MALDI-Mass Spectrometry Imaging Identifies Vitronectin as a Common Constituent of Amyloid Deposits |
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Authors: | Martin Winter Andreas Tholey Sandra Krüger Hartmut Schmidt Christoph R?cken |
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Institution: | Department of Pathology (MW, SK, CR);Research Group Systematic Proteome Research, Institute of Experimental Medicine (AT);Christian-Albrechts-University, Kiel, Germany (AT);Department of Transplant Medicine, University Hospital Münster, Münster, Germany (HS) |
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Abstract: | Amyloids are pathological intra- and extracellular fibrillar aggregates of polypeptides with a cross-β-sheet structure and characteristic tinctorial properties. The amyloid deposits commonly enclose several non-fibrillar components of the extracellular matrix. Their potential to regulate the formation and aggregation process of amyloid fibrils is still poorly understood. For a better understanding of the role of the extracellular matrix in amyloidosis, it is essential to gain deeper insights into the composition of amyloid deposits. Here, we utilized matrix-assisted laser desorption and ionization mass spectrometry imaging to identify extracellular matrix compounds in amyloid deposits. Using this technique, we identified and determined the spatial distribution of vitronectin within AApoAI-, ALλ-, ATTR- and AIns amyloid deposits and, using immunohistochemistry, validated the spatial overlap of vitronectin with amyloids in 175 cases with diverse types of amyloid in several different tissues. |
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Keywords: | amyloid formalin-fixed/paraffin-embedded tissue immunohistochemistry matrix-assisted laser desorption/ionization mass spectrometry imaging vitronectin |
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