Relevant bibliographies by topics / (or 17)-hydroxysteroid déhydrogénase

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic '(or 17)-hydroxysteroid déhydrogénase'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic '(or 17)-hydroxysteroid déhydrogénase.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "(or 17)-hydroxysteroid déhydrogénase"

1

ADAMSKI, JERZY, JOSHUA CARSTENSEN, BETTINA HUSEN, MEYKE KAUFMANN, YVAN de LAUNOIT, FRAUKE LEENDERS, MONIKA MARKUS, and PETER W. JUNGBLUT. "New 17?-Hydroxysteroid Dehydrogenases." Annals of the New York Academy of Sciences 784, no. 1 Challenges an (April 1996): 124–36. http://dx.doi.org/10.1111/j.1749-6632.1996.tb16232.x.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Poirier, Donald. "Inhibitors of 17β-Hydroxysteroid Dehydrogenases." Current Medicinal Chemistry 10, no. 6 (March 1, 2003): 453–77. http://dx.doi.org/10.2174/0929867033368222.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Mindnich, R., G. Möller, and J. Adamski. "The role of 17 beta-hydroxysteroid dehydrogenases." Molecular and Cellular Endocrinology 218, no. 1-2 (April 2004): 7–20. http://dx.doi.org/10.1016/j.mce.2003.12.006.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Penning, T. M. "17 -Hydroxysteroid dehydrogenase: inhibitors and inhibitor design." Endocrine Related Cancer 3, no. 1 (March 1, 1996): 41–56. http://dx.doi.org/10.1677/erc.0.0030041.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Isomaa, Veli V., Sergio A. Ghersevich, Olli K. Mäentausta, E. Hellevi Peltoketo, Matti H. Poutanen, and Reijo K. Vihko. "Steroid Biosynthetic Enzymes: 17 β Hydroxysteroid Dehydrogenase." Annals of Medicine 25, no. 1 (January 1993): 91–97. http://dx.doi.org/10.3109/07853899309147864.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Mendonca, B. B. "17 -Hydroxysteroid Dehydrogenase 3 Deficiency in Women." Journal of Clinical Endocrinology & Metabolism 84, no. 2 (February 1, 1999): 802–4. http://dx.doi.org/10.1210/jc.84.2.802.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Olusanjo, M. S., and S. Ahmed. "Inhibitors of 17-hydroxysteroid dehydrogenase type 3 (17-beta-HSD 3)." Drugs of the Future 34, no. 7 (2009): 555. http://dx.doi.org/10.1358/dof.2009.034.07.1380625.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Gobec, S., P. Brozic, and T. Rizner. "Inhibitors of 17β-Hydroxysteroid Dehydrogenase Type 1." Current Medicinal Chemistry 15, no. 2 (January 1, 2008): 137–50. http://dx.doi.org/10.2174/092986708783330629.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Antoun, G. R., I. Brglez, and D. G. Williamson. "A 17 β-hydroxysteroid dehydrogenase of female rabbit liver cytosol. Purification and characterization of multiple forms of the enzyme." Biochemical Journal 225, no. 2 (January 15, 1985): 383–90. http://dx.doi.org/10.1042/bj2250383.

Full text
Abstract:
Multiple forms of the soluble 17 beta-hydroxysteroid dehydrogenase of female rabbit liver were identified. NAD-dependent and NADP-dependent enzyme activities were separated by affinity chromatography on agarose-immobilized Procion Red HE3B, and three forms of the NADP-dependent enzyme activity were purified by chromatofocusing. These three enzyme forms are charge isomers and have no quaternary structure. The enzymes catalysed the C-17 oxidoreduction of oestrogens and androgens; with all enzyme forms the activity towards androgens was higher than that toward oestrogens. The enzymes also exhibited 3 alpha-hydroxysteroid dehydrogenase activity towards androgens of the 5 beta-androstane series. Comparison of the relative activities of the enzymes towards a number of oestrogen and androgen substrates revealed differences among the enzyme forms for both the oxidative and the reductive reactions. In particular, one enzyme form had a significantly lower Km for the 3 alpha-hydroxysteroid substrate and a higher 3 alpha-/17 beta-hydroxysteroid dehydrogenase activity ratio than the other two enzyme forms.
APA, Harvard, Vancouver, ISO, and other styles
10

VIHKO, R., O. MÄENTAUSTA, V. ISOMAA, V. P. LEHTO, K. BOMAN, and U. STENDAHL. "Human 17?-Hydroxysteroid Dehydrogenase in Normal and Malignant Endometrium." Annals of the New York Academy of Sciences 622, no. 1 The Primate E (May 1991): 392–401. http://dx.doi.org/10.1111/j.1749-6632.1991.tb37883.x.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "(or 17)-hydroxysteroid déhydrogénase"

1

Mensah-Nyagan, Guy Ayikoe. "Contribution à l'étude des neurostéroïdes dans le cerveau des amphibiens : biosynthèse des Delta(4)-3-cétostéroïdes et des 17β-hydroxystéroïdes, et régulation par les endozépines." Rouen, 1997. http://www.theses.fr/1997ROUES023.

Full text
Abstract:
En utilisant des anticorps dirigés respectivement contre la la 3β-hydroxystéroïde déshydrogénase (3β-HSD) et la 17β-hydroxystéroïde déshydrogénase (17β-HSD) placentaires humaines nous avons montré la présence de ces enzymes dans le système nerveux central (SNC) de la grenouille. Les neurones à 3β-HSD sont localisés dans le diencéphale et la 17β-HSD est exprimée par des épendymocytes du télencéphale. Des quantités importantes de progestérone (P), 17-hydroxyprogestérone (17OH-P), testostérone (T) et dihydrotestostérone (5α-DHT) ont été mesurées dans le télencéphale et le diencéphale de grenouilles mâles et femelles en combinant l'analyse HPLC d'extraits tissulaires au dosage radioimmunologique. La castration des animaux mâles ne modifie pas les concentrations cérébrales de T et de 5α-DHT. La T a été formellement caractérisée dans le télencephale par HPLC et chromatographie en phase gazeuse couplée à une identification par spectrométrie de masse. Les explants d'hypothalamus convertissent la prégnènolone tritiée ([3h]Delta(5)P) en [3h]P et [3H]17OH-P, et la formation de ces deux métabolites est réduite significativement par le trilostane, un inhibiteur spécifique de la 3β-HSD L'incubation des explants de télencephale avec la [3h]Delta(5)P a révélé la synthèse de 15 métabolites tritiés dont 7 coéluent avec la P, la 17OH-P, l'androsténédione, la T, la 5α-DHT et l'oestrone ou l'oestradiol. Par ailleurs, nous avons démontré que de nombreux neurones hypothalamiques à 3β-HSD expriment également des récepteurs périphériques aux benzodiazépines (PBR) localisés à la fois dans le cytoplasme et au niveau de la membrane plasmique. L'incubation des explants d'hypothalamus avec la [3h]Delta(5)P en présence du triakontatétraneuropeptide (TTN) induit une stimulation dose-dépendante de la biosynthèse des neurostéroïdes. L'effet du TTN est mimé par le Ro5-4864 et inhibé par le PK11195 mais n'est pas modifié par le flumazénil. En conclusion, ce travail démontre pour la première fois la biosynthèse des neurostéroïdes dans le SNC des amphibiens. Nos résultats indiquent également que la production des stéroïdes dans les neurones hypothalamiques est activée par le TTN lequel agit probablement via des PBR situés au niveau de la membrane plasmique.
APA, Harvard, Vancouver, ISO, and other styles
2

Breitling, Rainer. "Phylogenetische und bioinformatische Untersuchung der 17[beta]-Hydroxysteroiddehydrogenasen [17-beta-Hydroxysteroiddehydrogenasen] Struktur, Funktion und Evolution einer komplexen Proteinfamilie /." [S.l. : s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=962139920.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Green, Andrew Russell. "Regulatory factors in human breast : cytokines and 17#beta#-hydroxysteroid dehydrogenase." Thesis, University of Hull, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.389436.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Kobayashi, Kaori. "Expression of 17 β-hydroxysteroid dehydrogenase type IV in chick retinal pigment epithelium." Kyoto University, 1997. http://hdl.handle.net/2433/202174.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Wang, Ruixuan. "Expression and role of 17BETA-hydroxysteroid dehydrogenase type 1, 5 and 7 in epithelial ovarian cancer." Master's thesis, Université Laval, 2018. http://hdl.handle.net/20.500.11794/29632.

Full text
Abstract:
Le cancer de l’ovaire est l’une des cinq causes les plus fréquentes de décès par cancer chez les femmes dans le monde développé. Environ 90% des cancers de l’ovaire proviennent de l’épithélium que l’on nomme cancer de l’ovaire épithélial (EOC). Le EOC est un cancer hormono-dépendant et les stéroïdes sexuels jouent un rôle crucial en favoriant la prolifération et de la survie des cellules. Les 17β-hydroxystéroïdes déshydrogénases (17β-HSDs) jouent un rôle important pour le contrôle de la concentration intracellulaire de tous les stéroïdes sexuels actifs. Le mécanisme qui reculent le fonctionnent et l’expression des 17β-HSDs dans le EOC sont très peu compris. L’inhibition de certains 17β-HSDs pourrait être un traitement de l’EOC et ette approche thérapeutique doit être étudiée. Les résultats de notre étude ont démontré que les 17β- HSD types 1, 5 et 7 sont tous exprimés dans les cellules OOC-3, mais que la type 1 est la plus abondante. L’expression des 17β-HSD types 1 et 7 dans les tumeurs ovariennes épithéliales que dans les ovaires normaux (type 1, 2.2 fois; type 7, 1.9 fois). Mais l’expression de la 17β-HSD 5 est significativement plus faible dans les tumeurs, suite au développement de l’EOC (-5.217 fois). De plus, la prolifération cellulaire a diminué à la suite du knockdown la 17β-HSD type 1 ou type 7 par des siRNAs spécifiques dans les cellules OVCAR-3, mais, le knockdown de la type 5 a un effet contraire. Nous suggérons que la 17β-HSD 5 peut être impliquée dans une signalisation d’hormones stéroïdiennes pour le développement du cancer de l’ovaire épithélial. Les 17β-HSD 1 et 7 pourraient être des biomarqueurs importants pour l’EOC diagnostiqué tôt et ils peuvent également être de nouvelles cibles pour le traitement de l’EOC.
Ovarian cancer is one of the top five commonest causes of female cancer death in the developed world. About 90% of ovarian cancer have epithelial origins. Epithelial ovarian cancer (EOC) is a hormone-dependent cancer, in which the sex steroids play a crucial role in maintaining the cell proliferation and survival. The 17β-hydroxysteroid dehydrogenases (17β-HSDs) are important in the control of intracellular concentration of all active sex steroids. The function and expression of 17β-HSDs in EOC is not fully understood. Whether or not 17β-HSDs could be a therapeutic approach for the EOC treatment needs to be studied. Our results showed that 17β-HSD types 1, 5 and 7 are all expressed in EOC cells OVCAR-3 and type 1 is the highest one. The expression of 17β-HSD types 1 and 7 is higher in epithelial ovarian tumor tissues than in normal ovaries (type1, 2.2-fold; type7, 1.9-fold), but the expression of 17β-HSD type 5 is significantly lower in the tumor, following the EOC development (-5.2-fold). We found that cell proliferation was decreased after 17β-HSD type 1 or 7 knockdown by specific siRNAs in OVCAR-3 cells. While knocking down type 5 has the opposite effect. We suggest that 17β- HSD type 5 may be involved in steroid hormone signaling in EOC development. Moreover, 17β-HSD types 1 and 7 could be important biomarkers for early diagnosed EOC and novel targets for EOC treatment.
APA, Harvard, Vancouver, ISO, and other styles
6

Xu, Dan (Ph D). "Role of 17β-hydroxysteroid dehydrogenase type 5 in breast cancer studied by intracrinology." Doctoral thesis, Université Laval, 2015. http://hdl.handle.net/20.500.11794/27239.

Full text
Abstract:
Dans cette thèse, je présente une étude (1) du rôle de la 17β-HSD5 dans la modulation des taux d'hormones et dans la prolifération, et l'impact de l'expression de la 17β-HSD5 sur d’autres protéines de BC cellules; (2) une étude comparative sur trois enzymes (17β-HSD1, 17β-HSD7 et 3α-HSD3) avec la provision de DHEA et ses substrats directes soit l’E1 ou la DHT. Les principaux résultats obtenus dans cette étude sont les suivants: (1) en utilisant l'ARN d’interférence de la 17β-HSD5, des immunodosages enzymatiques et des tests de prolifération de cellules démontrent que l'expression de la 17β-HSD5 est positivement corrélée à un niveau de T et de DHT dans les BCC, mais négativement corrélée pour l’E2 et la prolifération des cellules de BC (2) les analyses quantitatives de PCR en temps réel et de Western blot ont démontré que l’inhibition de l’expression de la 17β-HSD5 régule à la hausse l'expression de l'aromatase dans les cellules MCF-7. (3) L’analyse d’ELISA de la prostaglandine E2 a vérifié que l'expression accrue de l'aromatase a été modulée par des niveaux élevés de PGE2 après l’inactivation de l’expression du gène de la 17β-HSD5. (4) Le test de cicatrisation a montré que l’inactivation de l’expression du gène de la 17β-HSD5 favorise l’augmentation de la migration cellulaire. (5) L'expression du gène 17β-HSD5 dans des échantillons cliniques, à partir de l'analyse de base de données ONCOMINE, a montré que sa plus faible expression a été corrélée avec le statut de l’HER-2 et de la métastase de la tumeur. (6) Les données protéomiques révèlent également que des protéines impliquées dans les voies métaboliques sont fortement exprimées dans les cellules MCF-7 après l’inactivation de l’expression du gène de la 17β-HSD5. (7) L’étude n'a démontré aucune différence dans la fonction biologique de la 17β-HSD1 et de la 17β-HSD7 lorsqu'elles sont cultivées avec différentes stéroïdes: tel que les niveaux de stéroides, la prolifération cellulaire et les protéines régulées. (8) Toutefois, la supplémentation du milieu de culture se révèle avoir un impact marqué sur l'étude de la 3α-HSD3. (9). Nous avons proposé que l'utilisation de la DHEA comme source d'hormone puisse entraîner une meilleure imitation des conditions physiologiques post-ménopausales en culture cellulaire selon l’intracrinologie.
Human 17β-hydroxysteroid dehydrogenase type 5 (17β-HSD5) mainly synthesizes the activate androgen testosterone (T) from △4-androstenedione (4-dione), then 4-dione and T aromatazion to estrone (E1) and estradiol (E2) by the action of aromatase. 17β-HSD1 and 7 catalyze the formation of E2 from E1 and inactivate androgen dihydrotestosterone (DHT). In this thesis, I present the study of (1) the roles of 17β-HSD5 in the modulation of hormone levels and in the proliferation. and the proteomic study of the impact of the 17β-HSD5 knock down in BCC; (2) a comparative study of three enzymes (17β-HSD1，7 and 3α-HSD3) with the provision of DHEA and the direct substrates, E1 or DHT. The main results obtained in this study are as follow: (1) Using RNA interference of 17β-HSD5, enzyme immunoassays, and cell proliferation assays demonstrate that 17β-HSD5 expression is positively correlated with T and DHT levels in BCC, but negatively correlated with E2 levels, and BCC proliferation. (2) Quantitative real-time PCR analyzes and western blot showed that 17β-HSD5 knockdown up-regulates aromatase expression in MCF-7 cells. (3) Prostaglandin E2 ELISA assay verified that aromatase expression increase was modulated by elevated PGE2 levels after 17β-HSD5 knockdown. (4) Wound healing assay showed that with the knockdown of 17β-HSD5 expression, cell migration increased. (5)17β-HSD5 gene expression in clinical samples from ONCOMINE analysis showed its lower expression was correlated with HER-2 status and tumor metastasis. (6) The proteomic data also reveal that proteins involved in metabolic pathways are highly expressed in 17β-HSD5 knockdown MCF-7 cells. (7) Cell biology study showed no difference in biological function for 17β-HSD1 and 17β-HSD7 when cultured with different steroids cell proliferation and estradiol levels decreased, whereas DHT accumulated; cyclin D1, PCNA, and pS2 were down-regulated after knocking down these two enzymes. (8) The culture medium supplementation was found to have a marked impact on the study of 3α-HSD3. (9) We first proposed that using DHEA as hormone source may result in better mimicking of the physiological conditions of post-menopausal in cell culture according intracrinology.
APA, Harvard, Vancouver, ISO, and other styles
7

