The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders

Steroidogenesis, the processes by which cholesterol is converted to steroid hormones, involves transport proteins, enzymes, redox partners and cofactors. Most steroidogenic enzymes are either forms of cytochrome P450 or are hydroxysteroid dehydrogenases. The P450s may be either Type 1, in mitochondr...

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Published in	Endocrine reviews Vol. 32; no. 1; pp. 81 - 151
Main Authors	Miller, Walter L., Auchus, Richard J.
Format	Journal Article
Language	English
Published	Bethesda, MD Oxford University Press 01.02.2011 Copyright by The Endocrine Society Endocrine Society
Subjects	Adrenal Glands - enzymology Aldo-keto reductase Aldosterone Animals Biochemistry Biological activity Biological and medical sciences Biological effects Catalytic converters Cellular structure Chemical synthesis Cholesterol Cholesterol - metabolism Cofactors Cytochrome Cytochrome P450 Cytochromes P450 Dehydrogenase Dehydrogenases Disorders Electron Transport Endoplasmic reticulum Enzymes Female Fertility Fundamental and applied biological sciences. Psychology Gonads Gonads - enzymology Homeostasis Hormones Humans Hydroxysteroids Hypertension Male Mice Mitochondria Mitochondria - enzymology Molecular biology Mutation Phenotypes Phosphoproteins - metabolism Physiology Pregnenolone Pregnenolone - biosynthesis Protein biosynthesis Protein transport Proteins Rats Reductases Regulatory mechanisms (biology) Reviews Sex differentiation Sex hormones Steroid hormones Steroidogenesis Steroids Steroids - biosynthesis Vertebrates: endocrinology Human Steroidogenesis Review Molecular biology
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Abstract	Steroidogenesis, the processes by which cholesterol is converted to steroid hormones, involves transport proteins, enzymes, redox partners and cofactors. Most steroidogenic enzymes are either forms of cytochrome P450 or are hydroxysteroid dehydrogenases. The P450s may be either Type 1, in mitochondria, or Type 2, in the endoplasmic reticulum; these two types differ in their electron-transfer redox partners as well as in their cellular locations. Hydroxysteroid dehydrogenases may be either shortchain dehydrogenases or aldo-keto reductases, which differ in their structures and catalytic mechanisms. Recent work has identified new enzymes, co-factors and protein modifications, and has described new pathways of steroidogenesis and new sites of steroid synthesis. Thus steroidogenesis is not confined to the adrenals and gonads, and involves more than the production of aldosterone, cortisol and sex steroids. We review the enzymes, factors and pathways of human steroidogenesis and the diseases resulting from their mutations.Steroidogenesis entails processes by which cholesterol is converted to biologically active steroid hormones. Whereas most endocrine texts discuss adrenal, ovarian, testicular, placental, and other steroidogenic processes in a gland-specific fashion, steroidogenesis is better understood as a single process that is repeated in each gland with cell-type-specific variations on a single theme. Thus, understanding steroidogenesis is rooted in an understanding of the biochemistry of the various steroidogenic enzymes and cofactors and the genes that encode them. The first and rate-limiting step in steroidogenesis is the conversion of cholesterol to pregnenolone by a single enzyme, P450scc (CYP11A1), but this enzymatically complex step is subject to multiple regulatory mechanisms, yielding finely tuned quantitative regulation. Qualitative regulation determining the type of steroid to be produced is mediated by many enzymes and cofactors. Steroidogenic enzymes fall into two groups: cytochrome P450 enzymes and hydroxysteroid dehydrogenases. A cytochrome P450 may be either type 1 (in mitochondria) or type 2 (in endoplasmic reticulum), and a hydroxysteroid dehydrogenase may belong to either the aldo-keto reductase or short-chain dehydrogenase/reductase families. The activities of these enzymes are modulated by posttranslational modifications and by cofactors, especially electron-donating redox partners. The elucidation of the precise roles of these various enzymes and cofactors has been greatly facilitated by identifying the genetic bases of rare disorders of steroidogenesis. Some enzymes not principally involved in steroidogenesis may also catalyze extraglandular steroidogenesis, modulating the phenotype expected to result from some mutations. Understanding steroidogenesis is of fundamental importance to understanding disorders of sexual differentiation, reproduction, fertility, hypertension, obesity, and physiological homeostasis.
