Literature DB >> 15203250

Antigenicity and immunogenicity of the C-terminal peptide of human thyroglobulin.

Rabii Ameziane El Hassani1, Valérie Estienne, Stéphanie Blanchin, Josée-Martine Durand-Gorde, Bernard Mallet, Catherine De Micco, Pierre Carayon, Khalid Lalaoui, Jean Ruf.   

Abstract

Thyroglobulin (Tg) is cleaved into several peptides during thyroid hormone synthesis, an oxidative process. P40, an iodinated C-terminal peptide from human Tg, has a molecular weight of about 40 kDa and contains two hormonogenic sites. P40 is the smallest peptide that is still recognized by monoclonal antibodies from mice immunized with human Tg directed against its immunodominant region. Since P40 also contains several T-cell epitopes, it is a good candidate for studying the primary events involved in the process of hormone synthesis leading to thyroid autoimmunity. The present results show that P40 is recognized by Tg antibodies from patients with thyroid disorders and induces Tg antibodies in CBA mice. P40 may therefore be involved in the autoimmune process, thus providing a useful tool for diagnostic and therapeutic purposes.

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Year:  2004        PMID: 15203250     DOI: 10.1016/j.peptides.2004.03.020

Source DB:  PubMed          Journal:  Peptides        ISSN: 0196-9781            Impact factor:   3.750


  2 in total

1.  Fine epitope mapping within the pathogenic thyroglobulin peptide 2340-2359: minimal epitopes retaining antigenicity across various MHC haplotypes are not necessarily immunogenic.

Authors:  Aikaterini Hatzioannou; Maria Alevizaki; George Carayanniotis; Peggy Lymberi
Journal:  Immunology       Date:  2012-03       Impact factor: 7.397

2.  A novel pathogenic peptide of thyroglobulin (2208-2227) induces autoreactive T-cell and B-cell responses in both high and low responder mouse strains.

Authors:  Ioannis Kanistras; Aikaterini Hatzioannou; Peggy Lymberi
Journal:  Immunology       Date:  2014-06       Impact factor: 7.397

  2 in total

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