Shafqat, Naeem. "Substrate specificities and functional properties of human short-chain dehydrogenases/reductases /." Stockholm, 2004. http://diss.kib.ki.se/2004/91-7349-829-7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Nokelainen, P. (Pasi). "Biosynthesis of estradiol:cloning and characterization of rodent 17β-hydroxysteroid dehydrogenase/17-ketosteroid reductase types 1 and 7." Doctoral thesis, University of Oulu, 2000. http://urn.fi/urn:isbn:9514257510.

Full text
Abstract:
Abstract 17β-Hydroxysteroid dehydrogenases (17HSDs)/17-ketosteroid reductases (17KSRs) modulate the biological activity of certain estrogens and androgens by catalyzing dehydrogenase and reductase reactions between 17β-hydroxy and 17-ketosteroids. In the present study, cDNAs encoding mouse and rat 17HSD/KSR1 were cloned in order to study the role of rodent type 1 enzyme in ovarian estradiol (E2) biosynthesis and its enzymatic characteristics. Both rat and mouse 17HSD/KSR1 were expressed in granulosa cells of developing follicles, where diethylstilbestrol and follicle-stimulating hormone stimulated follicular maturation and up-regulated the expression of 17HSD/KSR1, whereas human chorionic gonadotropin caused luteinization of follicles and down-regulation of the enzyme. In line with this, the rodent type 1 enzymes are not expressed in the corpus luteum (CL). Mouse 17HSD/KSR1 showed substrate specificity different from that of the human counterpart. The mouse type 1 enzyme catalyzed the reaction from androstenedione to testosterone at least as efficiently as estrone (E1) to E2, while human 17HSD/KSR1 clearly preferred the E1 to E2 reaction. A mouse mammary epithelial cell line was found to possess strong estrogenic 17KSR activity. A novel type of 17HSD/KSR responsible for this activity was expression-cloned on the basis of its ability to convert E1 to E2 and it was chronologically named 17HSD/KSR7. Interestingly, it showed 89 % identity with a rat protein called prolactin receptor-associated protein (PRAP), which is expressed in the CL. Enzymatic characterization showed that both mouse 17HSD/KSR7 and PRAP efficiently catalyzed the reaction from E1 to E2. The mouse type 7 enzyme was most abundantly expressed in the ovary and placenta. Similar primary structure, enzymatic characteristics, and tissue distribution of mouse 17HSD/KSR7 and PRAP suggest that PRAP is rat 17HSD/KSR7. Further studies showed that in rat ovaries 17HSD/KSR7 is primarily expressed in the middle and second half of pregnancy, in parallel with E2 secretion from the CL. Using in situ hybridization, cell-specific expression of 17HSD/KSR7 was studied in the mouse ovary, uterus and placenta. In the mouse ovary, the enzyme was expressed exclusively in the CL. In the uterus on day 5 post coitum (p.c.), the type 7 enzyme was expressed in the decidua, mostly in the inner zone of antimesometrial decidua. Between day 8 and 9 p.c. the enzyme was abundant in decidua capsularis of the developing placenta, after which expression moved to the basal zone. On days 12 and 14 p.c., mouse type 7 enzyme was abundantly expressed in the spongiotrophoblasts, where expression decreased towards parturition. Altogether, rodent 17HSD/KSR7 is a new 17HSD/KSR which is involved in the biosynthesis of E2 in the ovaries. In addition, E2 produced locally in the decidua and placenta by the type 7 enzyme may have a role in decidualization and/or implantation and placentation.
APA, Harvard, Vancouver, ISO, and other styles
9

