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Longitudinal proneuroactive and neuroactive steroid profiles in medication-free women with, without and at-risk for perinatal depression: A liquid chromatography-tandem mass spectrometry analysis.
Psychoneuroendocrinology
November 2020
Mass Spectrometry Facility, University of Massachusetts Medical School, Shrewsbury, MA, 01545, USA; Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA, 01655, USA. Electronic address:
Background: Neuroactive steroids (NAS) are derivatives of cholesterol or steroidal precursors made in the gonads, adrenal gland, placenta and brain. We characterized longitudinal plasma proneuroactive and NAS in healthy perinatal comparison women (HPCW), women at-risk for perinatal depression (AR-PND), and women with PND with/without comorbid anxiety. We hypothesized that AR-PND women who either did or did not go on to develop PND would have elevated NAS concentrations as compared to HPCW and that NAS would be correlated to depressive and anxiety symptoms.
View Article and Find Full Text PDFP450 Oxidoreductase Deficiency: Loss of Activity Caused by Protein Instability From a Novel L374H Mutation.
J Clin Endocrinol Metab
December 2016
Pediatric Endocrinology, Diabetology, and Metabolism (S.P., C.E.F., A.V.P.), University Children's Hospital, and Department of Clinical Research, University of Bern, CH-3010 Bern, Switzerland; Service d'Endocrinologie Moléculaire et Maladies Rares (F.R.-B., D.M., Y.M.), Centre de Biologie et Pathologie Est, Hospices Civils de Lyon, Université Lyon 1, 69002 Bron-Lyon, France; and Endocrinologie Pédiatrique Département de Pédiatrie Médicale (A.L.-R.), Hôpital de la Mère et de l'Enfant, 87042 Limoges, France.
Context: P450 oxidoreductase (POR) is required for the activities of steroid-metabolizing cytochrome P450 enzymes in the endoplasmic reticulum. POR deficiency (PORD) is a form of congenital adrenal hyperplasia. Objective and Aim: Enzymatic and structural analysis of a novel L374H POR mutation from a patient with 46,XX disorder of sexual development.
View Article and Find Full Text PDFEpoxidation activities of human cytochromes P450c17 and P450c21.
Biochemistry
December 2014
Division of Metabolism, Endocrinology, & Diabetes, Department of Internal Medicine and ‡Department of Pharmacology, University of Michigan, Ann Arbor, Michigan 48109, United States.
Some cytochrome P450 enzymes epoxidize unsaturated substrates, but this activity has not been described for the steroid hydroxylases. Physiologic steroid substrates, however, lack carbon-carbon double bonds in the parts of the pregnane molecules where steroidogenic hydroxylations occur. Limited data on the reactivity of steroidogenic P450s toward olefinic substrates exist, and the study of occult activities toward alternative substrates is a fundamental aspect of the growing field of combinatorial biosynthesis.
View Article and Find Full Text PDFMinor activities and transition state properties of the human steroid hydroxylases cytochromes P450c17 and P450c21, from reactions observed with deuterium-labeled substrates.
Biochemistry
September 2012
Division of Endocrinology & Metabolism, Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
The steroid hydroxylases CYP17A1 (P450c17, 17-hydroxylase/17,20-lyase) and CYP21A2 (P450c21, 21-hydroxylase) catalyze progesterone hydroxylation at one or more sites within a 2 Å radius. We probed their hydrogen atom abstraction mechanisms and regiochemical plasticity with deuterium-labeled substrates: 17-[(2)H]-pregnenolone; 17-[(2)H]-, 16α-[(2)H]-, 21,21,21-[(2)H(3)]-, and 21-[(2)H]-progesterone; and 21,21,21-[(2)H(3)]-17-hydroxyprogesterone. Product distribution and formation rates with recombinant human P450-oxidoreductase and wild-type human CYP17A1 or mutation A105L (reduced progesterone 16α-hydroxylation) and wild-type human CYP21A2 or mutation V359A (substantial progesterone 16α-hydroxylation) were used to calculate intramolecular and intermolecular kinetic isotope effects (KIEs).
View Article and Find Full Text PDFDeletion of P399_E401 in NADPH cytochrome P450 oxidoreductase results in partial mixed oxidase deficiency.
Biochem Biophys Res Commun
September 2011
Pediatric Endocrinology, Diabetology and Metabolism, University Children's Hospital, Bern, Switzerland.
P450 oxidoreductase (POR) is the electron donor for all microsomal P450s including steroidogenic enzymes CYP17A1, CYP19A1 and CYP21A2. We found a novel POR mutation P399_E401del in two unrelated Turkish patients with 46,XX disorder of sexual development. Recombinant POR proteins were produced in yeast and tested for their ability to support steroid metabolizing P450 activities.
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