Gelatinase A possesses a beta-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease.
FEBS Lett
; 377(2): 267-70, 1995 Dec 18.
Article
em En
| MEDLINE
| ID: mdl-8543065
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 beta-secretase site was cleaved by gelatinase A adjacent to a glutamate residue at position -3 (beta A4 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 beta-secretase activity.
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Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Metaloendopeptidases
/
Proteínas da Matriz Extracelular
/
Precursor de Proteína beta-Amiloide
/
Gelatinases
Limite:
Humans
Idioma:
En
Ano de publicação:
1995
Tipo de documento:
Article