Gunnarsson, Cecilia. "Steroid converting enzymes in breast cancer /." Linköping : Univ, 2005. http://www.bibl.liu.se/liupubl/disp/disp2005/med908s.pdf.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Olusanjo, Moniola Sarah. "Synthesis and biochemical evaluation of potential steroidal and non-steroidal inhibitors of 17[beta]-hydroxysteroid dehydrogenase (17[beta]-HSD) in the treatment of hormone-dependent cancers." Thesis, Kingston University, 2008. http://eprints.kingston.ac.uk/22361/.

Full text
Abstract:
Enzymes such as aromatase, 17[beta]-hydroxysteroid dehydrogenase [types 1 (17[beta]-HSD1) and 3 (17[beta]-HSD3)] and estrone sulfatase (ES) are all involved in the biosynthesis of steroids via the steroidal cascade. The inhibition of these enzymes may lead to a reduction in the levels of steroids present, thereby leading to a decrease in the stimulation of hormone-dependent tissues, in particular, hormone-dependent breast and prostate cancers. This approach has proved to be successful in postmenopausal women where the use of aromatase inhibitors has led to the decrease in tumour yield and has thus led to the treatment of the disease. Within the current study, the synthesis and biochemical evaluation of a number of compounds of varying structural features has been undertaken, in particular, the synthesis of sulfonate derivatives of 4-hydroxyphenyl ketone - the parent compound having already been shown to be a potent inhibitor of 17[beta]-HSD3 (with good specificity towards 17[beta]-HSD3) and the synthesis of a range of alkyl and cycloalkyl esters of steroids [in particular, testosterone (T) dehydroepiandrosterone (DHEA) and estrone (E10] as probes of the active sites of the HSD family of enzymes. The results show that the sulfonate (methanesulfonate and trifluromethanesulfonate) derivatives of 4-hydroxyphenyl ketone-based compounds were found to possess weak inhibitory activity against all three HSD enzymes considered (namely, 17[beta]-HSD1, 17[beta]-HSD3 and 3[beta]-HSD) in comparison to the parent 4-hydroxyphenyl ketone-based compounds. For example, within the methanesulfonate derivatives, methane sulfonic acid (4-cyclohexane carbonyl)-phenyl ester (164) was found to be the most potent inhibitor against 17[beta]-HSD3, however, it possessed ~30% inhibitory against this enzyme at an inhibitor concentration of 100[mu]M. Against 17[beta]-HSD1, the most potent compound within the same range was also compound 164 which pssessed ~45% inhibitory activity under similar conditions. Within the trifluromethane sulfonate derivatives, the most potent compounds proved to be extremely weak inhibitors of 17[beta]-HSD3, however, against 17[beta]-HSD1, the most potent compound was trifluromethane sulfonic acid 4-benzoyl-phenyl ester (180) which possess 43% inhibitory activity. The molecular modeling of these compounds within representations of the active sites of 17[beta]-HSD1 and 17[beta]-HSD3 shows that the lack of inhibitory activity is due to steric hindrance, in particular, the sulfonate moeity undergoes steric hindrance with groups at the active site which is close to the C(17) area of the natural substrate. The synthesis of the esters of T, DHEA and E1 and the subsequent biochemical evaluation of these compounds resulted in an interesting structure-activity relationship. In general, the compounds based on DHEA were found to be potent inhibitors of 17[beta]-HSD3 with weak inhibitory activity against 17[beta]-HSD1 and 3[beta]-HSD. For example, DHEA acetate (196) was found to possess an IC[sub]50 value of 0.74[mu]M in comparison to the most potent standard, namely 1-(4hydroxy-phenyl)-nonan-1-one (139) which was found to possess an IC[sub]50 value of 12.32[mu]M - this compound was found to possess good selectivity as it possessed ~40% and ~25% inhibitory activity against 17[beta]-HSD1 and 3[beta]-HSD respectively at an inhibitor concentration of 100[mu]M. The esters of E1 and T proved to be weaker inhibitors in comparison to the esters based on DHEA, however, the E1-based esters also showed some selectivity towards 17[beta]-HSD3. For example, E1 hexanoate (216) possessed an IC[sub]50 value of 37.28[mu]M and possessed 45% and 35% inhibitory activity against 17[beta]-HSD1 and 3[beta]-HSD respectively at an inhibitor concentration of 100[mu]M. The modelling of these compounds (using representations of the active sites of 17[beta]-HSD1 and 17[beta]-HSD3) showed that the lack of inhibitory activity was due to steric interactions between the inhibitors and groups within the active site. As such, these compounds proved to be extremely useful probes of the active sites of 17[beta]-HSD1 and 17[beta]-HSD3 and have further enhanced the models used in the design of these compounds.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "(or 17)-hydroxysteroid déhydrogénase"

