HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Estienne, V. Articles by Ruf, J. Search for Related Content PubMed PubMed Citation Articles by Estienne, V. Articles by Ruf, J. Social Bookmarking                      What's this?

J Biol Chem, Vol. 273, Issue 14, 8056-8062, April 3, 1998

A Conformational B-cell Epitope on the C-terminal End of the Extracellular Part of Human Thyroid Peroxidase

From the Unit 38 of INSERM and the Laboratoire de Biochimie Endocrinienne et Métabolique, Faculté de Médecine, 27, boulevard Jean Moulin, F-13385 Marseille Cedex 5, France

To investigate the B-cell autoimmune epitopes on human thyroid peroxidase (TPO), we generated proteolytic peptides by enzymatic hydrolysis of TPO in nondenaturing and nonreducing conditions. The hydrolysate was chromatographed on a reverse phase column. We eluted a material immunoreactive with both a TPO monoclonal antibody recognizing a linear epitope (mAb47, amino acid 713-721) and TPO autoantibodies (aAb) from patients. The aAb immunoreactivity, but not that of mAb47, was lost after reduction. Western blots after electrophoresis without reduction showed that the aAb and mAb47 were immunoreactive with a 66-kDa band and that aAb identified a doublet at 20 kDa. For electrophoresis under reducing conditions, the 66-kDa band resolved into two peptides of 40 and 26 kDa, whereas the doublet at 20 kDa remained unchanged. None of these reduced peptides was immunoreactive with aAb, whereas the 40-kDa peptide was immunoreactive with mAb47. The 40-kDa peptide extends from amino acid 549 to 933 of TPO, and its last 192 amino acids overlap the autoimmune 20-kDa peptide. After iodine labeling, the 20-kDa peptide lost its immunoreactivity. We conclude that the C-terminal end of the extracellular part of TPO, which includes all the tyrosine residues of the 20-kDa peptide, contains at least one conformational B-cell epitope involved in autoimmune thyroid diseases.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				D. Bresson, M. Pugniere, F. Roquet, S. A. Rebuffat, B. N-Guyen, M. Cerutti, J. Guo, S. M. McLachlan, B. Rapoport, V. Estienne, et al. Directed Mutagenesis in Region 713-720 of Human Thyroperoxidase Assigns 713KFPED717 Residues as Being Involved in the B Domain of the Discontinuous Immunodominant Region Recognized by Human Autoantibodies J. Biol. Chem., September 10, 2004; 279(37): 39058 - 39067. [Abstract] [Full Text] [PDF]

				D. Bresson, M. Cerutti, G. Devauchelle, M. Pugniere, F. Roquet, C. Bes, C. Bossard, T. Chardes, and S. Peraldi-Roux Localization of the Discontinuous Immunodominant Region Recognized by Human Anti-thyroperoxidase Autoantibodies in Autoimmune Thyroid Diseases J. Biol. Chem., March 7, 2003; 278(11): 9560 - 9569. [Abstract] [Full Text] [PDF]

				J. Guo, S. M. McLachlan, and B. Rapoport Localization of the Thyroid Peroxidase Autoantibody Immunodominant Region to a Junctional Region Containing Portions of the Domains Homologous to Complement Control Protein and Myeloperoxidase J. Biol. Chem., October 18, 2002; 277(43): 40189 - 40195. [Abstract] [Full Text] [PDF]

				Y. Ma, M. G. Thomas, M. Okamoto, D. P. Bogdanos, S. Nagl, N. Kerkar, A. R. Lopes, L. Muratori, M. Lenzi, F. B. Bianchi, et al. Key Residues of a Major Cytochrome P4502D6 Epitope Are Located on the Surface of the Molecule J. Immunol., July 1, 2002; 169(1): 277 - 285. [Abstract] [Full Text] [PDF]

				V. Estienne, C. Duthoit, S. Blanchin, R. Montserret, J.-M. Durand-Gorde, M. Chartier, D. Baty, P. Carayon, and J. Ruf Analysis of a conformational B cell epitope of human thyroid peroxidase: identification of a tyrosine residue at a strategic location for immunodominance Int. Immunol., April 1, 2002; 14(4): 359 - 366. [Abstract] [Full Text] [PDF]

				J. Guo, X.-M. Yan, S. M. McLachlan, and B. Rapoport Search for the Autoantibody Immunodominant Region on Thyroid Peroxidase: Epitopic Footprinting with a Human Monoclonal Autoantibody Locates a Facet on the Native Antigen Containing a Highly Conformational Epitope J. Immunol., January 15, 2001; 166(2): 1327 - 1333. [Abstract] [Full Text] [PDF]

				Y. Hayashi, Y. Muro, K. Kuriyama, Y. Tomita, and K. Sugimoto Differences in specificities of anti-centromere sera for the monomeric and dimeric C-terminal peptides of human centoromere protein C Int. Immunol., October 1, 2000; 12(10): 1431 - 1437. [Abstract] [Full Text] [PDF]

				P. Hobby, A. Gardas, R. Radomski, A. M. McGregor, J. P. Banga, and B. J. Sutton Identification of an Immunodominant Region Recognized by Human Autoantibodies in a Three-Dimensional Model of Thyroid Peroxidase Endocrinology, June 1, 2000; 141(6): 2018 - 2026. [Abstract] [Full Text] [PDF]

				V. Estienne, C. Blanchet, P. Niccoli-Sire, C. Duthoit, J.-M. Durand-Gorde, C. Geourjon, D. Baty, P. Carayon, and J. Ruf Molecular Model, Calcium Sensitivity, and Disease Specificity of a Conformational Thyroperoxidase B-cell Epitope J. Biol. Chem., December 10, 1999; 274(50): 35313 - 35317. [Abstract] [Full Text] [PDF]