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* Department of Neurology and Neuroscience, Cornell University, New York, NY 10021;
Department of Medicine and
Institute of Human Nutrition, Columbia University, New York, NY 10032;
Department of Neurosciences, University of Padova, Padova, Italy;
¶ Bioinformatics and Scientific Information Technology Program, Office of Technology Information Systems, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892;
|| Human Motor Control Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892; and
# Department of Neurology, St. Vincent’s Hospital Manhattan, New York, NY 10011
Celiac disease is an immune-mediated disorder triggered by ingestion of wheat gliadin and related proteins in genetically susceptible individuals. In addition to the characteristic enteropathy, celiac disease is associated with various extraintestinal manifestations, including neurologic complications such as neuropathy, ataxia, seizures, and neurobehavioral changes. The cause of the neurologic manifestations is unknown, but autoimmunity resulting from molecular mimicry between gliadin and nervous system proteins has been proposed to play a role. In this study, we sought to investigate the immune reactivity of the anti-gliadin Ab response toward neural proteins. We characterized the binding of affinity-purified anti-gliadin Abs from immunized animals to brain proteins by one- and two-dimensional gel electrophoresis, immunoblotting, and peptide mass mapping. The major immunoreactive protein was identified as synapsin I. Anti-gliadin Abs from patients with celiac disease also bound to the protein. Such cross-reactivity may provide clues into the pathogenic mechanism of the neurologic deficits that are associated with gluten sensitivity.
The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
1 This work was supported in part by an award from the National Ataxia Foundation (to A.A.).
2 Address correspondence and reprint requests to Dr. Armin Alaedini, Department of Neurology and Neuroscience, Cornell University, 1300 York Avenue, New York, NY 10021. E-mail address: ara2004{at}med.cornell.edu
3 Abbreviations used in this paper: TFMS, trifluoromethanesulfonic acid; MS/MS, tandem mass spectrometry.
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