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

Standard

Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site. / Schönherr, Caroline; Bien, Jessica; Isbert, Simone; Wichert, Rielana; Prox, Johannes; Altmeppen, Hermann; Kumar, Sathish; Walter, Jochen; Lichtenthaler, Stefan F; Weggen, Sascha; Glatzel, Markus; Becker-Pauly, Christoph; Pietrzik, Claus U.

in: MOL NEURODEGENER, Jahrgang 11, Nr. 1, 19.02.2016, S. 19.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Schönherr, C, Bien, J, Isbert, S, Wichert, R, Prox, J, Altmeppen, H, Kumar, S, Walter, J, Lichtenthaler, SF, Weggen, S, Glatzel, M, Becker-Pauly, C & Pietrzik, CU 2016, 'Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site', MOL NEURODEGENER, Jg. 11, Nr. 1, S. 19. https://doi.org/10.1186/s13024-016-0084-5

APA

Schönherr, C., Bien, J., Isbert, S., Wichert, R., Prox, J., Altmeppen, H., Kumar, S., Walter, J., Lichtenthaler, S. F., Weggen, S., Glatzel, M., Becker-Pauly, C., & Pietrzik, C. U. (2016). Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site. MOL NEURODEGENER, 11(1), 19. https://doi.org/10.1186/s13024-016-0084-5

Vancouver

Schönherr C, Bien J, Isbert S, Wichert R, Prox J, Altmeppen H et al. Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site. MOL NEURODEGENER. 2016 Feb 19;11(1):19. https://doi.org/10.1186/s13024-016-0084-5

Bibtex

@article{53a7bfa8f6984f86a12803e481002d5c,
title = "Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site",
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.",
author = "Caroline Sch{\"o}nherr and Jessica Bien and Simone Isbert and Rielana Wichert and Johannes Prox and Hermann Altmeppen and Sathish Kumar and Jochen Walter and Lichtenthaler, {Stefan F} and Sascha Weggen and Markus Glatzel and Christoph Becker-Pauly and Pietrzik, {Claus U}",
year = "2016",
month = feb,
day = "19",
doi = "10.1186/s13024-016-0084-5",
language = "English",
volume = "11",
pages = "19",
journal = "MOL NEURODEGENER",
issn = "1750-1326",
publisher = "BioMed Central Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site

AU - Schönherr, Caroline

AU - Bien, Jessica

AU - Isbert, Simone

AU - Wichert, Rielana

AU - Prox, Johannes

AU - Altmeppen, Hermann

AU - Kumar, Sathish

AU - Walter, Jochen

AU - Lichtenthaler, Stefan F

AU - Weggen, Sascha

AU - Glatzel, Markus

AU - Becker-Pauly, Christoph

AU - Pietrzik, Claus U

PY - 2016/2/19

Y1 - 2016/2/19

N2 - 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.

AB - 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.

U2 - 10.1186/s13024-016-0084-5

DO - 10.1186/s13024-016-0084-5

M3 - SCORING: Journal article

C2 - 26895626

VL - 11

SP - 19

JO - MOL NEURODEGENER

JF - MOL NEURODEGENER

SN - 1750-1326

IS - 1

ER -