Biosynthesis, post-translational modifications, maturation, and physiological function of human thyroid peroxidase
Journal Title: Postępy Nauk Medycznych - Year 2011, Vol 24, Issue 11
Abstract
Apart from being the major target autoantigen in autoimmune thyroid disease, thyroid peroxidase (TPO) is the key enzyme, together with DUOX proteins, responsible for the thyroid hormone generation. Newly synthesized TPO is processed in the endoplasmic reticulum, undergoing N-glycosylation, heme fixation, and transient interaction with molecular chaperones. Then, while transporting through the Golgi apparatus, O-glycans are attached to the TPO molecule, whereas N-linked oligosaccharides undergo further modifications. After exiting the Golgi, but before it reaches the cell surface, the propeptide is removed. TPO forms dimers, however, the mechanism of this process is still unknown. Only part of the synthesized TPO reaches the cell membrane, whereas partially or totally misfolded forms of TPO are degraded in the endoplasmic reticulum by the proteasome or a plasminogen-like protease, respectively.
Authors and Affiliations
Marlena Godlewska, Andrzej Gardas, Monika Góra
Keywords
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