1

Schomburg, Dietmar, and Dörte Stephan. "3(or 17)beta-Hydroxysteroid dehydrogenase." In Enzyme Handbook 9, 283–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-85200-8_51.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Schomburg, Dietmar, and Dörte Stephan. "3(or 17)alpha-Hydroxysteroid dehydrogenase." In Enzyme Handbook 10, 210–12. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-57756-7_57.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Richardson, Annely, Gerard T. Berry, Cheryl Garganta, and Mary-Alice Abbott. "Hydroxysteroid 17-Beta Dehydrogenase Type 10 Disease in Siblings." In JIMD Reports, 25–32. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/8904_2016_547.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Williamson, D. G. "The Biochemistry of the 17-Hydroxysteroid Dehydrogenases." In Steroid Biochemistry, 83–110. CRC Press, 2018. http://dx.doi.org/10.1201/9781351076906-3.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "(or 17)-hydroxysteroid déhydrogénase"

1

Hilborn, Erik, Olle Stal, and Agneta Jansson. "Abstract A52: The microRNA control of 17β-hydroxysteroid dehydrogenase type 1 and 2 in breast cancer." In Abstracts: AACR Special Conference: Advances in Breast Cancer; October 17-20, 2015; Bellevue, WA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1557-3125.advbc15-a52.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Xanthoulea, Sofia, Gonda Konings, Niina Saarinen, Bert Delvoux, Loes Kooreman, Pasi Koskimies, Merja Häkkinen, et al. "Abstract 2931: Pharmacological inhibition of 17β-hydroxysteroid dehydrogenase impairs endometrial cancer growth in an orthotopic xenograft mouse model." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-2931.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Collin, Lindsay Jane, Anders Kjærsgaard, Thomas P. Ahern, Michael Goodman, Lauren E. McCullough, Lance A. Waller, Kristina B. Christensen, et al. "Abstract 757: 17β-hydroxysteroid dehydrogenases 1 and 2: potential markers for breast cancer recurrence and tamoxifen resistance among premenopausal women diagnosed with breast cancer in Denmark." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-757.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic '(or 17)-hydroxysteroid déhydrogénase' for particular source types:
Journal articles Dissertations / Theses
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography