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Presenilin 2 mutations alter cystatin C trafficking in mouse primary neurons.

Abstract：

:Mutations in the presenilin genes account for the majority of familial Alzheimer disease (FAD) cases. In the present report we demonstrated that the FAD-linked presenilin 2 mutations (PS2 M239I and T122R) alter cystatin C trafficking in mouse primary neurons reducing secretion of its glycosylated form. These mutations showed a different impact on cystatin C: PS2 T122R had a much stronger effect determining a dramatic intracellular accumulation of cystatin C (native and glycosylated), followed by a reduction in the secretion of both forms. Several experimental evidences suggest that cystatin C exerts a protective role in the brain and favors stem cells proliferation. Confocal imaging showed that the effect of PS2 T122R mutation was a massive recruitment of cystatin C into the neuronal processes, in the presence of an intact cytoskeletal structure. The consequent reduction in the cystatin C extracellular levels might result in a failure of neuroregeneration. Understanding the interplay of PS2 and cystatin C in the pathogenesis of AD might highlight new therapeutic prospective.

journal_name

Neurobiol Aging

journal_title

Neurobiology of aging

authors

Ghidoni R,Benussi L,Paterlini A,Missale C,Usardi A,Rossi R,Barbiero L,Spano P,Binetti G

doi

10.1016/j.neurobiolaging.2006.01.007

subject

Has Abstract

pub_date

2007-03-01 00:00:00

pages

371-6

issue

3

eissn

0197-4580

issn

1558-1497

pii

S0197-4580(06)00039-X

journal_volume

28

pub_type

杂志文章

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