{"entity": "publication", "iuid": "1b3e1cd5018f4757851a77e4a6358e1a", "timestamp": "2026-09-10T00:56:37.626Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/1b3e1cd5018f4757851a77e4a6358e1a.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/1b3e1cd5018f4757851a77e4a6358e1a"}}, "title": "Deposition of C-terminally truncated A\u03b2 species A\u03b237 and A\u03b239 in Alzheimer's disease and transgenic mouse models.", "authors": [{"family": "Reinert", "given": "Jochim", "initials": "J"}, {"family": "Richard", "given": "Bernhard C", "initials": "BC"}, {"family": "Klafki", "given": "Hans W", "initials": "HW"}, {"family": "Friedrich", "given": "Beate", "initials": "B"}, {"family": "Bayer", "given": "Thomas A", "initials": "TA"}, {"family": "Wiltfang", "given": "Jens", "initials": "J"}, {"family": "Kovacs", "given": "Gabor G", "initials": "GG"}, {"family": "Ingelsson", "given": "Martin", "initials": "M"}, {"family": "Lannfelt", "given": "Lars", "initials": "L"}, {"family": "Paetau", "given": "Anders", "initials": "A"}, {"family": "Bergquist", "given": "Jonas", "initials": "J"}, {"family": "Wirths", "given": "Oliver", "initials": "O"}], "type": "journal article", "published": "2016-03-08", "journal": {"title": "Acta Neuropathol Commun", "issn": "2051-5960", "volume": "4", "pages": "24", "issn-l": null}, "abstract": "In Alzheimer's disease (AD) a variety of amyloid \u03b2-peptides (A\u03b2) are deposited in the form of extracellular diffuse and neuritic plaques (NP), as well as within the vasculature. The generation of A\u03b2 from its precursor, the amyloid precursor protein (APP), is a highly complex procedure that involves subsequent proteolysis of APP by \u03b2- and \u03b3-secretases. Brain accumulation of A\u03b2 due to impaired A\u03b2 degradation and/or altered ratios between the different A\u03b2 species produced is believed to play a pivotal role in AD pathogenesis. While the presence of A\u03b240 and A\u03b242 in vascular and parenchymal amyloid have been subject of extensive studies, the deposition of carboxyterminal truncated A\u03b2 peptides in AD has not received comparable attention. In the current study, we for the first time demonstrate the immunohistochemical localization of A\u03b237 and A\u03b239 in human sporadic AD (SAD). Our study further included the analysis of familial AD (FAD) cases carrying the APP mutations KM670/671NL, E693G and I716F, as well as a case of the PSEN1 \u0394Exon9 mutation. A\u03b237 and A\u03b239 were found to be widely distributed within the vasculature in the brains of the majority of studied SAD and FAD cases, the latter also presenting considerable amounts of A\u03b237 containing NPs. In addition, both peptides were found to be present in extracellular plaques but only scarce within the vasculature in brains of a variety of transgenic AD mouse models. Taken together, our study indicates the importance of C-terminally truncated A\u03b2 in sporadic and familial AD and raises questions about how these species are generated and regulated.", "doi": "10.1186/s40478-016-0294-7", "pmid": "26955942", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC4784385"}, {"db": "pii", "key": "10.1186/s40478-016-0294-7"}], "notes": [], "created": "2026-08-21T12:41:40.493Z", "modified": "2026-08-21T12:41:40.519Z"}