COX-2 but blocked the AKR1C3 mediated production of testosterone in LNCaP-AKR1C3 cells. These compounds offer promising leads toward new therapeutics for CRPC.
    [Show full text]
  • Data Supplement
    JPET#173179 1 SUPPLEMENTAL DATA Manuscript title: Naturally occurring variants of human aldo-keto reductases with reduced in vitro metabolism of daunorubicin and doxorubicin Authors: Onkar S. Bains, Thomas A. Grigliatti, Ronald E. Reid, and K. Wayne Riggs Journal name: Journal of Pharmacology and Experimental Therapeutics TABLES Supplemental Table 1—Primers for creating non-synonymous single nucleotide polymorphic variants of human AKRs and CBR4 using site-directed mutagenesis. The base pair mutation is given beneath each variant [in square brackets]. Also, the mutated base pair is underlined in the forward and reverse primer sequences. ENZYME VARIANT FORWARD PRIMER (5'3') REVERSE PRIMER (5'3') I15F CAAGATGCCCTTCCTGGGGTT CCAACCCCAGGAAGGGCATC AKR1B1 [AT] GG TTG H42L CGGGTACCGCCTCATCGACTG GGGCACAGTCGATGAGGCGG [AT] TGCCC TACCCG L73V GCGTGAGGAGGTCTTCATCGT GCTGACGATGAAGACCTCCTC [CG] CAGC ACGC K90E GGGCCTGGTGGAAGGAGCCTG GGCAGGCTCCTTCCACCAGGC [AG] CC CC G204S GCCAGTCCAAAAGCATCGTGG GTCACCACGATGCTTTTGGAC [GA] TGAC TGGC T288I CCAGGATATGACCATCTTACTC GTAGCTGAGTAAGATGGTCAT [CT] AGCTAC ATCCTGG P87S CACTTTCTTTGAGAGATCCCTT CTTTCCTCACAAGGGATCTCT AKR1B10 [CT] GTGAGGAAAG CAAAGAAAGTG M286T GTGATGAGGAGACGGCAACCA GAGTATGGTTGCCGTCTCCTC [TC] TACTC ATCAC N313D GACTATCCCTTCGATGCAGAA CAATATTCTGCATCGAAGGGA [AG] TATTG TAGTC R170H CCAACTTCAACCACAGGCAGC CTCCAGCTGCCTGTGGTTGAA AKR1C1 [GA] TGGAG GTTGG Q172L CTTCAACCGCAGGCTGCTGGA GGATCATCTCCAGCAGCCTGC [AT] GATGATCC GGTTGAAG F46Y CAATAGAAGCCGGGTACCACC GAATCAATATGGTGGTACCCG AKR1C2 [TA] ATATTTGATTC GCTTCTATTG JPET#173179
    [Show full text]
  • BCAT1 Expression Associates with Ovarian Cancer Progression: Possible Implications in Altered Disease Metabolism
    www.impactjournals.com/oncotarget/ Oncotarget, Vol. 6, No. 31 BCAT1 expression associates with ovarian cancer progression: possible implications in altered disease metabolism Zhi-Qiang Wang1,2, Adnen Faddaoui1,2, Magdalena Bachvarova2, Marie Plante2,3, Jean Gregoire2,3, Marie-Claude Renaud2,3, Alexandra Sebastianelli2,3, Chantal Guillemette4,5, Stéphane Gobeil1,4, Elizabeth Macdonald6, Barbara Vanderhyden6, Dimcho Bachvarov1,2 1Department of Molecular Medicine, Laval University, Québec PQ, Canada 2Centre de recherche du CHU de Québec, L’Hôtel-Dieu de Québec, Québec PQ, Canada 3Department of Obstetrics and Gynecology, Laval University, Québec PQ, Canada 4Centre de recherche du CHU de Québec, CHUL, Québec PQ, Canada 5Faculty of Pharmacy, Laval University, Québec PQ, Canada 6Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON, Canada Correspondence to: Dimcho Bachvarov, e-mail: [email protected] Keywords: BCAT1, ovarian cancer, cancer metabolism, metastasis, DNA hypomethylation Received: May 07, 2015 Accepted: August 28, 2015 Published: September 10, 2015 ABSTRACT Previously, we have identified the branched chain amino-acid transaminase 1 (BCAT1) gene as notably hypomethylated in low-malignant potential (LMP) and high-grade (HG) serous epithelial ovarian tumors, compared to normal ovarian tissues. Here we show that BCAT1 is strongly overexpressed in both LMP and HG serous epithelial ovarian tumors, which probably correlates with its hypomethylated status. Knockdown of the BCAT1 expression in epithelial ovarian cancer (EOC) cells led to sharp decrease of cell proliferation, migration and invasion and inhibited cell cycle progression. BCAT1 silencing was associated with the suppression of numerous genes and pathways known previously to be implicated in ovarian tumorigenesis, and the induction of some tumor suppressor genes (TSGs).
