Gutenberg Open Science: Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-7995

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DC Field	Value	Language
dc.contributor.author	Schönherr, Caroline	-
dc.contributor.author	Bien, Jessica	-
dc.contributor.author	Isbert, Simone	-
dc.contributor.author	Wichert, Rielana	-
dc.contributor.author	Prox, Johannes	-
dc.contributor.author	Altmeppen, Hermann	-
dc.contributor.author	Kumar, Sathish	-
dc.contributor.author	Walter, Jochen	-
dc.contributor.author	Lichtenthaler, Stefan F.	-
dc.contributor.author	Weggen, Sascha	-
dc.contributor.author	Glatzel, Markus	-
dc.contributor.author	Becker-Pauly, Christoph	-
dc.contributor.author	Pietrzik, Claus	-
dc.date.accessioned	2022-10-14T07:06:07Z	-
dc.date.available	2022-10-14T07:06:07Z	-
dc.date.issued	2016
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/8010	-
dc.description.abstract	BACKGROUND: The metalloprotease meprin β cleaves the Alzheimer's Disease (AD) relevant amyloid precursor protein (APP) as a β-secretase reminiscent of BACE-1, however, predominantly generating N-terminally truncated Aβ2-x variants. RESULTS: Herein, we observed increased endogenous sAPPα levels in the brains of meprin β knock-out (ko) mice compared to wild-type controls. We further analyzed the cellular interaction of APP and meprin β and found that cleavage of APP by meprin β occurs prior to endocytosis. The N-terminally truncated Aβ2-40 variant shows increased aggregation propensity compared to Aβ1-40 and acts even as a seed for Aβ1-40 aggregation. Additionally, we observed that different APP mutants affect the catalytic properties of meprin β and that, interestingly, meprin β is unable to generate N-terminally truncated Aβ peptides from Swedish mutant APP (APPswe). CONCLUSION: Concluding, we propose that meprin β may be involved in the generation of N-terminally truncated Aβ2-x peptides of APP, but acts independently from BACE-1.	en_GB
dc.description.sponsorship	DFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin	de
dc.language.iso	eng	de
dc.rights	CC BY	*
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	*
dc.subject.ddc	610 Medizin	de_DE
dc.subject.ddc	610 Medical sciences	en_GB
dc.title	Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-7995	-
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 04 Medizin	de
jgu.organisation.number	2700	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	Molecular neurodegeneration	de
jgu.journal.volume	11	de
jgu.pages.alternative	Art. 19	de
jgu.publisher.year	2016	-
jgu.publisher.name	BioMed Central	de
jgu.publisher.place	London	de
jgu.publisher.uri	http://dx.doi.org/10.1186/s13024-016-0084-5	de
jgu.publisher.issn	1750-1326	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	610	de
opus.date.modified	2017-05-11T10:27:05Z
opus.subject.dfgcode	00-000
opus.organisation.string	FB 04: Medizin: Institut für Physiologische Chemie und Pathobiochemie	de_DE
opus.identifier.opusid	56295
opus.institute.number	0404
opus.metadataonly	false
opus.type.contenttype	Keine	de_DE
opus.type.contenttype	None	en_EN
opus.affiliated	Pietrzik, Claus
jgu.publisher.doi	10.1186/s13024-016-0084-5	de
jgu.organisation.ror	https://ror.org/023b0x485	-
Appears in collections:	DFG-OA-Publizieren (2012 - 2017)

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