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Abstract
Dehydroepiandrosterone (DHEA) sulfotransferase, known as SULT2A1, converts the androgen precursor DHEA to its inactive sulfate ester, DHEAS, thereby preventing the conversion of DHEA to an active androgen. SULT2A1 requires 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for catalytic activity. We have identified compound heterozygous mutations in the gene encoding human PAPS synthase 2 (PAPSS2) in a girl with premature pubarche, hyperandrogenic anovulation, very low DHEAS levels, and increased androgen levels. In vitro coincubation of human SULT2A1 and wild-type or mutant PAPSS2 proteins confirmed the inactivating nature of the mutations. These observations indicate that PAPSS2 deficiency is a monogenic adrenocortical cause of androgen excess.
Original language | English |
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Pages (from-to) | 2310-2318 |
Number of pages | 9 |
Journal | New England Journal of Medicine |
Volume | 360 |
Issue number | 22 |
DOIs | |
Publication status | Published - 1 May 2009 |
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Dive into the research topics of 'Inactivating PAPSS2 Mutations in a Patient with Premature Pubarche'. Together they form a unique fingerprint.Projects
- 1 Finished
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Pre-Receptor Regulation of Dehydroepiandrosterone Synthesis, Metabolism and Action
1/08/04 → 31/10/09
Project: Research Councils