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Cover

Disorders of the Human Adrenal Cortex

Editor(s): Flück C.E. (Bern) 
Miller W.L. (San Francisco, Calif.) 
Table of Contents
Vol. 13, No. , 2008
Section title: Paper
Flück CE, Miller WL (eds): Disorders of the Human Adrenal Cortex. Endocr Dev. Basel, Karger, 2008, vol 13, pp 1-18
(DOI:10.1159/000134751)

Steroidogenic Enzymes

Miller W.
Division of Endocrinology, Department of Pediatrics, University of California, San Francisco, Calif., USA

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Article / Publication Details

First-Page Preview
Abstract of Paper

Published online: May 20, 2008
Cover Date: 2008

Number of Print Pages: 18
Number of Figures: 0
Number of Tables: 0

ISBN: 978-3-8055-8580-4 (Print)
eISBN: 978-3-8055-8581-1 (Online)

Abstract

The enzymes and pathways of steroidogenesis are familiar to most endocrinologists, but the biochemistry and molecular biology of these processes are still being studied. This chapter outlines current knowledge about each enzyme. The quantitative regulation of steroidogenesis occurs at the first step, the conversion of cholesterol to pregnenolone. Chronic regulation is principally at the level of transcription of the gene for P450 side chain cleave (P450scc), which is the enzymatically rate-limiting step. Acute regulation is mediated by steroidogenic acute regulatory protein, which facilitates the rapid influx of cholesterol into mitochondria, where P450scc resides. Qualitative regulation, determining the class of steroid produced, is principally determined by P450c17. In the absence of P450c17 in the zona glomerulosa, C21 deoxy steroids are produced, leading to the mineralocorticoid aldosterone. In the presence of the 17-hydroxylase but not the 17,20 lyase activity of P450c17 in the zona fasciculata, C21, 17-hydroxy steroids are produced, leading to the glucocorticoid cortisol. When both the 17-hydroxylase and 17,20 lyase activities of P450c17 are present in the zona reticularis, the androgen precursor dehydroepiandrosterone is produced. The discrimination between 17-hydroxylase and 17,20 lyase activities is regulated by two posttranslational events, the serine phosphorylation of P450c17 and the allosteric action of cytochrome b5, both of which act to optimize the interaction of P450c17 with its obligatory electron donor, P450 oxidoreductase.


Article / Publication Details

First-Page Preview
Abstract of Paper

Published online: May 20, 2008
Cover Date: 2008

Number of Print Pages: 18
Number of Figures: 0
Number of Tables: 0

ISBN: 978-3-8055-8580-4 (Print)
eISBN: 978-3-8055-8581-1 (Online)


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Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher or, in the case of photocopying, direct payment of a specified fee to the Copyright Clearance Center.
Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
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