Abstract:
:The majority of cases of early-onset familial Alzheimer disease are caused by mutations in the recently identified presenilin 1 (PS1) gene, located on chromosome 14. PS1, a 467 amino acid protein, is predicted to be an integral membrane protein containing seven putative transmembrane domains and a large hydrophilic loop between the sixth and seventh membrane-spanning domain. We produced 7 monoclonal antibodies that react with 3 non-overlapping epitopes on the N-terminal hydrophilic tail of PS1. The monoclonal antibodies can detect the full-size PS1 at Mr 47000 and a more abundant Mr 28000 product in membrane extracts from human brain and human cell lines. PC12 cells transiently transfected with PS1 constructs containing two different Alzheimer mutations fail to generate the 28 kDa degradation product in contrast to PC12 cells transfected with wild-type PS1. Our results indicate that missense mutations in this form of familial Alzheimer disease may act via a mechanism of impaired proteolytic processing of PS1.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Mercken M,Takahashi H,Honda T,Sato K,Murayama M,Nakazato Y,Noguchi K,Imahori K,Takashima Adoi
10.1016/0014-5793(96)00608-4subject
Has Abstractpub_date
1996-07-08 00:00:00pages
297-303issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(96)00608-4journal_volume
389pub_type
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