Relevant bibliographies by topics / P450c17

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

Academic literature on the topic 'P450c17'

Author: Grafiati
Published: 4 June 2021
Last updated: 27 April 2022

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Journal articles on the topic "P450c17"

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Miller, Walter L. "Minireview: Regulation of Steroidogenesis by Electron Transfer." Endocrinology 146, no. 6 (2005): 2544–50. http://dx.doi.org/10.1210/en.2005-0096.

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Abstract Cytochrome P450 enzymes catalyze the degradation of drugs and xenobiotics, but also catalyze a wide variety of biosynthetic processes, including most steps in steroidogenesis. The catalytic rate of a P450 enzyme is determined in large part by the rate of electron transfer from its redox partners. Type I P450 enzymes, found in mitochondria, receive electrons from reduced nicotinamide adenine dinucleotide (NADPH) via the intermediacy of two proteins—ferredoxin reductase (a flavoprotein) and ferredoxin (an iron/sulfur protein). Type I P450 enzymes include the cholesterol side-chain cleav
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Yoshimoto, Francis K., Hwei-Ming Peng, Haoming Zhang, Sean M. Anderson, and Richard J. Auchus. "Epoxidation Activities of Human Cytochromes P450c17 and P450c21." Biochemistry 53, no. 48 (2014): 7531–40. http://dx.doi.org/10.1021/bi5011865.

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Cole, Beth, Krista Hensinger, Gustavo A. R. Maciel, R. Jeffery Chang, and Gregory F. Erickson. "Human Fetal Ovary Development Involves the Spatiotemporal Expression of P450c17 Protein." Journal of Clinical Endocrinology & Metabolism 91, no. 9 (2006): 3654–61. http://dx.doi.org/10.1210/jc.2006-0641.

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Abstract Objective: The purpose of this research was to characterize the spatiotemporal expression of P450c17 in the human fetal ovary. Design: P450c17 protein was visualized in sections of control and anencephalic ovaries using immunohistochemistry. Subjects: Subjects included control (nonanencephalic) and anencephalic human fetal ovaries during the second and third trimesters. Results: In second-trimester control ovaries, P450c17 was highly expressed in primary interstitial cells (PIC) located between the ovigerous cords near the cortical-medullary border where meiosis and primordial follicl
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LeHoux, Jean-Guy, Mario Cloutier, Normand Brière, and Denis Martel. "Immunolocalization and Biochemical Determination of Cytochrome P450C17 in Adrenals of Hamsters Treated with ACTH." Journal of Histochemistry & Cytochemistry 45, no. 10 (1997): 1409–16. http://dx.doi.org/10.1177/002215549704501009.

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We used an anti-rat adrenal cytochrome P450C17 (P450C17) antibody to perform immunofluorescence and also immunogold electron microscopic studies to determine the zonal and intracellular distribution of P450C17 in hamster adrenals. Because P450C17 activity is regulated mainly by adrenocorticotropin (ACTH), its zonal and intracellular localization was also analyzed after ACTH treatment. The effect of ACTH treatment on protein concentration was also investigated by Western blotting analysis. By immunofluorescence, we found P450C17 to be confined to the zona fasciculata (ZF) in the hamster, in con
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Tee, Meng Kian, Qing Dong, and Walter L. Miller. "Pathways Leading to Phosphorylation of P450c17 and to the Posttranslational Regulation of Androgen Biosynthesis." Endocrinology 149, no. 5 (2008): 2667–77. http://dx.doi.org/10.1210/en.2007-1527.

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Cytochrome P450c17 (P450c17) is the single enzyme that catalyzes steroid 17α-hydroxylase and 17,20 lyase activities and hence is the crucial decision-making step that determines the class of steroid made in a steroidogenic cell. Although both activities are catalyzed on a single active site, the ratio of these activities is regulated by posttranslational events. Serine phosphorylation of P450c17 increases 17,20 lyase activity by increasing the enzyme’s affinity for its redox partner, P450 oxidoreductase. We searched for the relevant kinase(s) that phosphorylates P450c17 by microarray studies a
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Yamamoto, T., B. M. Chapman, D. C. Johnson, C. R. Givens, S. H. Mellon та M. J. Soares. "Cytochrome P450 17α-hydroxylase gene expression in differentiating rat trophoblast cells". Journal of Endocrinology 150, № 1 (1996): 161–68. http://dx.doi.org/10.1677/joe.0.1500161.

