Abstract
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 alpha-secretase site was not cleaved. The results demonstrate that 72 kDa gelatinase A is not an alpha-secretase, but that it may have a β-secretase activity.
Original language | English |
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Pages (from-to) | 267-70 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 377 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1995 |
Externally published | Yes |
Keywords
- Alzheimer' disease
- Amyloid
- Gelatinase
- Secretase
- Protease