AbstractList	Steroidogenesis, the processes by which cholesterol is converted to steroid hormones, involves transport proteins, enzymes, redox partners and cofactors. Most steroidogenic enzymes are either forms of cytochrome P450 or are hydroxysteroid dehydrogenases. The P450s may be either Type 1, in mitochondria, or Type 2, in the endoplasmic reticulum; these two types differ in their electron-transfer redox partners as well as in their cellular locations. Hydroxysteroid dehydrogenases may be either shortchain dehydrogenases or aldo-keto reductases, which differ in their structures and catalytic mechanisms. Recent work has identified new enzymes, co-factors and protein modifications, and has described new pathways of steroidogenesis and new sites of steroid synthesis. Thus steroidogenesis is not confined to the adrenals and gonads, and involves more than the production of aldosterone, cortisol and sex steroids. We review the enzymes, factors and pathways of human steroidogenesis and the diseases resulting from their mutations.Steroidogenesis entails processes by which cholesterol is converted to biologically active steroid hormones. Whereas most endocrine texts discuss adrenal, ovarian, testicular, placental, and other steroidogenic processes in a gland-specific fashion, steroidogenesis is better understood as a single process that is repeated in each gland with cell-type-specific variations on a single theme. Thus, understanding steroidogenesis is rooted in an understanding of the biochemistry of the various steroidogenic enzymes and cofactors and the genes that encode them. The first and rate-limiting step in steroidogenesis is the conversion of cholesterol to pregnenolone by a single enzyme, P450scc (CYP11A1), but this enzymatically complex step is subject to multiple regulatory mechanisms, yielding finely tuned quantitative regulation. Qualitative regulation determining the type of steroid to be produced is mediated by many enzymes and cofactors. Steroidogenic enzymes fall into two groups: cytochrome P450 enzymes and hydroxysteroid dehydrogenases. A cytochrome P450 may be either type 1 (in mitochondria) or type 2 (in endoplasmic reticulum), and a hydroxysteroid dehydrogenase may belong to either the aldo-keto reductase or short-chain dehydrogenase/reductase families. The activities of these enzymes are modulated by posttranslational modifications and by cofactors, especially electron-donating redox partners. The elucidation of the precise roles of these various enzymes and cofactors has been greatly facilitated by identifying the genetic bases of rare disorders of steroidogenesis. Some enzymes not principally involved in steroidogenesis may also catalyze extraglandular steroidogenesis, modulating the phenotype expected to result from some mutations. Understanding steroidogenesis is of fundamental importance to understanding disorders of sexual differentiation, reproduction, fertility, hypertension, obesity, and physiological homeostasis. Steroidogenesis entails processes by which cholesterol is converted to biologically active steroid hormones. Whereas most endocrine texts discuss adrenal, ovarian, testicular, placental, and other steroidogenic processes in a gland-specific fashion, steroidogenesis is better understood as a single process that is repeated in each gland with cell-type-specific variations on a single theme. Thus, understanding steroidogenesis is rooted in an understanding of the biochemistry of the various steroidogenic enzymes and cofactors and the genes that encode them. The first and rate-limiting step in steroidogenesis is the conversion of cholesterol to pregnenolone by a single enzyme, P450scc (CYP11A1), but this enzymatically complex step is subject to multiple regulatory mechanisms, yielding finely tuned quantitative regulation. Qualitative regulation determining the type of steroid to be produced is mediated by many enzymes and cofactors. Steroidogenic enzymes fall into two groupscytochrome P450 enzymes and hydroxysteroid dehydrogenases. A cytochrome P450 may be either type 1 (in mitochondria) or type 2 (in endoplasmic reticulum), and a hydroxysteroid dehydrogenase may belong to either the aldo-keto reductase or short-chain dehydrogenase/reductase families. The activities of these enzymes are modulated by posttranslational modifications and by cofactors, especially electron-donating redox partners. The elucidation of the precise roles of these various enzymes and cofactors has been greatly facilitated by identifying the genetic bases of rare disorders of steroidogenesis. Some enzymes not principally involved in steroidogenesis may also catalyze extraglandular steroidogenesis, modulating the phenotype expected to result from some mutations. Understanding steroidogenesis is of fundamental importance to understanding disorders of sexual differentiation, reproduction, fertility, hypertension, obesity, and physiological homeostasis. Steroidogenesis entails processes by which cholesterol is converted to biologically active steroid hormones. Whereas most endocrine texts discuss adrenal, ovarian, testicular, placental, and other steroidogenic processes in a gland-specific fashion, steroidogenesis is better understood as a single process that is repeated in each gland with cell-type-specific variations on a single theme. Thus, understanding steroidogenesis is rooted in an understanding of the biochemistry of the various steroidogenic enzymes and cofactors and the genes