title: Different concentrations of thyroid peroxidase and thyroglobulin in the nuclear envelope and the endoplasmic reticulum throughout the cytoplasm.
abstract: Thyroid peroxidase (TPO) and thyroglobulin (TG) represent two major glycoproteins of thyroid follicular cells performing biological functions such as iodination, transcytosis of thyroglobulin, and formation of thyroid hormones. They are involved in thyroid autoimmunity and thyroid inborn metabolic disorders. Studying these processes at a molecular level includes the determination of their precise intracellular distribution. An evaluation of the relative concentrations of TG and TPO in different subcellular compartments was carried out in stimulated human follicular cells using thin-frozen sections and the immunogold technique. It is documented that TG is transported from the endoplasmic reticulum and the Golgi apparatus to the follicular lumen by transport vesicles; most of it being present in the expanded endoplasmic reticulum throughout the cytoplasm. On the other hand, gold particles indicating TPO are adjacent to the membranes of the exocytotic pathway. They do not label the basolateral membrane but show the strongest density in the nuclear envelope and the apical membrane. The labeling density of TPO is about four times higher in the nuclear envelope than in the endoplasmic reticulum throughout the cytoplasm. In contrast, TG is concentrated three times higher in the rough endoplasmic reticulum throughout the cytoplasm than in the nuclear cisternae. Our results give the first quantitative evidence that TPO and TG are concentrated in different subcompartments of the endoplasmic reticulum. Because previous studies demonstrated the nuclear envelope as the site where the synthesis of endogenous peroxidase (Brökelmann, J., D. W. Fawcett, Biol. Reprod. 1, 59-71 (1969)) begins, we suggest that synthesis of these functionally related proteins happens in specialized parts of the endoplasmic reticulum.(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: Klinik und Poliklinik für Kinderheilkunde, Universität Münster, Münster/Deutschland.
authors.forename: K P
authors.initials: KP
authors.lastname: Zimmer
authors.forename: K
authors.initials: K
authors.lastname: Hengst
authors.forename: P
authors.initials: P
authors.lastname: Carayon
authors.forename: J
authors.initials: J
authors.lastname: Brämswig
authors.forename: E
authors.initials: E
authors.lastname: Harms
mesh_terms: D001692:Biological Transport; D016764:Cell Polarity; D003593:Cytoplasm / Q000201:enzymology; D004721:Endoplasmic Reticulum / Q000737:chemistry; D006111:Graves Disease / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D008562:Membrane Glycoproteins / Q000032:analysis; D009685:Nuclear Envelope / Q000737:chemistry; D009195:Peroxidase / Q000032:analysis*; D013347:Subcellular Fractions / Q000737:chemistry*; D013954:Thyroglobulin / Q000032:analysis*; D013961:Thyroid Gland / Q000737:chemistry* / Q000648:ultrastructure; D013965:Thyroidectomy
chemical_list: D008562:Membrane Glycoproteins; D013954:Thyroglobulin; D009195:Peroxidase