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Abstract Trophoblast giant cells of the rat placenta express cytochrome P450 17α-hydroxylase (P450c17) and synthesize androgens. The purpose of this study was to investigate androgen production and expression of P450c17 in the Rcho-1 trophoblast cell line. These cells are capable of differentiating along the trophoblast giant cell lineage. Androstenedione production increased approximately 70-fold as Rcho-1 trophoblast cells progressed from the proliferation to the differentiation state. P450c17 enzyme activity and mRNA also showed significant increases associated with trophoblast giant cell d
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Gray, S. A., M. A. Mannan та P. J. O'Shaughnessy. "Development of cytochrome P450 17α-hydroxylase (P450c17) mRNA and enzyme activity in neonatal ovaries of normal and hypogonadal (hpg) mice". Journal of Molecular Endocrinology 17, № 1 (1996): 55–60. http://dx.doi.org/10.1677/jme.0.0170055.

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ABSTRACT The cytochrome P450 enzyme 17α-hydroxylase (P450c17) is required for androgen synthesis and therefore regulates substrate supply for aromatization. In this study, changes in P450c17 activity and mRNA levels were measured during ovarian development in the normal mouse and in the hypogonadal (hpg) mouse which lacks circulating gonadotrophins. At birth, low levels of P450c17 activity and mRNA were detectable in normal ovaries. This basal level of expression did not change until after day 10 at which time both enzyme activity and mRNA levels increased by six- to eightfold. In the hpg mous
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Kempná, Petra, Andrea Hirsch, Gaby Hofer, Primus E. Mullis, and Christa E. Flück. "Impact of Differential P450c17 Phosphorylation by cAMP Stimulation and by Starvation Conditions on Enzyme Activities and Androgen Production in NCI-H295R Cells." Endocrinology 151, no. 8 (2010): 3686–96. http://dx.doi.org/10.1210/en.2010-0093.

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CYP17A1 plays a pivotal role in the biosynthesis of androgens in the adrenals and the gonads. Although this enzyme catalyzes two different reactions on one single active site, its specific activities are regulated independently. Although the 17α-hydroxylase activity is rather constant and regulated by gene expression, the 17,20-lyase activity varies significantly with the amount of cofactors or by protein phosphorylation. cAMP increases CYP17A1 expression, P450c17 phosphorylation, and androgen production. However, the exact mechanism(s) and the specific regulators of CYP17A1 remain unknown. Th
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Morán, F. M., C. A. VandeVoort, J. W. Overstreet, B. L. Lasley та A. J. Conley. "Molecular Target of Endocrine Disruption in Human Luteinizing Granulosa Cells by 2,3,7,8-Tetrachlorodibenzo-p-Dioxin: Inhibition of Estradiol Secretion Due to Decreased 17α-Hydroxylase/17,20-Lyase Cytochrome P450 Expression". Endocrinology 144, № 2 (2003): 467–73. http://dx.doi.org/10.1210/en.2002-220813.

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Estradiol (E2) production by human luteinized granulosa cells (hLGC) is inhibited by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). The molecular target of TCDD toxicity has not been identified. The decrease in E2 is ameliorated by androgen substrate addition and is not associated with changes in aromatase cytochrome P450 (P450arom) activity or protein expression. An antihuman 17α-hydroxylase/17,20-lyase cytochrome P450 (P450c17) antisera and a direct radiometric assay of 17,20-lyase activity were used to test the hypothesis that TCDD targets P450c17, thereby decreasing substrate availability for
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Bair, Susanna R., and Synthia H. Mellon. "Deletion of the Mouse P450c17 Gene Causes Early Embryonic Lethality." Molecular and Cellular Biology 24, no. 12 (2004): 5383–90. http://dx.doi.org/10.1128/mcb.24.12.5383-5390.2004.

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ABSTRACT Dehydroepiandrosterone (DHEA), a 19-carbon precursor of sex steroids, is abundantly produced in the human but not the mouse adrenal. However, mice produce DHEA and DHEA-sulfate (DHEAS) in the fetal brain. DHEA stimulates axonal growth from specific populations of mouse neocortical neurons in vitro, while DHEAS stimulates dendritic growth from those cells. The synthesis of DHEA and sex steroids, but not mouse glucocorticoids and mineralocorticoids, requires P450c17, which catalyzes both 17α-hydroxylase and 17,20-lyase activities. We hypothesized that P450c17-knockout mice would have di
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Dissertations / Theses on the topic "P450c17"

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Viana, Diego Carvalho. "Sazonalidade reprodutiva em machos de tartaruga (Kinosternon scorpioides) de vida livre no Nordeste brasileiro evidenciado por imunolocalização de enzimas esteroidogênicas no testículo e epidídimo." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/10/10132/tde-11052016-170811/.

