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Lack of β-amyloid production in M19 cells deficient in site 2 processing of the sterol regulatory element binding proteins

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
427
Issue
3
Identifiers
DOI: 10.1016/s0014-5793(98)00469-4
Keywords
  • Protein Processing
  • Proteolysis
  • Amyloid Precursor Protein
  • γ-Secretase
  • Chinese Hamster Ovary Cell
Disciplines
  • Biology

Abstract

Abstract The processing of the amyloid precursor protein (APP) and the sterol regulatory element binding protein show remarkable analogies. Following a first lumenal cleavage, both proteins undergo a cleavage within the transmembrane domain by enzymatic activities named γ-secretase and S2P, respectively. We analyzed the processing of APP in the mutant Chinese hamster ovary (CHO) cell line M19 which lacks the S2P gene encoding for a putative metalloprotease. In these cells, we were not able to detect any β-amyloid production from endogenous or transiently overexpressed APP, although the transport of APP along the secretory pathway, its processing by α- and β-secretase, as well as its secretion were normal. This strongly suggests that the γ-secretase cleavage in M19 cells is severely impaired.

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