title: Secretory activity of isolated thyroid adenomas.
abstract: The catabolic phase of thyroid secretion --thyroglubulin (Tg) uptake and hydrolysis, release of hormones--has been investigated in vitro, by incubating thyroid slices with 0.1% labelled Tg, in cases of isolated adenomas. Twenty-two specimens were examined: 11 cold follicular adenomas, 5 hot nodules from euthyroid patients, 2 untreated toxic adenomas, and 4 pretreated toxic adenomas. The results were compared with those obtained in 11 specimens of normal tissue. Tg pinocytosis (the amount of Tg taken up by the slices per mg of tissue) was severely impaired in all the non-toxic nodules, cold or hot, i.e., whatever the in vivo activity of the thyroid iodide pump. In toxic adenomas, every step of the catabolic hormonogenesis was activated: high pinocytotic activity, increased Tg hydrolysis, and the discharge of hormonal products; in pretreated cases, the whole process was slowed down. Enzymic activity of the acid hydrolases, beta-galactosidase and cathepsin, was elevated in all the nodules so far investigated, particularly in the toxic adenomas.
mesh_terms: D000236:Adenoma / Q000378:metabolism*; D002403:Cathepsins / Q000378:metabolism; D005696:Galactosidases / Q000378:metabolism; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D006801:Humans; D006867:Hydrolases / Q000378:metabolism; D066298:In Vitro Techniques; D013954:Thyroglobulin / Q000378:metabolism*; D013964:Thyroid Neoplasms / Q000378:metabolism*
chemical_list: D013954:Thyroglobulin; D005993:Glycerolphosphate Dehydrogenase; D006867:Hydrolases; D005696:Galactosidases; D002403:Cathepsins