当前位置： SCI文献检索 > FEBS LETTERS期刊下所有文献 > Identification of caspases that cleave presenilin-1 and presenilin-2. Five presenilin-1 (PS1) mutations do not alter the sensitivity of PS1 to caspases.

Identification of caspases that cleave presenilin-1 and presenilin-2. Five presenilin-1 (PS1) mutations do not alter the sensitivity of PS1 to caspases.

Abstract：

:Mutations in the presenilin (PS) genes PSI and PS2 are involved in Alzheimer's disease (AD). Recently, apoptosis-associated cleavage of PS proteins was identified. Here we demonstrate that PS1 as well as PS2 are substrates for different members of the caspase protein family. Remarkably, the caspases acting on PS1 could be subdivided in two groups. One group, containing caspase-8, -6 and -11, cleaved PSI after residues ENDD329 and to a lesser extent after residues AQRD341. A second group consisting of caspase-3, -7 and -1 acted uniquely on AQRD341. Importantly, these two cleavage sites were also recognized by caspases in the C-terminal PS1 fragment produced by constitutive proteolysis. In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. Caspase-8 and -3 exhibited the highest proteolytic activity on both PS1 and PS2. PS1 and PS2 were not hydrolyzed by caspase-2 and PS2 also not by caspase-11. None of five missense mutations affected the sensitivity of PSI to caspase-mediated cleavage. This suggests that AD pathogenesis associated with PS1 missense mutations cannot be explained by a change in caspase-dependent processing.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

van de Craen M,de Jonghe C,van den Brande I,Declercq W,van Gassen G,van Criekinge W,Vanderhoeven I,Fiers W,van Broeckhoven C,Hendriks L,Vandenabeele P

doi

10.1016/s0014-5793(99)00108-8

keywords:

subject

Has Abstract

pub_date

1999-02-19 00:00:00

pages

149-54

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)00108-8

journal_volume

445

pub_type

杂志文章

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