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The underlying mechanisms of the disease have not been fully elucidated yet. Matrix\u2010assisted laser desorption\/ionization mass spectrometry imaging (MALDI\u2010MSI) allows the spatial information of proteins to be obtained upon the tissue sections without homogenisation. In this study, we aimed to examine proteomic alterations in the brain tissue of an HD mouse model with MALDI\u2010MSI coupled to LC\u2013MS\/MS system. We used 3\u2010, 6\u2010 and 12\u2010month\u2010old YAC128 mice representing pre\u2010stage, mild stage and pathological stage of the HD and their non\u2010transgenic littermates, respectively. The intensity levels of 89 proteins were found to be significantly different in YAC128 in comparison to their control mice in the pre\u2010stage, 83 proteins in the mild stage, and 82 proteins in the pathological stage. Among them, Tau, EF2, HSP70, and NogoA proteins were validated with western blot analysis. In conclusion, the results of this study have provided remarkable new information about the spatial proteomic alterations in the HD mouse model, and we suggest that MALDI\u2010MSI is an excellent technique for identifying such regional proteomic changes and could offer new perspectives in examining complex diseases.<\/jats:p>","DOI":"10.1111\/ejn.16103","type":"journal-article","created":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T02:24:38Z","timestamp":1690856678000},"page":"2985-3002","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Detection of proteomic alterations at different stages in a Huntington's disease mouse model via matrix\u2010assisted laser desorption\/ionization mass spectrometry (MALDI\u2010MS) 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