Thyroidal extracellular glutathione peroxidase: a potential regulator of thyroid-hormone synthesis

Human thyrocytes were found to synthesize and secrete the selenoenzyme extracellular glutathione peroxidase (E-GPX), a process which was controlled by the Ca2+/phosphoinositol second-messenger cascade. The potential involvement of thyroidal E-GPX in the regulation of thyroid-hormone synthesis and in...

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Bibliographic Details
Published in:Biochemical journal 1995-06, Vol.308 ( Pt 3) (3), p.713-717
Main Authors: Howie, A F, Walker, S W, Akesson, B, Arthur, J R, Beckett, G J
Format: Article
Language:English
Subjects:
8-Bromo Cyclic Adenosine Monophosphate - pharmacology
Blotting, Western
Brefeldin A
Calcimycin - pharmacology
Cells, Cultured
Culture Media - metabolism
Cyclopentanes - pharmacology
Electrophoresis, Polyacrylamide Gel
Extracellular Space - enzymology
Glutathione Peroxidase - metabolism
Glutathione Peroxidase - pharmacology
Humans
Proteins - metabolism
Selenoproteins
Sodium Selenite - metabolism
Tetradecanoylphorbol Acetate - pharmacology
Thyroid Gland - drug effects
Thyroid Gland - enzymology
Thyroid Hormones - biosynthesis
Thyrotropin - pharmacology
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Summary:Human thyrocytes were found to synthesize and secrete the selenoenzyme extracellular glutathione peroxidase (E-GPX), a process which was controlled by the Ca2+/phosphoinositol second-messenger cascade. The potential involvement of thyroidal E-GPX in the regulation of thyroid-hormone synthesis and in the protection of the thyrocyte from peroxidative damage is discussed.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3080713