Thyroid microsomal/thyroid peroxidase autoantibodies show discrete patterns of cross-reactivity to myeloperoxidase, lactoperoxidase and horseradish peroxidase

Immunology. 1989 Jun;67(2):197-204.

Abstract

The recent cloning of the thyroid peroxidase (TPO) has shown that it is identical to the thyroid microsomal antigen (TMA), a potent antigen involved in autoimmune thyroid disease (ATD), which shares significant sequence homology with myeloperoxidase. The present study shows that autoantibodies (aAb) to the TMA/TPO antigen cross-react with human leucocyte myeloperoxidase, bovine lactoperoxidase and horseradish peroxidase. Cross-reactivity to myeloperoxidase was only apparent by ELISA using reduced and alkylated antigen preparations or by immunoblotting following denaturation with SDS. Sequential absorption of sera on SDS-denatured thyroid microsomes immobilized on Sepharose-4B followed by absorption on native microsomes removed all aAb specificities to TMA/TPO and the three peroxidase preparations, giving compelling evidence on the genuine cross-reactive nature of these aAbs. Sera from different patients contain different qualitative and quantitative specificities of aAb to the TMA/TPO antigen, confirming the polyclonal nature of this autoimmune response.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Absorption
  • Autoantibodies / immunology*
  • Binding Sites, Antibody
  • Cross Reactions
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme-Linked Immunosorbent Assay
  • Horseradish Peroxidase / immunology
  • Humans
  • Immunoblotting
  • Iodide Peroxidase / immunology*
  • Lactoperoxidase / immunology
  • Microsomes / immunology*
  • Peroxidase / immunology
  • Sodium Dodecyl Sulfate
  • Thyroiditis, Autoimmune / immunology*

Substances

  • Autoantibodies
  • thyroid microsomal antibodies
  • Sodium Dodecyl Sulfate
  • Horseradish Peroxidase
  • Lactoperoxidase
  • Peroxidase
  • Iodide Peroxidase