    [Show full text]
  • AKR1C1 Controls Cisplatin-Resistance in Head and Neck Squamous Cell
    Chang et al. Journal of Experimental & Clinical Cancer Research (2019) 38:245 https://doi.org/10.1186/s13046-019-1256-2 RESEARCH Open Access AKR1C1 controls cisplatin-resistance in head and neck squamous cell carcinoma through cross-talk with the STAT1/3 signaling pathway Wei-Min Chang1, Yu-Chan Chang1, Yi-Chieh Yang1, Sze-Kwan Lin2, Peter Mu-Hsin Chang3,4*† and Michael Hsiao1,5*† Abstract Background: Cisplatin is the first-line chemotherapy used against most upper aerodigestive tract carcinomas. In head and neck cancer, sensitivity to cisplatin remains the key issue in treatment response and outcome. Genetic heterogeneity and aberrant gene expression may be the intrinsic factors that cause primary cisplatin-resistance. Methods: Combination of the HNSCC gene expression data and the cisplatin sensitivity results from public database. We found that aldo-keto reductase family 1 member C1 (AKR1C1) may be associated with cisplatin sensitivity in HNSCC treatment of naïve cells. We examined the AKR1C1 expression and its correlation with cisplatin IC50 and prognosis in patients. The in vitro and in vivo AKR1C1 functions in cisplatin-resistance through overexpression or knockdown assays, respectively. cDNA microarrays were used to identify the upstream regulators that modulate AKR1C1-induced signaling in HNSCC. Finally, we used the cigarette metabolites to promote AKR1C1 expression and ruxolitinib to overcome AKR1C1-induced cisplatin-resistance. Results: AKR1C1 positively correlates to cisplatin-resistance in HNSCC cells. AKR1C1 is a poor prognostic factor for recurrence and death of HNSCC patients. Silencing of AKR1C1 not only reduced in vitro IC50 but also increased in vivo cisplatin responses and vise versa in overexpression cells.
    [Show full text]
  • Aldo-Keto Reductase 1C1 (AKR1C1) As the First Mutated Gene in a Family with Nonsyndromic Primary Lipedema
    International Journal of Molecular Sciences Article Aldo-Keto Reductase 1C1 (AKR1C1) as the First Mutated Gene in a Family with Nonsyndromic Primary Lipedema Sandro Michelini 1 , Pietro Chiurazzi 2,3, Valerio Marino 4 , Daniele Dell’Orco 4 , Elena Manara 5 , Mirko Baglivo 5, Alessandro Fiorentino 1, Paolo Enrico Maltese 6 , Michele Pinelli 7,8 , Karen Louise Herbst 9, Astrit Dautaj 10 and Matteo Bertelli 5,10,* 1 Dipartimento di Riabilitazione, Ospedale San Giovanni Battista, A.C.I.S.M.O.M., 00148 Rome, Italy; [email protected] (S.M.); a.fi[email protected] (A.F.) 2 Istituto di Medicina Genomica, Università Cattolica del Sacro Cuore, 00168 Rome, Italy; [email protected] 3 Fondazione Policlinico Universitario “A.Gemelli” IRCCS, UOC Genetica Medica, 00168 Rome, Italy 4 Dipartimento di Neuroscienze, Biomedicina e Movimento, Sezione di Chimica Biologica, Università di Verona, 37134 Verona, Italy; [email protected] (V.M.); [email protected] (D.D.) 5 MAGI Euregio, 39100 Bolzano, Italy; [email protected] (E.M.); [email protected] (M.B.) 6 MAGI’s LAB, 38068 Rovereto, Italy; [email protected] 7 Dipartimento di Scienze Mediche Traslazionali, Sezione di Pediatria, Università di Napoli Federico II, 80131 Naples, Italy; [email protected] 8 Telethon Institute of Genetics and Medicine (TIGEM), 80078 Pozzuoli, Italy 9 Departments of Medicine, Pharmacy, Medical Imaging, Division of Endocrinology, University of Arizona, Tucson, AZ 85721, USA; [email protected] 10 EBTNA-Lab, 38068 Rovereto, Italy; [email protected] * Correspondence: [email protected] Received: 20 July 2020; Accepted: 27 August 2020; Published: 29 August 2020 Abstract: Lipedema is an often underdiagnosed chronic disorder that affects subcutaneous adipose tissue almost exclusively in women, which leads to disproportionate fat accumulation in the lower and upper body extremities.
