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Antibodies 2014, 3(1), 169-181;

Characterization Analysis of Human Anti-Ferritin Autoantibodies

Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Aomori 034-8628, Japan
Author to whom correspondence should be addressed.
Received: 6 February 2014 / Revised: 11 March 2014 / Accepted: 12 March 2014 / Published: 21 March 2014
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Anti-ferritin autoantibodies are found in many animals. Human ferritin-binding proteins (FBPs) were partially purified from human serum by ion-exchange chromatography and immobilized metal affinity chromatography with Zn2+. Crude FBPs were immunocoprecipitated with canine liver ferritin followed by the addition of anti-ferritin antibodies. Immunoglobulins in the immunocoprecipitate were detected with antibodies specific for human IgG, IgM or IgA heavy chains, and immunoglobulins IgG, IgM and IgA to bind to expressed recombinant human H and L chain homopolymers were also found. A portion of human serum proteins bound to zinc ions immobilized on beads were released upon the addition of canine liver ferritin, and the released protein was identified as IgM antibody. Additionally, the released proteins recognized peptide sequence (DPHLCDF) commonly found in amino acid sequences of mammalian ferritin H and L subunits. These results suggest that human serum contains anti-ferritin autoantibodies (IgG, IgM and IgA) which bind zinc ions and preferentially bind ferritin over both the H and L subunits, and that a portion of, but not all, the IgM antibodies bound to ferritin with higher affinity than to zinc ions and may recognize the common sequence found in mammalian ferritin H and L subunits. View Full-Text
Keywords: anti-ferritin autoantibody; ferritin; H subunit; L subunit; zinc ion anti-ferritin autoantibody; ferritin; H subunit; L subunit; zinc ion

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Higashi, S.; Nagasawa, K.; Yoshikawa, Y.; Watanabe, K.; Orino, K. Characterization Analysis of Human Anti-Ferritin Autoantibodies. Antibodies 2014, 3, 169-181.

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