Gelatinase A possesses a β‐secretase‐like activity in cleaving the amyloid protein precursor of Alzheimer's disease

FEBS Letters

Fosang, Amanda J.⁴  Fuller, Stephanie J.²  Beyreuther, Konrad³  Evin, Geneviève²  LePage, Rex N.⁵  Murphy, Gillian¹  Masters, Colin L.²  Small, David H.⁵ 

[1] Strangeways Research Laboratory, Cambridge CB1 4RN, UK;Department of Pathology, University of Melbourne, Parkville, Vic. 3052, Australia;Centre for Molecular Biology, University of Heidelberg, Heidelberg, Germany;Orthopaedic Molecular Biology Research Unit, Department of Paediatrics, University of Melbourne, Parkville, Vic. 3052, Australia;Laboratory of Molecular Neurobiology, Melbourne Nerve Growth Research Unit, University of Melbourne, Parkville, Vic. 3052, Australia

关键词: Alzheimer's disease;    Amyloid;    Gelatinase;    Secretase;    Protease;    βA4;    amyloid protein;    AD;    Alzheimer's disease;    APP;    amyloid protein precursor;    APMA;    4-aminophenylmercuric acetate;   

DOI  :  10.1016/0014-5793(95)01358-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ability of the 72 kDa gelatinase A to cleave the amyloid protein precursor (APP) was investigated. HeLa cells were transfected with an APP₆₉₅ plasmid. The cells were incubated with gelatinase A, which cleaved the 110 kDa cell-surface APP, releasing a 100 kDa form of the protein. A peptide homologous to the β-secretase site was cleaved by gelatinase A adjacent to a glutamate residue at position −3 (βA4 numbering system). A peptide homologous to the α-secretase site was not cleaved. The results demonstrate that 72 kDa gelatinase A is not an α-secretase, but that it may have a β-secretase activity.

【 授权许可】

Unknown