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Aldo-keto reductase family 1, member C3

AKR1C3, prostaglandin F synthase, DD3, DDX, 17beta-hydroxysteroid dehydrogenase type 5
This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. It may play an important role in the pathogenesis of allergic diseases such as asthma, and may also have a role in controlling cell growth and/or differentiation. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2011] (from NCBI)
Top mentioned proteins: C-9, AKR1C2, ACID, CAN, HAD
Papers using AKR1C3 antibodies
Structure-function analysis of human l-prostaglandin D synthase bound with fatty acid molecules
Fortier Michel A. et al., In Frontiers in Pharmacology, 2009
... (Ser505) was from Santa Cruz biotechnology (Santa Cruz, CA, USA) and AKR1C3 was from Abcam Inc ...
Papers on AKR1C3
Knockdown of AKR1C3 exposes a potential epigenetic susceptibility in prostate cancer cells.
Campbell et al., Buffalo, United States. In J Steroid Biochem Mol Biol, Jan 2016
This raises an interesting possibility of a novel rational to target AKR1C3, the utilization of AKRIC3 selective inhibitors in combination with HDAC inhibition as part of novel epigenetic therapies in androgen deprivation therapy recurrent prostate cancer.
Epigenetic down-regulated DDX10 promotes cell proliferation through Akt/NF-κB pathway in ovarian cancer.
Qi et al., Dongying, China. In Biochem Biophys Res Commun, Jan 2016
However, the functions of DEAD box protein (DDX) members in ovarian cancer development remain largely unknown.
Berberine inhibits androgen synthesis by interaction with aldo-keto reductase 1C3 in 22Rv1 prostate cancer cells.
Li et al., Changchun, China. In Asian J Androl, Jan 2016
UNASSIGNED: Aldo-keto reductase family 1 member C3 has recently been regarded as a potential therapeutic target in castrate-resistant prostate cancer.
A novel function for the DEAD-box RNA helicase DDX-23 in primary microRNA processing in Caenorhabditis elegans.
Chan et al., Taipei, Taiwan. In Dev Biol, Dec 2015
In a let-7(mg279) sensitized genetic background, knockdown of a homolog of yeast splicing factor Prp28p, DDX-23, or a homolog of human helicases p68 and p72, DDX-17, enhanced let-7 loss-of-function phenotypes, suggesting that these helicases play a role in let-7 processing and/or function.
Osteoblasts promote castration-resistant prostate cancer by altering intratumoral steroidogenesis.
Welén et al., Göteborg, Sweden. In Mol Cell Endocrinol, Dec 2015
Osteoblast-stimulated LNCaP-19 cells displayed an increased expression of genes encoding for steroidogenic enzymes (CYP11A1, HSD3B1, and AKR1C3), estrogen signaling-related genes (CYP19A1, and ESR2), and genes for DHT-inactivating enzymes (UGT2B7, UGT2B15, and UGT2B17).
The DHEA-sulfate depot following P450c17 inhibition supports the case for AKR1C3 inhibition in high risk localized and advanced castration resistant prostate cancer.
Penning et al., Philadelphia, United States. In Chem Biol Interact, Jul 2015
The final step in conversion of Δ(4)-androstene-3,17-dione and 5α-androstanedione to T and DHT, respectively, is catalyzed by AKR1C3.
Updated survey of the steroid-converting enzymes in human adipose tissues.
Luu-The et al., Québec, Canada. In J Steroid Biochem Mol Biol, Mar 2015
Our work on 20α-HSD (AKR1C1), 3α-HSD type 3 (AKR1C2) and 17β-HSD type 5 (AKR1C3) allowed us to clarify the relevance of these enzymes for some aspects of adipose tissue function.
Effect of insulin on AKR1C3 expression in female adipose tissue: in-vivo and in-vitro study of adipose androgen generation in polycystic ovary syndrome.
Tomlinson et al., Birmingham, United Kingdom. In Lancet, Mar 2015
We hypothesised that insulin might drive adipose testosterone generation from androstenedione through aldoketoredutase type 3 (AKR1C3) in women with insulin resistance.
Drug resistance in castration resistant prostate cancer: resistance mechanisms and emerging treatment strategies.
Gao et al., Sacramento, United States. In Am J Clin Exp Urol, 2014
Expression of constitutively active variants of the androgen receptor, such as AR-V7, intracrine androgens and overexpression of androgen synthesis enzymes like AKR1C3, and increased drug efflux through ABCB1 are just some of the many discovered mechanisms of drug resistance.
Understanding androgen action in adipose tissue.
Tomlinson et al., Birmingham, United Kingdom. In J Steroid Biochem Mol Biol, 2014
In particular, AKR1C2 and AKR1C3 are crucial in the regulation of local androgen bioavailability within adipose tissue.
Function of PCA3 in prostate tissue and clinical research progress on developing a PCA3 score.
Yao et al., Shanghai, China. In Chin J Cancer Res, 2014
Prostate cancer gene 3 (PCA3, also known as DD3) is a new biomarker that could improve the accuracy of prostate cancer diagnosis.
RNA helicase DDX3 is a regulatory subunit of casein kinase 1 in Wnt-β-catenin signaling.
Niehrs et al., Heidelberg, Germany. In Science, 2013
The results also suggest that the kinase-stimulatory function extends to other DDX and CK1 members, opening fresh perspectives for one of the longest-studied protein kinase families.
Structure of AKR1C3 with 3-phenoxybenzoic acid bound.
Squire et al., Auckland, New Zealand. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012
determined the X-ray crystal structure of AKR1C3 with the cofactor NADP+ and the drug-like inhibitor 3-phenoxybenzoic acid bound at a resolution of 1.68 A degrees in space group P212121
Aldo-keto reductase 1C3 is expressed in differentiated human epidermis, affects keratinocyte differentiation, and is upregulated in atopic dermatitis.
Pentland et al., Rochester, United States. In J Invest Dermatol, 2012
AKR1C3 functions in differentiation-associated gene regulation and also has a role in supporting inflammation in atopic dermatitis.
Retinaldehyde is a substrate for human aldo-keto reductases of the 1C subfamily.
Parés et al., Barcelona, Spain. In Biochem J, 2012
the pro-proliferative action of AKR1C3 in HL-60 cells involves the retinoic acid signalling pathway and that this is in part due to the retinaldehyde reductase activity of AKR1C3
Aldo-keto reductase family 1 member C3 (AKR1C3) is expressed in adenocarcinoma and squamous cell carcinoma but not small cell carcinoma.
Fung et al., Oklahoma City, United States. In Int J Clin Exp Pathol, 2011
AKR1C3 immunoreactivity was extensively present in both adenocarcinoma and squamous cell carcinoma arising from the lung and the gastroesophageal junction, but not in small cell carcinoma.
Stereospecific reduction of 5β-reduced steroids by human ketosteroid reductases of the AKR (aldo-keto reductase) superfamily: role of AKR1C1-AKR1C4 in the metabolism of testosterone and progesterone via the 5β-reductase pathway.
Penning et al., Philadelphia, United States. In Biochem J, 2011
role of AKR1C3 in the metabolism of testosterone and progesterone via the 5beta-reductase pathway.
A network model of a cooperative genetic landscape in brain tumors.
Sikic et al., Chicago, United States. In Jama, 2009
A multigene risk scoring model based on 7 landscape genes (POLD2, CYCS, MYC, AKR1C3, YME1L1, ANXA7, and PDCD4) is associated with the duration of overall survival in 189 glioblastoma samples from TCGA (global log-rank P = .02
RGD peptides induce apoptosis by direct caspase-3 activation.
Salmon et al., Birmingham, United Kingdom. In Nature, 1999
On the basis of the ability of RGD-DDX interactions to trigger integrin activation, we suggest that RGD peptides induce apoptosis by triggering conformational changes that promote pro-caspase-3 autoprocessing and activation.
Further molecular complexities of H-2 K- and D-region antigens.
Iványi et al., In Nature, 1981
Three different types of molecule, distinct from Ia and Qa antigens, are distinguished in the products of the Ddx region, and two in the products of the Dk and Kd regions.
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