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

Rex N. LePage, Amanda J. Fosang, Stephanie J. Fuller, Gillian Murphy, Genevieve Evin, Konrad Beyreuther, Colin L. Masters, David H. Small

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)

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 languageEnglish
Pages (from-to)267-70
Number of pages4
JournalFEBS Letters
Volume377
Issue number2
DOIs
Publication statusPublished - 1995
Externally publishedYes

Keywords

  • Alzheimer' disease
  • Amyloid
  • Gelatinase
  • Secretase
  • Protease

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