Authors:
RN LePage, AJ Fosang, SJ Fuller, G Murphy, G Evin, K Beyreuther, CL Masters, DH Small
Journal name: 
FEBS Lett
Citation info: 
377(2):267-270
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 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.
DOI: 
http://doi.org/10.1016/0014-5793(95)01358-x
E-pub date: 
30 Nov 1995
Users with this publication listed: 
Gillian Murphy