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Gelatinase A possesses a β‐secretase‐like activity in cleaving the amyloid protein precursor of Alzheimer's disease
Author(s) -
LePage Rex N.,
Fosang Amanda J.,
Fuller Stephanie J.,
Murphy Gillian,
Evin Geneviève,
Beyreuther Konrad,
Masters Colin L.,
Small David H.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01358-x
Subject(s) - amyloid precursor protein secretase , amyloid precursor protein , chemistry , protein precursor , gelatinase , alzheimer's disease , biochemistry , amyloid (mycology) , β amyloid , amyloid β , disease , medicine , enzyme , inorganic chemistry
The ability of the 72 kDa gelatinase A to cleave the amyloid protein precursor (APP) was investigated. HeLa cells were transfected with an APP 695 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.