Cited by 205

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Maturation and Pro-peptide Cleavage of β-Secretase

Capell, Anja, Steiner, Harald, Willem, Michael, Kaiser, Hartmut, Meyer, Carmen, Walter, Jochen, Lammich, Sven, Multhaup, Gerd, Haass, Christian·2000·Journal of Biological Chemistry

Abstract

Amyloid beta-peptide is generated by two sequential proteolytic cleavages mediated by beta-secretase (BACE) and gamma-secretase. BACE was recently identified as a membrane-associated aspartyl protease. We have now analyzed the maturation and pro-peptide cleavage of BACE. Pulse-chase experiments revealed that BACE is post-translationally modified during transport to the cell surface, which can be monitored by a significant increase in the molecular mass. The increase in molecular mass is caused by complex N-glycosylation. Treatment with tunicamycin and N-glycosidase F led to a BACE derivative with a molecular weight corresponding to an unmodified version. In contrast, the mature form of BACE was resistant to endoglycosidase H treatment. The cytoplasmic tail of BACE was required for efficient maturation and trafficking through the Golgi; a BACE variant lacking the cytoplasmic tail undergoes inefficient maturation. In contrast a soluble BACE variant that does not contain a membrane anchor matured more rapidly than full-length BACE. Pro-BACE was predominantly located within the endoplasmic reticulum. Pro-peptide cleavage occurred immediately before full maturation and trafficking through the Golgi.

Overview

Integrity signals

Registry

Crossref · 10.1074/jbc.m003202200

Cites

4 of 4 references verified0 citation errors · 0 not checkable

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  • Overexpression of BACE1 strongly increases β-secretory cleavage of APP already in early secretory compartments.

    “Indeed, it has been shown that overexpression of BACE1 strongly increases ␤-secretory cleavage of APP already in early secretory compartments (Capell et al., 2000;Liu et al., 2002;Lee et al., 2005)”

Citations

Cites

Flagged first, then by citations

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Metadata

Authors
Capell, A., Steiner, H., Willem, M., Kaiser, H., Meyer, C., Walter, J., Lammich, S., Multhaup, G., & Haass, C.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2000-10
Volume
275
Issue
40
Pages
30849-30854
ISSN
0021-9258
Cited by
205
References
4
Language
en

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