Conformation of the N-Terminal Ectodomain Elicits Different Effects on DUOX Function: A Potential Impact on Congenital Hypothyroidism Caused by a H2 O2 Production Defect

Thyroid : Official Journal of the American Thyroid Association
Ruy A N LouzadaCorinne Dupuy

Abstract

Dual oxidases (DUOX1 and DUOX2) were initially identified as H2O2 sources involved in thyroid hormone synthesis. Congenital hypothyroidism (CH) resulting from inactivating mutations in the DUOX2 gene highlighted that DUOX2 is the major H2O2 provider to thyroperoxidase. The role of DUOX1 in the thyroid remains unknown. A recent study suggests that it could compensate for DUOX2 deficiency in CH. Both DUOX enzymes and their respective maturation factors DUOXA1 and DUOXA2 form a stable complex at the cell surface, which is fundamental for their enzymatic activity. Recently, intra- and intermolecular disulfide bridges were identified that are essential for the structure and the function of the DUOX2-DUOXA2 complex. This study investigated the involvement of cysteine residues conserved in DUOX1 toward the formation of disulfide bridges, which could be important for the function of the DUOX1DUOXA1 complex. To analyze the role of these cysteine residues in both the targeting and function of dual oxidase, different human DUOX1 mutants were constructed, where the cysteine residues were replaced with glycine. The effect of these mutations on cell surface expression and H2O2-generating activity of the DUOX1-DUOXA1 complex was analyzed. Mut...Continue Reading

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Citations

Jan 8, 2019·Endocrine-related Cancer·Rabii Ameziane El HassaniCorinne Dupuy
Nov 30, 2019·Brazilian Journal of Biology = Revista Brasleira De Biologia·H T YangG W Yang
May 27, 2020·Genetics and Molecular Biology·Caroline Coelho de Faria, Rodrigo Soares Fortunato
Apr 4, 2021·Antioxidants·Jessica BouviereRuy A Louzada

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Methods Mentioned

BETA
transfection
electrophoresis
Immunoprecipitation
Fluorescence
fluorescence-activated cell sorting
glycosylation

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