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Volumn 178, Issue 1-3, 2009, Pages 221-227

Type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase (AKR1C3): Role in breast cancer and inhibition by non-steroidal anti-inflammatory drug analogs

Author keywords

Aldo keto reductase; Indomethacin; N Phenylanthranilic acids; Prostaglandin metabolism; Steroid hormone metabolism

Indexed keywords

ACETYLSALICYLIC ACID; EFENAMIC ACID; ESTRADIOL; FLURBIPROFEN; IBUPROFEN; INDOLEACETIC ACID; INDOMETACIN; MECLOFENAMIC ACID; MELATONIN DERIVATIVE; N (4 CHLOROBENZOYL)MELATONIN; NAPROXEN; NONSTEROID ANTIINFLAMMATORY AGENT; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PROGESTERONE; PROSTAGLANDIN; PROSTAGLANDIN F; PROSTANOID RECEPTOR; SALICYLIC ACID; STEROID; SULINDAC; TESTOSTERONE 17BETA DEHYDROGENASE; UNCLASSIFIED DRUG; ZOMEPIRAC; 15 HYDROXYPROSTAGLANDIN DEHYDROGENASE; 3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; AKR1C3 PROTEIN, HUMAN; ENZYME INHIBITOR;

EID: 59049089110     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.10.024     Document Type: Article
Times cited : (67)

References (32)
  • 3
    • 0034287545 scopus 로고    scopus 로고
    • Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones
    • Penning T.M., Burczynski M.E., Jez J.M., Hung C.F., Lin H.K., Ma H., Moore M., Palackal N., and Ratnam K. Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones. Biochem. J. 351 (2000) 67-77
    • (2000) Biochem. J. , vol.351 , pp. 67-77
    • Penning, T.M.1    Burczynski, M.E.2    Jez, J.M.3    Hung, C.F.4    Lin, H.K.5    Ma, H.6    Moore, M.7    Palackal, N.8    Ratnam, K.9
  • 4
    • 0001429526 scopus 로고    scopus 로고
    • Characteristics of a highly labile human type 5 17β-hydroxysteroid dehydrogenase
    • Dufort I., Rheault P., Huang X.F., Soucy P., and Luu-The V. Characteristics of a highly labile human type 5 17β-hydroxysteroid dehydrogenase. Endocrinology 140 (1999) 568-574
    • (1999) Endocrinology , vol.140 , pp. 568-574
    • Dufort, I.1    Rheault, P.2    Huang, X.F.3    Soucy, P.4    Luu-The, V.5
  • 7
    • 48249132500 scopus 로고    scopus 로고
    • Progesterone receptor inhibits aromatase and inflammatory response pathways in breast cancer cells via ligand-dependent and ligand-independent mechanisms
    • Hardy D.B., Janowski B.A., Chen C.C., and Mendelson C.R. Progesterone receptor inhibits aromatase and inflammatory response pathways in breast cancer cells via ligand-dependent and ligand-independent mechanisms. Mol. Endocrinol. 22 (2008) 1812-1824
    • (2008) Mol. Endocrinol. , vol.22 , pp. 1812-1824
    • Hardy, D.B.1    Janowski, B.A.2    Chen, C.C.3    Mendelson, C.R.4
  • 10
    • 1442278729 scopus 로고    scopus 로고
    • 2α receptor in human endometrial adenocarcinoma: regulation of proliferation by activation of the epidermal growth factor receptor and mitogen-activated protein kinase signaling pathways
    • 2α receptor in human endometrial adenocarcinoma: regulation of proliferation by activation of the epidermal growth factor receptor and mitogen-activated protein kinase signaling pathways. J. Clin. Endocrinol. Metab. 89 (2004) 986-993
    • (2004) J. Clin. Endocrinol. Metab. , vol.89 , pp. 986-993
    • Sales, K.J.1    Milne, S.A.2    Williams, A.R.3    Anderson, R.A.4    Jabbour, H.N.5
  • 11
    • 17144381253 scopus 로고    scopus 로고
    • α,β-Unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor γ
    • Shiraki T., Kamiya N., Shiki S., Kodama T.S., Kakizuka A., and Jingami H. α,β-Unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor γ. J. Biol. Chem. 280 (2005) 14145-14153
    • (2005) J. Biol. Chem. , vol.280 , pp. 14145-14153
    • Shiraki, T.1    Kamiya, N.2    Shiki, S.3    Kodama, T.S.4    Kakizuka, A.5    Jingami, H.6
  • 14
    • 59049101352 scopus 로고    scopus 로고
    • 2 formation and progesterone elimination in MCF-7 breast cancer cells and promotes estrogen-dependent cell proliferation 16 June 2008, The Endocrine Society's 90th Annual Meeting, abstract # P2-43.
    • 2 formation and progesterone elimination in MCF-7 breast cancer cells and promotes estrogen-dependent cell proliferation 16 June 2008, The Endocrine Society's 90th Annual Meeting, abstract # P2-43.
  • 15
    • 11244348953 scopus 로고    scopus 로고
    • Development of nonsteroidal anti-inflammatory drug analogs and steroid carboxylates selective for human aldo-keto reductase isoforms: potential antineoplastic agents that work independently of cyclooxygenase isozymes
    • Bauman D.R., Rudnick S.I., Szewczuk L.M., Jin Y., Gopishetty S., and Penning T.M. Development of nonsteroidal anti-inflammatory drug analogs and steroid carboxylates selective for human aldo-keto reductase isoforms: potential antineoplastic agents that work independently of cyclooxygenase isozymes. Mol. Pharmacol. 67 (2005) 60-68
    • (2005) Mol. Pharmacol. , vol.67 , pp. 60-68
    • Bauman, D.R.1    Rudnick, S.I.2    Szewczuk, L.M.3    Jin, Y.4    Gopishetty, S.5    Penning, T.M.6
  • 16
    • 37349047898 scopus 로고    scopus 로고
    • An indomethacin analogue, N-(4-chlorobenzoyl)-melatonin, is a selective inhibitor of aldo-keto reductase 1C3 (type 2 3α-HSD, type 5 17β-HSD, and prostaglandin F synthase), a potential target for the treatment of hormone dependent and hormone independent malignancies
    • Byrns M.C., Steckelbroeck S., and Penning T.M. An indomethacin analogue, N-(4-chlorobenzoyl)-melatonin, is a selective inhibitor of aldo-keto reductase 1C3 (type 2 3α-HSD, type 5 17β-HSD, and prostaglandin F synthase), a potential target for the treatment of hormone dependent and hormone independent malignancies. Biochem. Pharmacol. 75 (2008) 484-493
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 484-493
    • Byrns, M.C.1    Steckelbroeck, S.2    Penning, T.M.3
  • 17
    • 9944264069 scopus 로고    scopus 로고
    • Characterization of a monoclonal antibody for human aldo-keto reductase AKR1C3 (type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase); immunohistochemical detection in breast and prostate
    • Lin H.K., Steckelbroeck S., Fung K.M., Jones A.N., and Penning T.M. Characterization of a monoclonal antibody for human aldo-keto reductase AKR1C3 (type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase); immunohistochemical detection in breast and prostate. Steroids 69 (2004) 795-801
    • (2004) Steroids , vol.69 , pp. 795-801
    • Lin, H.K.1    Steckelbroeck, S.2    Fung, K.M.3    Jones, A.N.4    Penning, T.M.5
  • 19
    • 5644246147 scopus 로고    scopus 로고
    • 17β-hydroxysteroid dehydrogenase type 1 is an independent prognostic marker in breast cancer
    • Oduwole O.O., Li Y., Isomaa V.V., Mantyniemi A., Pulkka A.E., Soini Y., and Vihko P.T. 17β-hydroxysteroid dehydrogenase type 1 is an independent prognostic marker in breast cancer. Cancer Res. 64 (2004) 7604-7609
    • (2004) Cancer Res. , vol.64 , pp. 7604-7609
    • Oduwole, O.O.1    Li, Y.2    Isomaa, V.V.3    Mantyniemi, A.4    Pulkka, A.E.5    Soini, Y.6    Vihko, P.T.7
  • 20
    • 33845728020 scopus 로고    scopus 로고
    • 17β-hydroxysteroid dehydrogenase 14 affects estradiol levels in breast cancer cells and is a prognostic marker in estrogen receptor-positive breast cancer
    • Jansson A.K., Gunnarsson C., Cohen M., Sivik T., and Stal O. 17β-hydroxysteroid dehydrogenase 14 affects estradiol levels in breast cancer cells and is a prognostic marker in estrogen receptor-positive breast cancer. Cancer Res. 66 (2006) 11471-11477
    • (2006) Cancer Res. , vol.66 , pp. 11471-11477
    • Jansson, A.K.1    Gunnarsson, C.2    Cohen, M.3    Sivik, T.4    Stal, O.5
  • 21
    • 37249090364 scopus 로고    scopus 로고
    • Cyclooxygenase-2-mediated metabolism of arachidonic acid to 15-oxo-eicosatetraenoic acid by rat intestinal epithelial cells
    • Lee S.H., Rangiah K., Williams M.V., Wehr A.Y., DuBois R.N., and Blair I.A. Cyclooxygenase-2-mediated metabolism of arachidonic acid to 15-oxo-eicosatetraenoic acid by rat intestinal epithelial cells. Chem. Res. Toxicol. 20 (2007) 1665-1675
    • (2007) Chem. Res. Toxicol. , vol.20 , pp. 1665-1675
    • Lee, S.H.1    Rangiah, K.2    Williams, M.V.3    Wehr, A.Y.4    DuBois, R.N.5    Blair, I.A.6
  • 22
    • 0343299437 scopus 로고
    • Inhibition of a major NAD(P)-linked oxidoreductase from rat liver cytosol by steroidal and nonsteroidal anti-inflammatory agents and by prostaglandins
    • Penning T.M., and Talalay P. Inhibition of a major NAD(P)-linked oxidoreductase from rat liver cytosol by steroidal and nonsteroidal anti-inflammatory agents and by prostaglandins. Proc. Natl. Acad. Sci. U.S.A. 80 (1983) 4504-4508
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 4504-4508
    • Penning, T.M.1    Talalay, P.2
  • 25
    • 37349053079 scopus 로고    scopus 로고
    • A salicylic acid-based analogue discovered from virtual screening as a potent inhibitor of human 20α-hydroxysteroid dehydrogenase
    • Dhagat U., Carbone V., Chung R.P., Matsunaga T., Endo S., Hara A., and El Kabbani O. A salicylic acid-based analogue discovered from virtual screening as a potent inhibitor of human 20α-hydroxysteroid dehydrogenase. Med. Chem. 3 (2007) 546-550
    • (2007) Med. Chem. , vol.3 , pp. 546-550
    • Dhagat, U.1    Carbone, V.2    Chung, R.P.3    Matsunaga, T.4    Endo, S.5    Hara, A.6    El Kabbani, O.7
  • 26
    • 10644285687 scopus 로고    scopus 로고
    • Molecular basis of the time-dependent inhibition of cyclooxygenases by indomethacin
    • Prusakiewicz J.J., Felts A.S., Mackenzie B.S., and Marnett L.J. Molecular basis of the time-dependent inhibition of cyclooxygenases by indomethacin. Biochemistry 43 (2004) 15439-15445
    • (2004) Biochemistry , vol.43 , pp. 15439-15445
    • Prusakiewicz, J.J.1    Felts, A.S.2    Mackenzie, B.S.3    Marnett, L.J.4
  • 27
    • 0034681109 scopus 로고    scopus 로고
    • Biochemically based design of cyclooxygenase-2 (COX-2) inhibitors: facile conversion of nonsteroidal antiinflammatory drugs to potent and highly selective COX-2 inhibitors
    • Kalgutkar A.S., Crews B.C., Rowlinson S.W., Marnett A.B., Kozak K.R., Remmel R.P., and Marnett L.J. Biochemically based design of cyclooxygenase-2 (COX-2) inhibitors: facile conversion of nonsteroidal antiinflammatory drugs to potent and highly selective COX-2 inhibitors. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 925-930
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 925-930
    • Kalgutkar, A.S.1    Crews, B.C.2    Rowlinson, S.W.3    Marnett, A.B.4    Kozak, K.R.5    Remmel, R.P.6    Marnett, L.J.7
  • 28
    • 0034721194 scopus 로고    scopus 로고
    • Ester and amide derivatives of the nonsteroidal antiinflammatory drug, indomethacin, as selective cyclooxygenase-2 inhibitors
    • Kalgutkar A.S., Marnett A.B., Crews B.C., Remmel R.P., and Marnett L.J. Ester and amide derivatives of the nonsteroidal antiinflammatory drug, indomethacin, as selective cyclooxygenase-2 inhibitors. J. Med. Chem. 43 (2000) 2860-2870
    • (2000) J. Med. Chem. , vol.43 , pp. 2860-2870
    • Kalgutkar, A.S.1    Marnett, A.B.2    Crews, B.C.3    Remmel, R.P.4    Marnett, L.J.5
  • 29
    • 27644575900 scopus 로고    scopus 로고
    • Indolyl esters and amides related to indomethacin are selective COX-2 inhibitors
    • Kalgutkar A.S., Crews B.C., Saleh S., Prudhomme D., and Marnett L.J. Indolyl esters and amides related to indomethacin are selective COX-2 inhibitors. Bioorg. Med. Chem. 13 (2005) 6810-6822
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 6810-6822
    • Kalgutkar, A.S.1    Crews, B.C.2    Saleh, S.3    Prudhomme, D.4    Marnett, L.J.5
  • 30
    • 3042748128 scopus 로고    scopus 로고
    • The role of COX-2 inhibition in breast cancer treatment and prevention
    • Arun B., and Goss P. The role of COX-2 inhibition in breast cancer treatment and prevention. Semin. Oncol. 31 (2004) 22-29
    • (2004) Semin. Oncol. , vol.31 , pp. 22-29
    • Arun, B.1    Goss, P.2
  • 31
    • 36849065197 scopus 로고    scopus 로고
    • Suppression of aromatase in human breast cells by a cyclooxygenase-2 inhibitor and its analog involves multiple mechanisms independent of cyclooxygenase-2 inhibition
    • Su B., Diaz-Cruz E.S., Landini S., and Brueggemeier R.W. Suppression of aromatase in human breast cells by a cyclooxygenase-2 inhibitor and its analog involves multiple mechanisms independent of cyclooxygenase-2 inhibition. Steroids 73 (2008) 104-111
    • (2008) Steroids , vol.73 , pp. 104-111
    • Su, B.1    Diaz-Cruz, E.S.2    Landini, S.3    Brueggemeier, R.W.4
  • 32
    • 12344300599 scopus 로고    scopus 로고
    • The roles of aldo-keto reductases in steroid hormone action
    • Bauman D.R., Steckelbroeck S., and Penning T.M. The roles of aldo-keto reductases in steroid hormone action. Drug News Perspect. 17 (2004) 563-578
    • (2004) Drug News Perspect. , vol.17 , pp. 563-578
    • Bauman, D.R.1    Steckelbroeck, S.2    Penning, T.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.