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DOI 10.1073/pnas.1716621115

Медицинская библиотека · Proceedings of the National Academy of Sciences of the United States of America · 2017

Clinical, genetic, and structural basis of apparent mineralocorticoid excess due to 11β-hydroxysteroid dehydrogenase type 2 deficiency.

Yau Mabel, Haider Shozeb, Khattab Ahmed, Ling Chen, Mathew Mehr, Zaidi Samir, Bloch Madison, Patel Monica, Ewert Sinead, Abdullah Wafa, Toygar Aysenur, Mudryi Vitalii, Al Badi Maryam, Al-zubaydi Mawj, Wilson Robert C, Al Azkawi Hanan Said, Ozdemir Hatice Nur, Abu-Amer Wahid, Hertecant Jozef, Razzaghy-Azar Maryam, Funder John W, Al Senani Aisha, Sun Li, Kim Se-Min, Yuen Tony, Zaidi Mone, New Maria I

СтатьяПоддержка NIH: внешняя программаПоддержка исследования: вне правительства СШАПеревод пока не подготовлен

Аннотация

Mutations in 11β-hydroxysteroid dehydrogenase type 2 gene (HSD11B2) cause an extraordinarily rare autosomal recessive disorder, apparent mineralocorticoid excess (AME). AME is a form of low renin hypertension that is potentially fatal if untreated. Mutations in the HSD11B2 gene result either in severe AME or a milder phenotype (type 2 AME). To date, ∼40 causative mutations have been identified. As part of the International Consortium for Rare Steroid Disorders, we have diagnosed and followed the largest single worldwide cohort of 36 AME patients. Here, we present the genotype and clinical phenotype of these patients, prominently from consanguineous marriages in the Middle East, who display profound hypertension and hypokalemic alkalosis. To correlate mutations with phenotypic severity, we constructed a computational model of the HSD11B2 protein. Having used a similar strategy for the in silico evaluation of 150 mutations of CYP21A2, the disease-causing gene in congenital adrenal hyperplasia, we now provide a full structural explanation for the clinical severity of AME resulting from each known HSD11B2 missense mutation. We find that mutations that allow the formation of an inactive dimer, alter substrate/coenzyme binding, or impair structural stability of HSD11B2 yield severe AME. In contrast, mutations that cause an indirect disruption of substrate binding or mildly alter intramolecular interactions result in type 2 AME. A simple in silico evaluation of novel missense mutations could help predict the often-diverse phenotypes of an extremely rare monogenic disorder.

Для цитирования: Yau Mabel, Haider Shozeb, Khattab Ahmed, Ling Chen, Mathew Mehr, Zaidi Samir, Bloch Madison, Patel Monica, Ewert Sinead, Abdullah Wafa, Toygar Aysenur, Mudryi Vitalii, Al Badi Maryam, Al-zubaydi Mawj, Wilson Robert C, Al Azkawi Hanan Said, Ozdemir Hatice Nur, Abu-Amer Wahid, Hertecant Jozef, Razzaghy-Azar Maryam, Funder John W, Al Senani Aisha, Sun Li, Kim Se-Min, Yuen Tony, Zaidi Mone, New Maria I. Clinical, genetic, and structural basis of apparent mineralocorticoid excess due to 11β-hydroxysteroid dehydrogenase type 2 deficiency.. Proceedings of the National Academy of Sciences of the United States of America. 2017. DOI: 10.1073/pnas.1716621115.

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