Does kidney transplantation normalise cortisol metabolism in apparent mineralocorticoid excess syndrome?

2000 ◽  
Vol 23 (7) ◽  
pp. 457-462 ◽  
Author(s):  
M. Palermo ◽  
G. Delitala ◽  
G. Sorba ◽  
M. Cossu ◽  
R. Satta ◽  
...  
Keyword(s):  
Kidney Transplantation ◽  
Cortisol Metabolism ◽  
Apparent Mineralocorticoid Excess ◽  
Apparent Mineralocorticoid Excess Syndrome

Steroid characteristics of mineralocorticoid adrenocortical hypertension

1991 ◽  
Vol 37 (10) ◽  
pp. 1843-1848 ◽  
Author(s):  
E G Biglieri ◽  
C E Kater
Keyword(s):  
Plasma Renin ◽  
Zona Glomerulosa ◽  
Zona Fasciculata ◽  
Hydroxylase Deficiency ◽  
Aldosterone Production ◽  
Apparent Mineralocorticoid Excess ◽  
Tomography Scan ◽  
Apparent Mineralocorticoid Excess Syndrome ◽  
Hydroxy Steroid ◽  
Steroid Dehydrogenase

Abstract Adrenocortical causes of hypertension are established by examining the mineralocorticoid hormones produced in the zona glomerulosa and zona fasciculata. In the zona glomerulosa, aldosterone excess leads to hypertension, hypokalemia, and suppressed plasma renin activity, with increased concentrations of urinary aldosterone (either as the 18-glucuronide or free aldosterone) as an index of its production. Identifying a tumor by computed tomography scan verifies the diagnosis of a correctable lesion. If no tumor is found, several maneuvers are used to identify primary adrenal hyperplasia, a disorder with autonomous aldosterone production, for which reduction of adrenal mass is curative. The zona fasciculata has two major pathways: the 17-deoxy pathway, where deoxycorticosterone (DOC) and corticosterone are the significant steroids, and the 17-hydroxy pathway, which leads to cortisol production. Tumors of the 17-deoxy pathway, DOC-producing adenomas, have increased concentrations of DOC and its precursor steroids, normal concentrations of cortisol, and suppression of aldosterone production secondary to suppression of the renin system. Two enzymatic defects in the zona fasciculata, 11 beta- and 17 alpha-hydroxylase deficiency, can be first readily identified by the virilization in the former, hypogonadal features in the latter. Steroid patterns are diagnostic. DOC is produced in excess in both deficiencies and is the cause of the hypertension. Deficient or impaired 11 beta-hydroxy steroid dehydrogenase in the apparent mineralocorticoid excess syndrome or after licorice ingestion retards the conversion of cortisol to inactive cortisone in the kidney, leading to mineralocorticoid hypertension; this leads to suppression of the renin system and subsequently of aldosterone.

Nephrocalcinosis and renal cysts associated with apparent mineralocorticoid excess syndrome

2000 ◽  
Vol 15 (1-2) ◽  
pp. 60-62 ◽  
Author(s):  
A. Moudgil ◽  
G. Rodich ◽  
S. C. Jordan ◽  
E. S. Kamil
Keyword(s):  
Renal Cysts ◽  
Apparent Mineralocorticoid Excess ◽  
Apparent Mineralocorticoid Excess Syndrome

Alterations of Cortisol Metabolism in Human Disorders

2018 ◽  
Vol 89 (5) ◽  
pp. 320-330 ◽  
Author(s):  
Perrin C. White
Keyword(s):  
Drug Target ◽  
Severe Form ◽  
Physiological Effects ◽  
Gene Encoding ◽  
Cortisol Metabolism ◽  
Low Renin Hypertension ◽  
Apparent Mineralocorticoid Excess ◽  
Human Disorders

The interconversion of active and inactive corticosteroids – cortisol and cortisone, respectively, in humans – is modulated by isozymes of 11β-hydroxysteroid dehydrogenase (11-HSD). Studies of this process have provided crucial insights into glucocorticoid effects in a wide variety of tissues. The 11-HSD1 isozyme functions mainly as an oxoreductase (cortisone to cortisol) and is expressed at high levels in the liver and other glucocorticoid target tissues. Because it is required for full physiological effects of cortisol, it has emerged as a drug target for metabolic syndrome and type 2 diabetes. Mutations in the corresponding HSD11B1 gene, or in the H6PD gene encoding hexose-6-phosphate dehydrogenase (which supplies the NADPH required for the oxoreductase activity of 11-HSD1), cause apparent cortisone reductase deficiency, a rare syndrome of adrenocortical hyperactivity and hyperandrogenism. In contrast, the 11-HSD2 isozyme functions as a dehydrogenase (cortisol to cortisone) and is expressed mainly in mineralocorticoid target tissues, where it bars access of cortisol to the mineralocorticoid receptor. Mutations in the HSD11B2 gene encoding 11-HSD2 cause the syndrome of apparent mineralocorticoid excess, a severe form of familial hypertension. The role of this enzyme in the pathogenesis of common forms of low-renin hypertension remains uncertain.

scholarly journals Clinical, Biochemical, and Genetic Characteristics of “Nonclassic” Apparent Mineralocorticoid Excess Syndrome

2018 ◽  
Vol 104 (2) ◽  
pp. 595-603 ◽  
Author(s):  
Alejandra Tapia-Castillo ◽  
Rene Baudrand ◽  
Anand Vaidya ◽  
Carmen Campino ◽  
Fidel Allende ◽  
...  
Keyword(s):  
Genetic Characteristics ◽  
Apparent Mineralocorticoid Excess ◽  
Apparent Mineralocorticoid Excess Syndrome

scholarly journals Apparent mineralocorticoid excess syndrome in a Brazilian boy caused by the homozygous missense mutation p.R186C in the HSD11B2 gene

2008 ◽  
Vol 52 (8) ◽  
pp. 1277-1281 ◽  
Author(s):  
Fernanda Borchers Coeli ◽  
Lúcio Fábio Caldas Ferraz ◽  
Sofia H. V. de Lemos-Marini ◽  
Sumara Zuanazi Pinto Rigatto ◽  
Vera Maria Santoro Belangero ◽  
...  
Keyword(s):  
Mineralocorticoid Receptor ◽  
Autosomal Recessive ◽  
Autosomal Recessive Disorder ◽  
Homozygous Mutation ◽  
Molecular Studies ◽  
Apparent Mineralocorticoid Excess ◽  
Gene Maps ◽  
Apparent Mineralocorticoid Excess Syndrome

The apparent mineralocorticoid excess syndrome (AME) is a rare autosomal recessive disorder due to the deficiency of 11β-hydroxysteroid dehydrogenase type 2 enzyme (11beta-HSD2). The 11beta-HSD2 enzyme, encoded by HSD11B2 gene, metabolizes active cortisol in cortisone. Mutations on HSD11B2 gene affect the enzyme activity by leading to an excess of cortisol, which causes its inappropriate access to mineralocorticoid receptor. Therefore, cortisol will bind mineralocorticoid receptor. The human HSD11B2 gene maps to chromosome 16q22 and consists of five exons encoding a protein of 405 amino acids. We present here clinical and molecular studies on a Brazilian boy who was born pre-term after an oligodramnious pregnancy. He was diagnosed as having AME at the age of 26 months. His parents are second cousins. Molecular characterization of the HSD11B2 gene revealed the homozygous mutation p.R186C. The patient described here is the second case of HDS11B2 gene mutation reported in Brazilian patients with AME.

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