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Hydroxyprostaglandin dehydrogenase 15-

15-hydroxyprostaglandin dehydrogenase, PGDH, 15-PGDH
This gene encodes a member of the short-chain nonmetalloenzyme alcohol dehydrogenase protein family. The encoded enzyme is responsible for the metabolism of prostaglandins, which function in a variety of physiologic and cellular processes such as inflammation. Mutations in this gene result in primary autosomal recessive hypertrophic osteoarthropathy and cranioosteoarthropathy. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2009] (from NCBI)
Top mentioned proteins: cyclooxygenase, ACID, Cyclooxygenase 2, CAN, HAD
Papers on 15-hydroxyprostaglandin dehydrogenase
Concerted actions of ameliorated colitis, aberrant crypt foci inhibition and 15-hydroxyprostaglandin dehydrogenase induction by sonic hedgehog inhibitor led to prevention of colitis-associated cancer.
Hahm et al., South Korea. In Int J Cancer, Apr 2016
Especially, CAC was accompanied with significant cancellation of 15-hydroxyprostaglandin dehydrogenase (15-PGDH), but their levels were significantly preserved with Shh inhibitors.
Sonic hedgehog inhibitors prevent colitis-associated cancer via orchestrated mechanisms of IL-6/gp130 inhibition, 15-PGDH induction, Bcl-2 abrogation, and tumorsphere inhibition.
Hahm et al., South Korea. In Oncotarget, Jan 2016
UNASSIGNED: Sonic hedgehog (SHH) signaling is essential in normal development of the gastrointestinal (GI) tract, whereas aberrantly activated SHH is implicated in GI cancers because it facilitates carcinogenesis by redirecting stem cells.
OATP2A1/SLCO2A1-mediated prostaglandin E2 loading into intracellular acidic compartments of macrophages contributes to exocytotic secretion.
Tamai et al., Kanazawa, Japan. In Biochem Pharmacol, Jan 2016
Expression of Cox-2 and 15-hydroxyprostaglandin dehydrogenase (15-Pgdh) was unchanged between PMs from Slco2a1(-/-) and WT mice.
Endogenous conversion of ω-6 to ω-3 polyunsaturated fatty acids in fat-1 mice attenuated intestinal polyposis by either inhibiting COX-2/β-catenin signaling or activating 15-PGDH/IL-18.
Hahm et al., Seoul, South Korea. In Int J Cancer, Jan 2016
As a result, ω-3 PUFAs significantly attenuated Apc mutation-induced intestinal polyposis accompanied with significant inhibition of Wnt/β-catenin signaling, COX-2, and PGE2, but induced significant levels of 15-PGDH.
15-oxo-ETE-induced internal carotid artery constriction in hypoxic rats is mediated by potassium channels.
Zhu et al., Harbin, China. In Physiol Res, Nov 2015
15-HETE was found to be rapidly converted into 15-oxo-ETE by 15-hydroxyprostaglandin dehydrogenase (15-PGDH) in some circumstances.
TISSUE REGENERATION. Inhibition of the prostaglandin-degrading enzyme 15-PGDH potentiates tissue regeneration.
Markowitz et al., Cleveland, United States. In Science, Jul 2015
Here, we show that inhibition of 15-hydroxyprostaglandin dehydrogenase (15-PGDH), a prostaglandin-degrading enzyme, potentiates tissue regeneration in multiple organs in mice.
Biomarker-directed Targeted Therapy in Colorectal Cancer.
Carethers, Ann Arbor, United States. In J Dig Cancer Rep, Jun 2015
Molecular biomarkers for CRC that may alter patient care and treatment include the presence or absence of microsatellite instability, the presence or absence of mutant KRAS, BRAF or PIK3CA, and the level of expression of 15-PGDH in the colorectal mucosa.
Multiple drug resistance-associated protein 4 (MRP4), prostaglandin transporter (PGT), and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) as determinants of PGE2 levels in cancer.
Fulton et al., Baltimore, United States. In Prostaglandins Other Lipid Mediat, 2015
15-hydroxyprostaglandin dehydrogenase (15-PGDH) metabolizes PGE2 and silences the pathway in this manner.
Expression and Cellular Localization of 15-Hydroxy-Prostaglandin-Dehydrogenase in Abdominal Aortic Aneurysm.