    [Show full text]
  • AKR1C1 As a Biomarker for Differentiating the Biological Effects of Combustible from Non-Combustible Tobacco Products
    G C A T T A C G G C A T genes Article AKR1C1 as a Biomarker for Differentiating the Biological Effects of Combustible from Non-Combustible Tobacco Products Sangsoon Woo 1,†, Hong Gao 2,†, David Henderson 1, Wolfgang Zacharias 2,3, Gang Liu 4, Quynh T. Tran 4,* and G.L. Prasad 4 1 Statistical Genetics, Axio Research LLC, 4th Ave. Suite 200, Seattle, WA 98121, USA; [email protected] (S.W.); [email protected] (D.H.) 2 Department of Medicine, James Graham Brown Cancer Center, University of Louisville School of Medicine, Louisville, KY 40202, USA; [email protected] (H.G.); [email protected] (W.Z.) 3 Department of Pharmacology and Toxicology, University of Louisville School of Medicine, Louisville, KY 40202, USA 4 RAI Services Company, 401 N. Main Street, Winston-Salem, NC 27101, USA; [email protected] (G.L.); [email protected] (G.L.P.) * Correspondence: [email protected]; Tel.: +1-336-741-2772 † Co-first authors. Academic Editor: Selvarangan Ponnazhagan Received: 24 January 2017; Accepted: 25 April 2017; Published: 3 May 2017 Abstract: Smoking has been established as a major risk factor for developing oral squamous cell carcinoma (OSCC), but less attention has been paid to the effects of smokeless tobacco products. Our objective is to identify potential biomarkers to distinguish the biological effects of combustible tobacco products from those of non-combustible ones using oral cell lines. Normal human gingival epithelial cells (HGEC), non-metastatic (101A) and metastatic (101B) OSCC cell lines were exposed to different tobacco product preparations (TPPs) including cigarette smoke total particulate matter (TPM), whole-smoke conditioned media (WS-CM), smokeless tobacco extract in complete artificial saliva (STE), or nicotine (NIC) alone.
    [Show full text]
  • The Roles of AKR1C1 and AKR1C2 in Ethyl-3,4-Dihydroxybenzoate Induced Esophageal Squamous Cell Carcinoma Cell Death
    www.impactjournals.com/oncotarget/ Oncotarget, Vol. 7, No. 16 The roles of AKR1C1 and AKR1C2 in ethyl-3,4-dihydroxybenzoate induced esophageal squamous cell carcinoma cell death Wei Li1,*, Guixue Hou2,3,4,*, Dianrong Zhou5, Xiaomin Lou2, Yang Xu1, Siqi Liu2,4, Xiaohang Zhao1 1 State Key Laboratory of Molecular Oncology, Cancer Hospital, Peking Union Medical College & Chinese Academy of Medical Sciences, Beijing, China 2 CAS Key Laboratory of Genome Sciences and Information, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China 3University of Chinese Academy of Sciences, Beijing, China 4Proteomics Division, BGI-Shenzhen, Shenzhen, Guangdong, China 5Third School of Clinical Medicine, Southern Medical University, Guangzhou, China *These authors have contributed equally to this work Correspondence to: Xiaohang Zhao, e-mail: [email protected] Siqi Liu, e-mail: [email protected] Yang Xu, e-mail: [email protected] Keywords: aldo-keto reductase 1C1/C2, ethyl-3, 4-dihydroxybenzoate, MRM, ESCC Received: November 19, 2015 Accepted: February 20, 2016 Published: February 27, 2016 ABSTRACT The aldo-keto reductase (AKR) superfamily of enzymes is critical for the detoxification of drugs and toxins in the human body; these enzymes are involved not only in the development of drug resistance in cancer cells but also in the metabolism of polycyclic aromatic hydrocarbons. Here, we demonstrated that AKR1C1/C2 increased the metabolism of ethyl-3,4-dihydroxybenzoate (EDHB) in esophageal squamous cell carcinoma (ESCC) cells. Previous studies have shown that EDHB can effectively induce esophageal cancer cell autophagy and apoptosis, and the AKR1C family represents one set of highly expressed genes after EDHB treatment.
