Identification of a Truncated Dual Oxidase 2 (DUOX2) Messenger Ribonucleic Acid (mRNA) in Two Rat Thyroid Cell Lines. Insulin and Forskolin Regulation of DUOX2 mRNA Levels in FRTL-5 Cells and Porcine Thyrocytes

Autor: Jacques Kaniewski, Stanislas Morand, Renée Ohayon, Orquidea Filipe Dos Santos, Marie-Sophie Noel-Hudson, Alain Virion, Corinne Dupuy

Publikováno v: Endocrinology. 144:567-574

The Duox2 flavoprotein is strongly expressed in the thyroid gland, where it plays a critical role in the synthesis of thyroid hormones likely by providing thyroperoxidase with H(2)O(2). A truncated DUOX2 mRNA was isolated from the rat thyroid cell li

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37672a8da43d6cc7420d3aa944d46bdf
https://doi.org/10.1210/en.2002-220824

Iodotyrosine dehalogenase 1 (DEHAL1) is a transmembrane protein involved in the recycling of iodide close to the thyroglobulin iodination site

Autor: Sédami Gnidehou, Alphonse Sezan, Françoise Courtin, Bernard Caillou, Monique Talbot, Corinne Dupuy, Marie-Sophie Noël-Hudson, Diane Agnangji, Alain Virion, Renée Ohayon, Stanislas Morand, Jacques Kaniewski

Publikováno v: The FASEB Journal. 18:1574-1576

In the thyroid, iodotyrosine dehalogenase acts on the mono and diiodotyrosines released during the hydrolysis of thyroglobulin to liberate iodide, which can then reenter the hormone-producing pathways. It has been reported that the deiodination of io

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2090d31ba943a318469b784ef61bc97e
https://doi.org/10.1096/fj.04-2023fje

Effect of N-glycan removal on the enzymatic activity of porcine thyroid peroxidase

Autor: Jean-Louis Franc, Yannick Long, Annie Giraud, Jacques Kaniewski, Jeanne Lanet

Publikováno v: European Journal of Biochemistry
European Journal of Biochemistry, Wiley, 1991, 202 (2), pp.501-5
European Journal of Biochemistry, 1991, 202 (2), pp.501-5

International audience; Active porcine thyroid peroxidase (pTPO) has been purified either by deoxycholate extraction followed by immunoaffinity purification (pTPO A) or by trypsin/digitonin extraction followed by ion-exchange and gelfiltration chroma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::249bf1889c76ff65b681797e894783f2
https://doi.org/10.1111/j.1432-1033.1991.tb16401.x

Mechanism of hydrogen peroxide formation catalyzed by NADPH oxidase in thyroid plasma membrane

Autor: Danielle Dème, Renée Ohayon, Alain Virion, Corinne Dupuy, Jacques Pommier, Jacques Kaniewski

Publikováno v: Journal of Biological Chemistry. 266:3739-3743

The thyroid plasma membrane contains a Ca2(+)-regulated NADPH-dependent H2O2 generating system which provides H2O2 for the thyroid peroxidase-catalyzed biosynthesis of thyroid hormones. The plasma membrane fraction contains a Ca2(+)-independent cytoc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25c7307597f00a5885925f4661e85b54
https://doi.org/10.1016/s0021-9258(19)67857-9

Targeting of the dual oxidase 2 N-terminal region to the plasma membrane

Autor: Marie-Sophie Noel-Hudson, Sédami Gnidehou, Sandrine Buisson, Valérie Nicolas, Corinne Dupuy, Laetitia Macon-Lemaitre, Jacques Kaniewski, Diane Agnandji, Alain Virion, Stanislas Morand, Renée Ohayon

Publikováno v: The Journal of biological chemistry. 279(29)

Dual oxidase 2 (Duox2) is a cell surface glycoprotein that probably provides thyroperoxidase with the H2O2 required to catalyze thyroid hormone synthesis. No functional H2O2-generating system has yet been obtained after transfecting Duox2 into non-th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbcd6a48b734cb7e314a199609882603
https://pubmed.ncbi.nlm.nih.gov/15150274