Literature DB >> 1138879

Electron microscopy of low iodinated thyroglobulin molecules.

G Berg, R Ekholm.   

Abstract

Thyroglobulin molecules were studied in the electron microscope with negative staining technique. In a first series of experiments samples of thyroglobulin varying in iodine content from 0.5 to 0.03% were prepared from the thyroids of mice and rats kept on iodine-poor diets. All samples contained thyroglobulin molecules of the normal ovoid shape, not deviating in size or shape from molecules obtained from normal thyroids. However, in addition, another type of molecule having a cylindrical shape was observed in all samples. The proportion of these cylindrical molecules increased from a few per cent in the moderately iodine-poor thyroglobulin samples to more than 80% in the highly iodine-deficient thyroglobulin (0.03%). In a second series of experiments extremely iodine-poor thyroglobulin (smaller than 0.005%) was obtained from propylthiouracil-treated rats. In these preparations practically all molecules had a cylindrical shape. These samples also contained smaller particles interpreted to be dissociation products. The cylindrical molecules were of two types, one appearing compact and measuring 250 times 135 A (length times diameter) and the other appearing porous and having a length of 145 and a diameter of 205 A. It is concluded that the cylindrical molecules represent non- or low-iodinated thyroglobulin and it is suggested that the porous cylindrical molecule is an unfolded form of the compact cylinder.

Entities:  

Mesh:

Substances:

Year:  1975        PMID: 1138879     DOI: 10.1016/0005-2795(75)90285-8

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  6 in total

1.  The cholinesterase-like domain, essential in thyroglobulin trafficking for thyroid hormone synthesis, is required for protein dimerization.

Authors:  Jaemin Lee; Xiaofan Wang; Bruno Di Jeso; Peter Arvan
Journal:  J Biol Chem       Date:  2009-03-09       Impact factor: 5.157

2.  Iodination of murine thyroglobulin enhances autoimmune reactivity in the NOD.H2 mouse.

Authors:  J G Barin; M V Talor; R B Sharma; N R Rose; C L Burek
Journal:  Clin Exp Immunol       Date:  2005-11       Impact factor: 4.330

3.  Iodination of human thyroglobulin (Tg) alters its immunoreactivity. I. Iodination alters multiple epitopes of human Tg.

Authors:  A M Saboori; N R Rose; H S Bresler; M Vladut-Talor; C L Burek
Journal:  Clin Exp Immunol       Date:  1998-08       Impact factor: 4.330

4.  Selective autoimmune response to the chicken-specific structures of thyroglobulin in Obese strain chickens.

Authors:  C T Chan; P G Byfield; B R Champion; R L Himsworth
Journal:  Clin Exp Immunol       Date:  1989-07       Impact factor: 4.330

5.  Thyroglobulin Represents a Novel Molecular Architecture of Vertebrates.

Authors:  Guillaume Holzer; Yoshiaki Morishita; Jean-Baptiste Fini; Thibault Lorin; Benjamin Gillet; Sandrine Hughes; Marie Tohmé; Gilbert Deléage; Barbara Demeneix; Peter Arvan; Vincent Laudet
Journal:  J Biol Chem       Date:  2016-06-16       Impact factor: 5.157

6.  Modelling of Thyroid Peroxidase Reveals Insights into Its Enzyme Function and Autoantigenicity.

Authors:  Sarah N Le; Benjamin T Porebski; Julia McCoey; James Fodor; Blake Riley; Marlena Godlewska; Monika Góra; Barbara Czarnocka; J Paul Banga; David E Hoke; Itamar Kass; Ashley M Buckle
Journal:  PLoS One       Date:  2015-12-01       Impact factor: 3.240

  6 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.