Camacho et al., Barcelona, Spain. In Plos One, 2014
PGE2 has been implicated in abdominal aortic aneurysm (AAA) associated hypervascularization. PGE2-metabolism involves 15-hydroxyprostaglandin-dehydrogenase (15-PGDH) the expression of which in AAA is unknown.
Breast cancer--new aspects of tumor biology: are calcitriol and cyclooxygenase-2 possible targets for breast cancer?
Friedrich et al., In Eur J Gynaecol Oncol, 2013
Two of these targets might be the cyclooxygenase-2 (COX-2), the key enzyme required to convert arachidonic acid to prostaglandins, and calcitriol [1,25(OH)2D3] which is the biologically active form of vitamin D. Both calcitriol and the inhibition of COX-2 have shown antiproliferative and prodifferentiation, as well as pro-apoptotic effects in different malignancies in vitro and in vivo, and the key prostaglandin catabolic enzyme 15-hydroxyprostaglandin dehydrogenase (15-PGDH) is known to have tumor suppressor activity.
Biochemical pathogenesis of aspirin exacerbated respiratory disease (AERD).
Teran et al., Mexico. In Clin Biochem, 2013
Underproduced PGE2 is metabolized by overexpression of 15 prostaglandin dehydrogenase (15-PGDH) to inactive products further reducing PGE2 at real time.
Fetal sex and preterm birth.
Bocking et al., Toronto, Canada. In Placenta, 2013
Placental or chorion trophoblast cells from pregnancies with a male fetus produced more pro-inflammatory TNFα in response to LPS stimulation and less anti-inflammatory IL-10 and granulocyte colony stimulating factor (G-CSF) than cells from pregnancies with a female fetus, more prostaglandin synthase (PTGS-2) and less prostaglandin dehydrogenase (PGDH).
β-catenin represses expression of the tumour suppressor 15-prostaglandin dehydrogenase in the normal intestinal epithelium and colorectal tumour cells.
Paraskeva et al., Bristol, United Kingdom. In Gut, 2012
beta-catenin has a novel role in promoting colorectal tumorigenesis through very early 15-PGDH suppression leading to increased PGE(2) levels, possibly even before COX-2 upregulation.
The potential therapeutic benefits of vitamin D in the treatment of estrogen receptor positive breast cancer.
Feldman et al., Stanford, United States. In Steroids, 2012
Calcitriol suppresses COX-2 expression and increases that of 15-PGDH thereby reducing the levels of inflammatory prostaglandins (PGs).
Identifying Allosteric Binding Sites in Proteins with a Two-State Go̅ Model for Novel Allosteric Effector Discovery.
Lai et al., Beijing, China. In J Chem Theory Comput, 2012
By use of one of the new allosteric sites predicted from Escherichia coli phosphoglycerate dehydrogenase (PGDH), novel allosteric regulating molecules were screened by molecular docking and enzymatic assay.
15-PGDH is reduced and induces apoptosis and cell cycle arrest in gastric carcinoma.
Wu et al., Shanghai, China. In World J Gastroenterol, 2012
Data suggest that reduction of 15-PGDH is associated with carcinogenesis and development of gastric carcinoma.
15-Hydroxyprostaglandin dehydrogenase associates with poor prognosis in breast cancer, induces epithelial-mesenchymal transition, and promotes cell migration in cultured breast cancer cells.
Iljin et al., Turku, Finland. In J Pathol, 2012
Our results indicate that HPGD is highly expressed in metastatic and aggressive breast cancer and promotes epithelial-mesenchymal transition and migration in breast cancer cells.
VEGF-D promotes tumor metastasis by regulating prostaglandins produced by the collecting lymphatic endothelium.
Stacker et al., Melbourne, Australia. In Cancer Cell, 2012
We identified regulation of PGDH, the key enzyme in prostaglandin catabolism, in endothelial cells of collecting lymphatics, as a key molecular change during VEGF-D-driven tumor spread.
Protein tyrosine nitration of 15-hydroxy prostaglandin dehydrogenase in the human mast cell line LAD2.
Befus et al., Edmonton, Canada. In Nitric Oxide, 2012
protein tyrosine nitration of 15-hydroxy prostaglandin dehydrogenase in the human mast cells
15-hydroxyprostaglandin dehydrogenase is downregulated and exhibits tumor suppressor activity in gastric cancer.
Kim et al., Seoul, South Korea. In Cancer Invest, 2011
Demonstrate both downregulation and a tumor suppressor activity of 15-PGDH in gastric cancer.
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