Transport of thyroglobulin and peroxidase in the thyroid follicle cell.
The purpose of this study was to explore the nature of the protein(s) in the exocytotic vesicles in the thyroid follicle cells and to ascertain whether or not thyroglobulin and peroxidase are transported by the same vesicles through the apical region of the cells to the follicle lumen. The study was performed on rats pretreated with thyroxine for 2 days in order to inhibit endocytosis. A fraction of exocytotic vesicles was isolated by centrifugation in continuous and discontinuous sucrose density gradients. The protein content of the vesicles were analysed by electrophoresis in continuous polyacrylamide gradient gels. The vesicles contained (uniodinated) thyroglobulin, 12-S protein and thyralbumin. Parallel histochemical studies in the electron microscope. These observations have important bearings on the mechanisms for thyroglobulin iodination, since it has been demonstrated that iodination does not occur in the exocytotic vesicles but in connection with the opening of the vesicles at the apical cell surface.
D000818:Animals; D002458:Cell Fractionation; D005089:Exocytosis; D008854:Microscopy, Electron; D008861:Microsomes / Q000378:metabolism; D010544:Peroxidases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism; D051381:Rats; D013954:Thyroglobulin / Q000378:metabolism*; D013961:Thyroid Gland / Q000166:cytology / Q000378:metabolism* / Q000648:ultrastructure
D011506:Proteins; D013954:Thyroglobulin; D010544:Peroxidases