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No Estado do Maranhão, na região da Baixada Maranhense, presenta na fauna silvestre o réptil Kinosternon scorpioides, um quelônio de água doce popularmente conhecido como jurará e que possui valor social, econômico e ambiental para os ribeirinhos da cidade de São Bento. Este estudo contempla suas características biológicas reprodutivas baseadas em seu ambiente natural, com o intuito de permitir a preservação e o estabelecimento de planos de manejo reprodutivo e de uso sustentável da espécie. Recentemente poucos estudos em todo o mundo tratam sobre os aspectos do ciclo reprodutivo de tartarugas
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Courtemanche, Jean. "Caractérisation des cytochromes P450c11 et P450c18 chez le hamster." Mémoire, Université de Sherbrooke, 1995. http://hdl.handle.net/11143/12059.

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Lors de l'étude du P450c18 de hamsters sous-diète faible en sodium, une analyse par buvardage de type Northern, à partir de surrénale, a permis de révéler trois bandes à 2 kb, 2.3 kb et 3.4 kb respectivement à l'aide d'une sonde spécifique au P450c18. Ces trois formes d'ADNc ont été recherchées dans une banque d'ADNc de surrénale de hamster. Deux clones différents ont été isolés codant pour le P450c18 (clone 18 et clone 5) et deux codant pour le P450c11 (clone 43 et clone ?1). La comparaison de la région codante du P450c11 clone ?1 avec le P450c18 clone 18 montre une homologie de 90% entre les
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Gentil, Michaela [Verfasser]. "Wiedereinsetzen der Steroidbiosynthese nach Downregulation der Hodenfunktion beim Rüden : Expression von StAR-Protein, P450scc und P450c17 / Michaela Gentil." Gießen : Universitätsbibliothek, 2012. http://d-nb.info/1064760856/34.

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Carvalho, Luciane Carneiro de. "Avaliação clínica, laboratorial, genética e ovariana de pacientes 46,XX com deficiência da atividade do P450c17: uma revisão." Universidade de São Paulo, 2015. http://www.teses.usp.br/teses/disponiveis/5/5135/tde-04082015-112303/.

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A hiperplasia adrenal congênita (HAC) por deficiência no P450c17 é uma doença de herança autossômica recessiva raramente relatada em pacientes 46, XX. Nosso objetivo foi o de caracterizar o fenótipo e genótipo desta doença rara revendo os dados clínicos, laboratoriais, genéticos, e da função ovariana de pacientes 46,XX de uma coorte brasileira avaliada no HCFMUSP e dos casos já publicados na literatura. Foram avaliados retrospectivamente os dados de 18 pacientes brasileiras pertencentes a 12 famílias avaliadas no HCFMUSP, e revisados os dados de literatura de pacientes de 10 coortes com defici
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Picard, Mireille. "Le clonage et l'expression du cytochrome P450c17 humain dans le but d'étudier le rôle de la phosphorylation dans son activation." Sherbrooke : Université de Sherbrooke, 2003.

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Picard, Mireille. "Le clonage et l'expression du cytochrome P450c17 humain dans le but d'étudier le rôle de la phosphorylation dans son activation." Mémoire, Université de Sherbrooke, 2003. http://savoirs.usherbrooke.ca/handle/11143/3339.

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Le but de ce projet est d'étudier la phosphorylation sur le P450c17 humain. Un clone a donc été construit à partir de l'ARN extrait de glandes surrénales foetales et de cellules H295R. Une RT-PCR a été réalisée afin d'amplifier la séquence codante du P450c17, soit 1725 pb. Une fois l'ADNc humain cloné, séquencé et corrigé, son expression a été étudiée dans les cellules COS-1 (ces cellules ont été choisies car elles n'expriment pas le P450c17) à l'aide du vecteur pcDNA3.1/V5-His[indice supérieur Copyright]TOPO[indice supérieur Marque déposée]. Des tests d'optimisation de la transfection ont mon
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Béland, Fanny. "Impacts moléculaires d’un excès d’acides gras sur l’androgenèse des cellules surrénaliennes." Mémoire, Université de Sherbrooke, 2016. http://hdl.handle.net/11143/8848.

