MALDI-mass spectrometry imaging identifies vitronectin as a common constituent of amyloid deposits.

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.

• Authors: Martin Winter, Andreas Tholey, Sandra Krüger, Hartmut Schmidt, Christoph Röcken
• Journal: The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society (J Histochem Cytochem) Vol. 63 Issue 10 Pg. 772-9 (10 2015) ISSN: 1551-5044 [Electronic] United States
• PMID: 26101327 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: © The Author(s) 2015.

Chemical References

• Amyloid
• Vitronectin

Topics

• Adult
• Aged
• Aged, 80 and over
• Amyloid (chemistry)
• Amyloidosis (pathology)
• Brain (pathology)
• Female
• Humans
• Immunohistochemistry (methods)
• Intestine, Large (pathology)
• Kidney (pathology)
• Liver (pathology)
• Male
• Middle Aged
• Paraffin Embedding (methods)
• Plaque, Amyloid (pathology)
• Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (methods)
• Tissue Fixation (methods)
• Vitronectin (analysis)
• Young Adult