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Liepold, Thomas
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Liepold, Thomas
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Liepold, Thomas
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Liepold, T.
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2019Journal Article [["dc.bibliographiccitation.firstpage","849"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","858"],["dc.bibliographiccitation.volume","67"],["dc.contributor.author","Hornung, Karen"],["dc.contributor.author","Zampar, Silvia"],["dc.contributor.author","Engel, Nadine"],["dc.contributor.author","Klafki, Hans"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2020-12-10T18:44:12Z"],["dc.date.available","2020-12-10T18:44:12Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.3233/JAD-181134"],["dc.identifier.eissn","1875-8908"],["dc.identifier.issn","1387-2877"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78365"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","N-Terminal Truncated Aβ4-42 Is a Substrate for Neprilysin Degradation in vitro and in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI2022Journal Article [["dc.bibliographiccitation.firstpage","578"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","589"],["dc.bibliographiccitation.volume","160"],["dc.contributor.affiliation","Wirths, Oliver; 1\r\nDepartment of Psychiatry and Psychotherapy\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.affiliation","Mollenhauer, Brit; 2\r\nDepartment of Neurology\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.affiliation","Liepold, Thomas; 4\r\nMax Planck Institute of Experimental Medicine\r\nProteomics Group\r\nGoettingen Germany"],["dc.contributor.affiliation","Rieper, Petra; 1\r\nDepartment of Psychiatry and Psychotherapy\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.affiliation","Esselmann, Hermann; 1\r\nDepartment of Psychiatry and Psychotherapy\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.affiliation","Vogelgsang, Jonathan; 1\r\nDepartment of Psychiatry and Psychotherapy\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.affiliation","Wiltfang, Jens; 1\r\nDepartment of Psychiatry and Psychotherapy\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.author","Klafki, Hans‐Wolfgang"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Rieper, Petra"],["dc.contributor.author","Esselmann, Hermann"],["dc.contributor.author","Vogelgsang, Jonathan"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Jahn, Olaf"],["dc.date.accessioned","2022-02-01T10:31:26Z"],["dc.date.available","2022-02-01T10:31:26Z"],["dc.date.issued","2022"],["dc.date.updated","2022-06-15T00:17:43Z"],["dc.description.abstract","Abstract Neurochemical biomarkers can support the diagnosis of Alzheimer’s disease and may facilitate clinical trials. In blood plasma, the ratio of the amyloid‐β (Aβ) peptides Aβ−3–40/Aβ1–42 can predict cerebral amyloid‐β pathology with high accuracy (Nakamura et al., 2018). Whether or not Aβ−3–40 (aka. amyloid precursor protein (APP) 669–711) is also present in cerebrospinal fluid (CSF) is not clear. Here, we investigated whether Aβ−3–40 can be detected in CSF and to what extent the CSF Aβ−3–40/Aβ42 ratio is able to differentiate between individuals with or without amyloid‐β positron emission tomography (PET) evidence of brain amyloid. The occurrence of Aβ−3–40 in human CSF was assessed by immunoprecipitation followed by mass spectrometry. For quantifying the CSF concentrations of Aβ−3–40 in 23 amyloid PET‐negative and 17 amyloid PET‐positive subjects, we applied a sandwich‐type immunoassay. Our findings provide clear evidence of the presence of Aβ−3–40 and Aβ−3–38 in human CSF. While there was no statistically significant difference in the CSF concentration of Aβ−3–40 between the two diagnostic groups, the CSF Aβ−3–40/Aβ42 ratio was increased in the amyloid PET‐positive individuals. We conclude that Aβ−3–40 appears to be a regular constituent of CSF and may potentially serve to accentuate the selective decrease in CSF Aβ42 in Alzheimer's disease. image"],["dc.description.abstract","Cerebral amyloid‐β pathology can be predicted by the Aβ−3–40/Aβ1–42 peptide ratio in blood plasma (Nakamura et al., 2018, Nature 554, 249). However, it is still unclear whether Aβ−3–x peptides occur in cerebrospinal fluid (CSF). By immunoprecipitation‐mass spectrometry (IP‐MS), we show that Aβ−3–40 and Aβ−3–38 are regular constituents of CSF. The CSF Aβ−3–40/Aβ42 ratio, measured with a sandwich immunoassay, was found to be increased in individuals with positron emission tomography (PET) evidence of brain amyloid. Thus, CSF Aβ−3–40 may serve to accentuate the selective decrease in CSF Aβ42 in Alzheimer's disease. image"],["dc.identifier.doi","10.1111/jnc.15571"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/98861"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-517"],["dc.relation.eissn","1471-4159"],["dc.relation.issn","0022-3042"],["dc.rights","This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes."],["dc.rights.uri","http://creativecommons.org/licenses/by-nc/4.0/"],["dc.title","Detection and quantification of Aβ−3–40 (APP669‐711) in cerebrospinal fluid"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI