title: Biochemical and functional changes during the bovine fetal thyroid development.
abstract: To establish biochemical and functional relations during thyroid development, the activity of thyroid peroxidase (TPO), nicotinamide adenine dinucleotide phosphate (NADPH)-cytochrome c reductase and monoamine oxidase (MAO) in a particulate fraction and the iodide transport and organification in slices of bovine fetal thyroid were examined throughout gestation. The cytochemical localization of TPO, H2O2 generating sites and MAO was also studied. Fetal glands were grouped in stages I to V according to increasing developmental features; adult tissues were also analyzed. TPO activity in each of the fetal stages was higher than in the adult; a marked increase was observed in stages IV and V. Iodide transport (T/M) was similar in stages I to V and the adult. Iodide organification in fetal thyroids showed a similar pattern to that of TPO activity. When compared with the adult, at midgestation (stages II to III), a lower iodination coexisted with a higher TPO activity. The activity of NADPH-cytochrome c reductase and MAO, two enzymes previously proposed to participate in thyroid H2O2 generation, did not parallel the level of iodide organification. Cells from stages II to V exhibited a positive cytochemical reaction for TPO in the rough endoplasmic reticulum (RER) and the perinuclear cisternae (PC). In stages IV, V, and adult, TPO was occasionally found in apical vesicles and microvilli, whereas H2O2 was detected within the RER and the PC. MAO reaction was positive in adult, but not in fetal thyroid. These results indicate that a high TPO activity accompanied the onset of the organification process during fetal thyroid development. The level of iodination was associated with the presence of TPO at a proper site rather than to the level of TPO activity. Evidence against a role of NADPH-cytochrome c reductase and MAO in the iodide organification was obtained.
authors.affiliation: Departamento de Bioquímica Clínica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Argentina.
authors.forename: A M
authors.initials: AM
authors.lastname: Masini-Repiso
authors.forename: E
authors.initials: E
authors.lastname: Orgnero-Gaisán
authors.forename: M
authors.initials: M
authors.lastname: Bonaterra
authors.forename: A M
authors.initials: AM
authors.lastname: Cabanillas
authors.forename: A H
authors.initials: AH
authors.lastname: Coleoni
mesh_terms: D000818:Animals; D001692:Biological Transport / Q000502:physiology; D002417:Cattle / Q000196:embryology; D004247:DNA / Q000378:metabolism; D005314:Embryonic and Fetal Development / Q000502:physiology; D005333:Fetus / Q000378:metabolism / Q000502:physiology*; D006651:Histocytochemistry; D006861:Hydrogen Peroxide / Q000378:metabolism; D007453:Iodide Peroxidase / Q000378:metabolism; D007454:Iodides / Q000378:metabolism; D008995:Monoamine Oxidase / Q000378:metabolism; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism; D011506:Proteins / Q000378:metabolism; D013961:Thyroid Gland / Q000196:embryology* / Q000378:metabolism / Q000502:physiology
chemical_list: D007454:Iodides; D011506:Proteins; D004247:DNA; D006861:Hydrogen Peroxide; D007453:Iodide Peroxidase; D008995:Monoamine Oxidase; D009251:NADPH-Ferrihemoprotein Reductase