that encode them. The first and rate-limiting step in steroidogenesis is the conversion of cholesterol to pregnenolone by a single enzyme, P450scc (CYP11A1), but this enzymatically complex step is subject to multiple regulatory mechanisms, yielding finely tuned quantitative regulation. Qualitative regulation determining the type of steroid to be produced is mediated by many enzymes and cofactors. Steroidogenic enzymes fall into two groups: cytochrome P450 enzymes and hydroxysteroid dehydrogenases. A cytochrome P450 may be either type 1 (in mitochondria) or type 2 (in endoplasmic reticulum), and a hydroxysteroid dehydrogenase may belong to either the aldo-keto reductase or short-chain dehydrogenase/reductase families. The activities of these enzymes are modulated by posttranslational modifications and by cofactors, especially electron-donating redox partners. The elucidation of the precise roles of these various enzymes and cofactors has been greatly facilitated by identifying the genetic bases of rare disorders of steroidogenesis. Some enzymes not principally involved in steroidogenesis may also catalyze extraglandular steroidogenesis, modulating the phenotype expected to result from some mutations. Understanding steroidogenesis is of fundamental importance to understanding disorders of sexual differentiation, reproduction, fertility, hypertension, obesity, and physiological homeostasis. Steroidogenesis entails processes by which cholesterol is converted to biologically active steroid hormones. Whereas most endocrine texts discuss adrenal, ovarian, testicular, placental, and other steroidogenic processes in a gland-specific fashion, steroidogenesis is better understood as a single process that is repeated in each gland with cell-type-specific variations on a single theme. Thus, understanding steroidogenesis is rooted in an understanding of the biochemistry of the various steroidogenic enzymes and cofactors and the genes that encode them. The first and rate-limiting step in steroidogenesis is the conversion of cholesterol to pregnenolone by a single enzyme, P450scc (CYP11A1), but this enzymatically complex step is subject to multiple regulatory mechanisms, yielding finely tuned quantitative regulation. Qualitative regulation determining the type of steroid to be produced is mediated by many enzymes and cofactors. Steroidogenic enzymes fall into two groups: cytochrome P450 enzymes and hydroxysteroid dehydrogenases. A cytochrome P450 may be either type 1 (in mitochondria) or type 2 (in endoplasmic reticulum), and a hydroxysteroid dehydrogenase may belong to either the aldo-keto reductase or short-chain dehydrogenase/reductase families. The activities of these enzymes are modulated by posttranslational modifications and by cofactors, especially electron-donating redox partners. The elucidation of the precise roles of these various enzymes and cofactors has been greatly facilitated by identifying the genetic bases of rare disorders of steroidogenesis. Some enzymes not principally involved in steroidogenesis may also catalyze extraglandular steroidogenesis, modulating the phenotype expected to result from some mutations. Understanding steroidogenesis is of fundamental importance to understanding disorders of sexual differentiation, reproduction, fertility, hypertension, obesity, and physiological homeostasis.Steroidogenesis entails processes by which cholesterol is converted to biologically active steroid hormones. Whereas most endocrine texts discuss adrenal, ovarian, testicular, placental, and other steroidogenic processes in a gland-specific fashion, steroidogenesis is better understood as a single process that is repeated in each gland with cell-type-specific variations on a single theme. Thus, understanding steroidogenesis is rooted in an understanding of the biochemistry of the various steroidogenic enzymes and cofactors and the genes that encode them. The first and rate-limiting step in steroidogenesis is the conversion of cholesterol to pregnenolone by a single enzyme, P450scc (CYP11A1), but this enzymatically complex step is subject to multiple regulatory mechanisms, yielding finely tuned quantitative regulation. Qualitative regulation determining the type of steroid to be produced is mediated by many enzymes and cofactors. Steroidogenic enzymes fall into two groups: cytochrome P450 enzymes and hydroxysteroid dehydrogenases. A cytochrome P450 may be either type 1 (in mitochondria) or type 2 (in endoplasmic reticulum), and a hydroxysteroid dehydrogenase may belong to either the aldo-keto reductase or short-chain dehydrogenase/reductase families. The activities of these enzymes are modulated by posttranslational modifications and by cofactors, especially electron-donating redox partners. The elucidation of the precise roles of these various enzymes and cofactors has been greatly facilitated by identifying the genetic bases of rare disorders of steroidogenesis. Some enzymes not principally involved in steroidogenesis may also catalyze extraglandular steroidogenesis, modulating the phenotype expected to result from some mutations. Understanding steroidogenesis is of fundamental importance to understanding disorders of sexual differentiation, reproduction, fertility, hypertension, obesity, and physiological homeostasis. Steroidogenesis, the processes by which cholesterol is converted to steroid hormones, involves transport proteins, enzymes, redox partners and cofactors. Most steroidogenic