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Le syndrome des ovaires polykystiques (SOPK) touche entre 5 à 10 % des femmes en âge de procréer et est associé à de nombreuses complications. Ce désordre endocrinien est caractérisé par des niveaux circulants élevés d’androgènes, dont la production est principalement modulée par la P450c17 et son cofacteur, soit la P450oxydoréductase (POR). Plusieurs études démontrent que l’hyperandrogénie présente chez les femmes SOPK pourrait être causée par la formation de phénomènes toxiques survenant à la suite de l’exposition des tissus non adipeux à un excès d’acides gras non estérifiés (AGNE), appelé
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Santos, Amilton Cesar dos. "Expressão das enzimas: citocromo P450 aromatase, NADPH-citocromo P450 redutase e citocromo P450c17 (17-α-hidroxilase/17, 20-liase) na vagina de fêmeas de preás (Galea spixii, Wagler, 1831)." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/10/10132/tde-24092013-161549/.

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Para a metabolização de hormônios esteroides sexuais é essencial a participação de enzimas esteroidogênicas. A enzima citocromo P450c17 é responsável pela produção de andrógenos e a enzima citocromo P450 aromatase é responsável pela produção de estrógenos, sendo que, ambas as enzimas necessitam formar um complexo com uma enzima parceira, denominada NADPH citocromo P450 redutase, para realizar a metabolização destes hormônios essenciais para a diferenciação sexual. Objetivou-se imunolocalisar as três enzimas acima citadas no tecido vaginal de fêmeas de roedores Galea spixii. Para tanto, o exper
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Mathieu, Axel Patrick. "Modélisation moléculaire de la protéine "Steroidogenic Acute Regulatory" (StAR) et du cytochrome P450 17[alpha]-hydroxylase/17,20-Lyase (P450c17) une approche moléculaire pour comprendre les mécanismes de la stéroïdogenèse." Thèse, Université de Sherbrooke, 2002. http://savoirs.usherbrooke.ca/handle/11143/4149.

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L'hyperplasie lipoïde surrénalienne congénitale a été attribuée à la protéine"steroidogenic acute regulatory" (StAR) portant des mutations qui inhibent sa fonction primaire. Nous avons donc entrepris des démarches pour clarifier le mécanisme d'action de la StAR en utilisant des techniques à la fine pointe de la technologie, telle que la modélisation moléculaire. Nous avons développé un modèle StAR basé sur les données cristallographiques de la protéine MLN64 humaine. Nous démontrons par notre modèle que StAR possède une cavité hydrophobe et non un tunnel tel qu'observé pour la molécule MLN64.
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Arroyo, Maria Angélica Machado. "Ultraestrutura e expressão das enzimas: citocromo P450 aromatase e citocromo P450c17 (17-α-hidroxilase/17,20-liase) nas diferentes fases do desenvolvimento da via espermática e espermatogênese em cutia (Dasyprocta sp.) criada em cativeiro." Universidade de São Paulo, 2013. http://www.teses.usp.br/teses/disponiveis/10/10132/tde-03122013-081304/.

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Espécies silvestres com grande potencial zootécnico devem ser exploradas de forma racional a fim de se evitar a extinção das mesmas. Assim se dá a importância de pesquisas voltadas à reprodução daquelas criadas em cativeiro, como a cutia (Dasyprocta sp.). Este animal é um mamífero e roedor vivente, em sua maioria, na Caatinga brasileira. A ultraestrutura é a base para determinar os estágios celulares e, assim, facilitar as comparações dos processos entre cutias e roedores silvestres ou outros mamíferos. As enzimas P450 aromatase e P450c17 são responsáveis pela regulagem da produção de estrógen
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Books on the topic "P450c17"

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Esler, Dan. Quantifying temporal variation in harlequin duck cytochrome P4501A induction. EVOS Trustee Council, 2008.

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Esler, Dan. Quantifying temporal variation in harlequin duck cytochrome P4501A induction. EVOS Trustee Council, 2008.

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Trudeau, S. A method to determine cytochrome P4501A activity in wildlife microsomes. Canadian Wildlife Service, 2001.

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Book chapters on the topic "P450c17"

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Miller, Walter L. "P450c17—The Qualitative Regulator of Steroidogenesis." In Molecular and Cellular Pediatric Endocrinology. Humana Press, 1999. http://dx.doi.org/10.1007/978-1-59259-697-3_8.

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Miller, W. L., and R. J. Auchus. "Biochemistry and Genetics of Human P450c17." In Adrenal Disease in Childhood. KARGER, 2000. http://dx.doi.org/10.1159/000060844.