    [Show full text]
  • AKR1C1 As a Biomarker for Differentiating the Biological Effects of Combustible from Non-Combustible Tobacco Products
    Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted: 25 January 2017 doi:10.20944/preprints201701.0111.v1 Peer-reviewed version available at Genes 2017, 8, , 132; doi:10.3390/genes8050132 Articles AKR1C1 as a Biomarker for Differentiating the Biological Effects of Combustible from Non-Combustible Tobacco Products Sangsoon Woo 1,†, Hong Gao 2,†, David Henderson 1, Wolfgang Zacharias 2,3, Gang Liu 4, Quynh T. Tran 4,* and G. L. Prasad 4 1 Statistical Genetics, Axio Research LLC, 4th Ave. Suite 200, Seattle, WA 98121, USA; [email protected] (S.W.); [email protected] (D.H.) 2 Department of Medicine, James Graham Brown Cancer Center, University of Louisville School of Medicine, Louisville, KY 40202, USA; [email protected] (H.G.); [email protected] (W.Z.) 3 Department of Pharmacology and Toxicology, University of Louisville School of Medicine, Louisville, KY 40202, USA 4 RAI Services Company, 401 N. Main Street, Winston-Salem, NC 27101, USA; [email protected] (G.L.); [email protected] (G.L.P.) * Correspondence: [email protected]; Tel.: +01-336-741-2772 † Co-first authors Abstract Smoking has been established as a major risk factor for developing oral squamous cell carcinoma (OSCC), but less attention has been paid to the effects of smokeless tobacco products. Our objective is to identify potential biomarkers to distinguish the biological effects of combustible tobacco products from those of non-combustible using oral cell lines. Normal human gingival epithelial cells (HGEC), non-metastatic (101A) and metastatic (101B) OSCC cell lines were exposed to different tobacco product preparations (TPPs) including cigarette smoke total particulate matter (TPM), whole-smoke conditioned media (WS-CM), smokeless tobacco extract in complete artificial saliva (STE), or nicotine (NIC) alone.
    [Show full text]
  • Gene Expression Changes in Subcutaneous Adipose Tissue Due to Cushing’S Disease
    I HOCHBERG and others RNA analysis of adipose from 55:2 81–94 Research Cushing’s disease Open Access Gene expression changes in subcutaneous adipose tissue due to Cushing’s disease Irit Hochberg1,2, Innocence Harvey3, Quynh T Tran4, Erin J Stephenson3, Ariel L Barkan5, Alan R Saltiel2, William F Chandler6 and Dave Bridges1,3,7 1Institute of Endocrinology, Diabetes and Metabolism, Rambam Health Care Campus, Haifa, Israel Correspondence 2Life Science Institute, University of Michigan, Ann Arbor, MI, USA should be addressed 3Physiology, UTHSC, Memphis, TN, USA to I Hochberg or D Bridges 4Preventive Medicine, UTHSC, Memphis, TN, USA Emails 5Internal Medicine, University of Michigan, Ann Arbor, MI USA i_hochberg@rambam. 6Neurosurgery, University of Michigan, Ann Arbor, MI USA health.gov.il or 7Pediatrics, UTHSC, Memphis, TN, USA [email protected] Abstract Glucocorticoids have major effects on adipose tissue metabolism. To study tissue mRNA Key Words expression changes induced by chronic elevated endogenous glucocorticoids, we performed " Cushing’s syndrome RNA sequencing on the subcutaneous adipose tissue from patients with Cushing’s disease (nZ5) " lipolysis compared to patients with nonfunctioning pituitary adenomas (nZ11). We found a higher " insulin resistance expression of transcripts involved in several metabolic pathways, including lipogenesis, " glucocorticoid proteolysis and glucose oxidation as well as a decreased expression of transcripts involved in " lipogenesis inflammation and protein synthesis. To further study this in a model system, we subjected mice " RNA sequencing to dexamethasone treatment for 12 weeks and analyzed their inguinal (subcutaneous) fat pads, " transcriptome Journal of Molecular Endocrinology which led to similar findings. Additionally, mice treated with dexamethasone showed drastic decreases in lean body mass as well as increased fat mass, further supporting the human transcriptomic data.
    [Show full text]
  • The Role of AKR1B10 in Physiology and Pathophysiology
    H OH metabolites OH Review The Role of AKR1B10 in Physiology and Pathophysiology Satoshi Endo 1,* , Toshiyuki Matsunaga 2 and Toru Nishinaka 3 1 Laboratory of Biochemistry, Gifu Pharmaceutical University, Gifu 501-1196, Japan 2 Education Center of Green Pharmaceutical Sciences, Gifu Pharmaceutical University, Gifu 502-8585, Japan; [email protected] 3 Laboratory of Biochemistry, Faculty of Pharmacy, Osaka Ohtani University, Tondabayashi 584-8540, Osaka, Japan; [email protected] * Correspondence: [email protected] Abstract: AKR1B10 is a human nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reductase belonging to the aldo-keto reductase (AKR) 1B subfamily. It catalyzes the reduction of aldehydes, some ketones and quinones, and interacts with acetyl-CoA carboxylase and heat shock protein 90α. The enzyme is highly expressed in epithelial cells of the stomach and intestine, but down-regulated in gastrointestinal cancers and inflammatory bowel diseases. In contrast, AKR1B10 expression is low in other tissues, where the enzyme is upregulated in cancers, as well as in non- alcoholic fatty liver disease and several skin diseases. In addition, the enzyme’s expression is elevated in cancer cells resistant to clinical anti-cancer drugs. Thus, growing evidence supports AKR1B10 as a potential target for diagnosing and treating these diseases. Herein, we reviewed the literature on the roles of AKR1B10 in a healthy gastrointestinal tract, the development and progression of cancers and acquired chemoresistance, in addition to its gene regulation, functions, and inhibitors. Keywords: aldo-keto reductases; AKR1B10; biomarkers Citation: Endo, S.; Matsunaga, T.; Nishinaka, T. The Role of AKR1B10 in 1. Introduction Physiology and Pathophysiology.
    [Show full text]
  • Microbial Hydroxysteroid Dehydrogenases: from Alpha to Omega
    microorganisms Review Microbial Hydroxysteroid Dehydrogenases: From Alpha to Omega Heidi L. Doden 1,2 and Jason M. Ridlon 1,2,3,4,5,* 1 Microbiome Metabolic Engineering Theme, Carl R. Woese Institute for Genomic Biology, Urbana, IL 61801, USA; [email protected] 2 Department of Animal Sciences, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA 3 Division of Nutritional Sciences, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA 4 Cancer Center of Illinois, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA 5 Department of Microbiology and Immunology, Virginia Commonwealth University School of Medicine, Richmond, VA 23298, USA * Correspondence: [email protected] Abstract: Bile acids (BAs) and glucocorticoids are steroid hormones derived from cholesterol that are important signaling molecules in humans and other vertebrates. Hydroxysteroid dehydrogenases (HSDHs) are encoded both by the host and by their resident gut microbiota, and they reversibly convert steroid hydroxyl groups to keto groups. Pairs of HSDHs can reversibly epimerize steroids from α-hydroxy conformations to β-hydroxy, or β-hydroxy to !-hydroxy in the case of !-muricholic acid. These reactions often result in products with drastically different physicochemical properties than their precursors, which can result in steroids being activators or inhibitors of host receptors, can affect solubility in fecal water, and can modulate toxicity. Microbial HSDHs modulate sterols associated with diseases such as colorectal cancer, liver cancer, prostate cancer, and polycystic ovary syndrome. Although the role of microbial HSDHs is not yet fully elucidated, they may have therapeutic potential as steroid pool modulators or druggable targets in the future.
    [Show full text]
  • SUPPLEMENTARY DATA Supplementary Table 1. Characteristics of the Organ Donors and Human Islet Preparations Used for RNA-Seq
    SUPPLEMENTARY DATA Supplementary Table 1. Characteristics of the organ donors and human islet preparations used for RNA-seq and independent confirmation and mechanistic studies. Gender Age BMI Cause of death Purity (years) (kg/m2) (%) F 77 23.8 Trauma 45 M 36 26.3 CVD 51 M 77 25.2 CVD 62 F 46 22.5 CVD 60 M 40 26.2 Trauma 34 M 59 26.7 NA 58 M 51 26.2 Trauma 54 F 79 29.7 CH 21 M 68 27.5 CH 42 F 76 25.4 CH 30 F 75 29.4 CVD 24 F 73 30.0 CVD 16 M 63 NA NA 46 F 64 23.4 CH 76 M 69 25.1 CH 68 F 23 19.7 Trauma 70 M 47 27.7 CVD 48 F 65 24.6 CH 58 F 87 21.5 Trauma 61 F 72 23.9 CH 62 M 69 25 CVD 85 M 85 25.5 CH 39 M 59 27.7 Trauma 56 F 76 19.5 CH 35 F 50 20.2 CH 70 F 42 23 CVD 48 M 52 24.5 CH 60 F 79 27.5 CH 89 M 56 24.7 Cerebral ischemia 47 M 69 24.2 CVD 57 F 79 28.1 Trauma 61 M 79 23.7 NA 13 M 82 23 CH 61 M 32 NA NA 75 F 23 22.5 Cardiac arrest 46 M 51 NA Trauma 37 Abbreviations: F: Female; M: Male; BMI: Body mass index; CVD: Cardiovascular disease; CH: Cerebral hemorrhage.
    [Show full text]