enzymes are either forms of cytochrome P450 or are hydroxysteroid dehydrogenases. The P450s may be either Type 1, in mitochondria, or Type 2, in the endoplasmic reticulum; these two types differ in their electron-transfer redox partners as well as in their cellular locations. Hydroxysteroid dehydrogenases may be either shortchain dehydrogenases or aldo-keto reductases, which differ in their structures and catalytic mechanisms. Recent work has identified new enzymes, co-factors and protein modifications, and has described new pathways of steroidogenesis and new sites of steroid synthesis. Thus steroidogenesis is not confined to the adrenals and gonads, and involves more than the production of aldosterone, cortisol and sex steroids. We review the enzymes, factors and pathways of human steroidogenesis and the diseases resulting from their mutations. Steroidogenesis entails processes by which cholesterol is converted to biologically active steroid hormones. Whereas most endocrine texts discuss adrenal, ovarian, testicular, placental, and other steroidogenic processes in a gland-specific fashion, steroidogenesis is better understood as a single process that is repeated in each gland with cell-type-specific variations on a single theme. Thus, understanding steroidogenesis is rooted in an understanding of the biochemistry of the various steroidogenic enzymes and cofactors and the genes that encode them. The first and rate-limiting step in steroidogenesis is the conversion of cholesterol to pregnenolone by a single enzyme, P450scc (CYP11A1), but this enzymatically complex step is subject to multiple regulatory mechanisms, yielding finely tuned quantitative regulation. Qualitative regulation determining the type of steroid to be produced is mediated by many enzymes and cofactors. Steroidogenic enzymes fall into two groups: cytochrome P450 enzymes and hydroxysteroid dehydrogenases. A cytochrome P450 may be either type 1 (in mitochondria) or type 2 (in endoplasmic reticulum), and a hydroxysteroid dehydrogenase may belong to either the aldo-keto reductase or short-chain dehydrogenase/reductase families. The activities of these enzymes are modulated by posttranslational modifications and by cofactors, especially electron-donating redox partners. The elucidation of the precise roles of these various enzymes and cofactors has been greatly facilitated by identifying the genetic bases of rare disorders of steroidogenesis. Some enzymes not principally involved in steroidogenesis may also catalyze extraglandular steroidogenesis, modulating the phenotype expected to result from some mutations. Understanding steroidogenesis is of fundamental importance to understanding disorders of sexual differentiation, reproduction, fertility, hypertension, obesity, and physiological homeostasis.
Author	Miller, Walter L. Auchus, Richard J.
AuthorAffiliation	Department of Pediatrics (W.L.M.), University of California, San Francisco, San Francisco, California 94143-0978; and Department of Medicine (R.J.A.), University of Texas Southwestern Medical Center, Dallas, Texas 75235-8857
AuthorAffiliation_xml	– name: Department of Pediatrics (W.L.M.), University of California, San Francisco, San Francisco, California 94143-0978; and Department of Medicine (R.J.A.), University of Texas Southwestern Medical Center, Dallas, Texas 75235-8857
Author_xml	– sequence: 1 givenname: Walter L. surname: Miller fullname: Miller, Walter L. email: wlmlab@ucsf.edu organization: 1Department of Pediatrics (W.L.M.), University of California, San Francisco, San Francisco, California 94143-0978 – sequence: 2 givenname: Richard J. surname: Auchus fullname: Auchus, Richard J. organization: 2Department of Medicine (R.J.A.), University of Texas Southwestern Medical Center, Dallas, Texas 75235-8857
BackLink	http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23866007$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/21051590$$D View this record in MEDLINE/PubMed
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Snippet	Steroidogenesis, the processes by which cholesterol is converted to steroid hormones, involves transport proteins, enzymes, redox partners and cofactors. Most... Steroidogenesis entails processes by which cholesterol is converted to biologically active steroid hormones. Whereas most endocrine texts discuss adrenal,...
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SubjectTerms	Adrenal Glands - enzymology Aldo-keto reductase Aldosterone Animals Biochemistry Biological activity Biological and medical sciences Biological effects Catalytic converters Cellular structure Chemical synthesis Cholesterol Cholesterol - metabolism Cofactors Cytochrome Cytochrome P450 Cytochromes P450 Dehydrogenase Dehydrogenases Disorders Electron Transport Endoplasmic reticulum Enzymes Female Fertility Fundamental and applied biological sciences. Psychology Gonads Gonads - enzymology Homeostasis Hormones Humans Hydroxysteroids Hypertension Male Mice Mitochondria Mitochondria - enzymology Molecular biology Mutation Phenotypes Phosphoproteins - metabolism Physiology Pregnenolone Pregnenolone - biosynthesis Protein biosynthesis Protein transport Proteins Rats Reductases Regulatory mechanisms (biology) Reviews Sex differentiation Sex hormones Steroid hormones Steroidogenesis Steroids Steroids - biosynthesis Vertebrates: endocrinology
Title	The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders
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