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Kühn-Velten, W. N. "Cytochrome P450c17: Regulation of Gene Expression and Enzyme Function at the Bifurcation in Steroid Hormone Synthesis." In Cytochrome P450. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77763-9_43.

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Stok, Jeanette E., Kate E. Slessor, Anthony J. Farlow, David B. Hawkes, and James J. De Voss. "Cytochrome P450cin (CYP176A1)." In Advances in Experimental Medicine and Biology. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16009-2_12.

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Wong, Luet-Lok, Andrew C. G. Westlake, and Darren P. Nickerson. "Protein engineering of cytochrome P450cam." In Metal Sites in Proteins and Models. Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/3-540-62870-3_6.

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Mueller, Ernest J., Paul J. Loida, and Stephen G. Sligar. "Twenty-five Years of P450cam Research." In Cytochrome P450. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_3.

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Goodin, David B., Shih-Wei Chuo, and Shu-Hao Liou. "CHAPTER 13. Conformational Changes in Cytochrome P450cam and the Effector Role of Putidaredoxin." In Dioxygen-dependent Heme Enzymes. Royal Society of Chemistry, 2018. http://dx.doi.org/10.1039/9781788012911-00292.

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Davydov, D. R., G. Hui Bon Hoa, and J. A. Peterson. "The Dynamics of Protein-Bound Water in the Heme Domain of P450BM3 as Compared with P450cam and P450 2B4." In Advances in High Pressure Bioscience and Biotechnology. Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-60196-5_44.

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Berbner, Th, and Th Braunbeck. "Änderungen des Cytochrom P4501A-Gehalts in isolierten Hepatocyten aus der Regenbogenforelle (Oncorhynchus mykiss) nach Belastung mit verschiedenen Modellinduktoren." In Ersatz- und Ergänzungsmethoden zu Tierversuchen. Springer Vienna, 2000. http://dx.doi.org/10.1007/978-3-7091-6760-1_61.

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Stagg, R. M., P. A. Gillibrand, A. M. McIntosh, and W. A. Turrell. "The Effects of Produced Water on Hydrocarbon Levels and on P4501A Monooxygenase Activity in Fish Larvae in the Northern North Sea." In Produced Water 2. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0379-4_18.

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Conference papers on the topic "P450c17"

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Tamae, Daniel, Elahe Mostaghel, Bruce Montgomery, et al. "Abstract 3450: Resistance to P450c17 inhibitors in castration-resistant prostate cancer may result from the DHEA-S depot that remains and can be used by AKR1C3 for intratumoral androgen biosynthesis." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-3450.

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Ramos, Sashary, and Megan Thielges. "SITE-SPECIFIC CHARACTERIZATION OF P450CAM SUBSTRATE RECOGNITION VIA 2D IR SPECTROSCOPY." In 2020 International Symposium on Molecular Spectroscopy. University of Illinois at Urbana-Champaign, 2020. http://dx.doi.org/10.15278/isms.2020.fb08.

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Ramos, Sashary, Megan Thielges, and Edward Basom. "CONFORMATIONAL DYNAMICS OF THE CYTOCHROME P450CAM-PUTIDAREDOXIN COMPLEX PROBED VIA 2D IR SPECTROSCOPY." In 73rd International Symposium on Molecular Spectroscopy. University of Illinois at Urbana-Champaign, 2018. http://dx.doi.org/10.15278/isms.2018.td09.

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Ramos, Sashary, Megan Thielges, and Claire Mammoser. "SITE-SPECIFIC CHARACTERIZATION OF P450CAM SUBSTRATE RECOGNITION <i>VIA</i> 2D IR SPECTROSCOPY." In 2021 International Symposium on Molecular Spectroscopy. University of Illinois at Urbana-Champaign, 2021. http://dx.doi.org/10.15278/isms.2021.tc09.

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Moorthy, Bhagavatula, Jiang Weiwu, Lihua Wang, Chun Chu, Sudha R. Kondraganti, and Paramahamsa Maturu. "Abstract 825: Molecular mechanisms of regulation of cytochrome P4501A enzymes by 3-methylcholanthrene (MC) in micein vivo." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-825.

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Sasaki, Issei. "In vivo observations of cytochrome P4501A isozyme reaction in liver of living rats by using fiber-optic sensor." In 13th International Conference on Optical Fiber Sensors. SPIE, 1999. http://dx.doi.org/10.1117/12.2302130.

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