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    Constitutive and Inflammatory Immunopeptidome of Pancreatic beta-Cells

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    Author
    Dudek, NL; Tan, CT; Gorasia, DG; Croft, NP; Illing, PT; Purcell, AW
    Date
    2012-11-01
    Source Title
    Diabetes
    Publisher
    AMER DIABETES ASSOC
    University of Melbourne Author/s
    Dudek, Nadine; Gorasia, Dhana; CROFT, NATHAN; PURCELL, ANTHONY; TAN, CHOR; ILLING, PATRICIA
    Affiliation
    Academic Services and Registrar
    Melbourne Dental School
    Biochemistry and Molecular Biology
    Microbiology and Immunology
    Metadata
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    Document Type
    Journal Article
    Citations
    Dudek, N. L., Tan, C. T., Gorasia, D. G., Croft, N. P., Illing, P. T. & Purcell, A. W. (2012). Constitutive and Inflammatory Immunopeptidome of Pancreatic beta-Cells. DIABETES, 61 (11), pp.3018-3025. https://doi.org/10.2337/db11-1333.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/264709
    DOI
    10.2337/db11-1333
    Abstract
    Type 1 diabetes is characterized by the autoimmune destruction of pancreatic β-cells. Recognition of major histocompatibility complex (MHC)-bound peptides is critical for both the initiation and progression of disease. In this study, MHC peptide complexes were purified from NIT-1 β-cells, interferon-γ (IFN-γ)-treated NIT-1 cells, splenic and thymic tissue of 12-week-old NOD mice, and peptides identified by mass spectrometry. In addition to global liquid chromatography-tandem mass spectrometry analysis, the targeted approach of multiple-reaction monitoring was used to quantitate the immunodominant K(d)-restricted T-cell epitope islet-specific glucose-6-phosphatase catalytic subunit-related protein (IGRP)₂₀₆₋₂₁₄. We identified >2,000 MHC-bound peptides; 1,100 of these presented by β-cells grown under normal conditions or after exposure to IFN-γ. These include sequences from a number of known autoantigens. Quantitation of IGRP₂₀₆₋₂₁₄ revealed low-level presentation by K(d) (~25 complexes/cell) on NIT-1 cells after IFN-γ treatment compared with the simultaneous presentation of the endogenously processed K(d)-restricted peptide Janus kinase-1₃₅₅₋₃₆₃ (~15,000 copies/cell). We have successfully sequenced peptides from NIT-1 β-cells under basal and inflammatory conditions. We have shown the feasibility of quantitating disease-associated peptides and provide the first direct demonstration of the disparity between presentation of a known autoantigenic epitope and a common endogenously presented peptide.

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