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Volume 271, Number 51, Issue of December 20, 1996 pp. 32825-32833
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Cryptic Antigenic Determinants on the Extracellular Pyruvate Dehydrogenase Complex/Mimeotope Found in Primary Biliary Cirrhosis
A PROBE BY AFFINITY MASS SPECTROMETRY

(Received for publication, June 18, 1996, and in revised form, September 12, 1996)

Tai-Tung Yip ^§ , Judy Van de Water ^¶ , M. Eric Gershwin ^¶ , Ross L. Coppel and T. William Hutchens

From the  Department of Food Science and Technology and the ^¶ Department of Rheumatology, Allergy and Clinical Immunology, University of California Davis, School of Medicine, Davis, California 95616, ^§ Molecular Analytical Systems, Davis, California 95616, and the Department of Microbiology, Monash University, Victoria, Australia 3168

Affinity mass spectrometry (AMS) was used to evaluate the structural diversity of the E2 component of pyruvate dehydrogenase complex (PDC) in normal and diseased liver cells, including those from patients with the autoimmune disease primary biliary cirrhosis (PBC). Two different antibodies to PDC-E2, the immunodominant mitochondrial autoantigen in patients with PBC, were used. AMS was performed directly on frozen liver sections and purified bile duct epithelial cells. Mass spectrometric signals associated with the molecular recognition of PBC-specific antigenic determinants were enhanced by an in situ enzyme-linked signal amplification process. Samples from patients with PBC gave strong positive signals for the antigen(s) recognized by the monoclonal antibody C355.1. Conversely, tissues from normal and disease controls showed only a minimal signal. AMS was used to identify specific antigenic determinants within the E2 component of PDC for comparison with unknown antigenic determinants observed by affinity capture with C355.1 monoclonal antibody from PBC samples. PDC components bound to C355.1 were mapped and identified by mass before dissociation from the E2 component. A similar approach was used to identify unknown antigenic determinants associated with PBC. We believe AMS may be an important new approach with wide application to the identification of molecules associated with a number of disease states.

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