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-?-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-, AL?-, 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.

SUBMITTER: Winter M 

PROVIDER: S-EPMC4823803 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature