Calpain inhibitor I decreases βA4 secretion from human embryonal kidney cells expressing β-amyloid precursor protein carrying the APP670/671 double mutation
References (19)
- et al.
Degradation of secretory immunoglobulin M in B lymphocytes occurs in a postendoplasmic reticulum compartment and is mediated by a cysteine protease
J. Biol. Chem.
(1992) - et al.
Generation of β-amyloid in the secretory pathway in neuronal and nonneuronal cells
- et al.
High efficiency transformation of mammalian cells by plasmid DNA
Mol. Cell. Biol.
(1987) - et al.
Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production
Nature
(1992) - et al.
Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: the multicatalytic proteinase complex and m-calpain
J. Neurochem.
(1994) - et al.
Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments
Nature
(1992) - et al.
Amyloid β-peptide is produced by cultured cells during normal metabolism
Nature
(1992) - et al.
β-amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms
J. Biol. Chem.
(1993) - et al.
Inhibition of β-amyloid formation identifies proteolytic precursors and subcellular site of catabolism
Neuron
(1995)
Cited by (30)
γ-Secretase as a Target for Alzheimer's Disease
2012, Advances in PharmacologyCitation Excerpt :Nicastrin was independently isolated biochemically as a PSEN-associated protein and found to be essential for γ-secretase processing of both APP and Notch (Yu et al., 2000). A saturation screen in Caenorabditis elegans for PSEN modifiers identified these two proteins as well as Pen-2 (Francis et al., 2002). All four proteins (PSEN, nicastrin, Aph-1, and Pen-2) associate with one another and with an immobilized γ-secretase inhibitor (GSI) (Kimberly et al., 2003; Takasugi et al., 2003).
Adherence-dependent shifts in the patterns of β-amyloid peptides secreted by human mononuclear phagocytes
2008, Brain, Behavior, and ImmunityPlatelet as a physiological model to investigate apoptotic mechanisms in Alzheimer β-amyloid peptide production
2008, Mechanisms of Ageing and DevelopmentThe Protease Inhibitor, MG132, Blocks Maturation of the Amyloid Precursor Protein Swedish Mutant Preventing Cleavage by β-Secretase
2001, Journal of Biological ChemistryCitation Excerpt :This suggests that treatment of cells with high concentrations of peptide aldehydes may cause a more general impairment of the secretory pathway. This impairment blocks transport and processing of APPSw through the secretory pathway, thus explaining the decrease in Aβ peptide secretion observed by others (12-14). In previous studies, peptide aldehydes such as MG132 were thought to inhibit Aβ and p3 peptide secretion by blocking γ-secretase cleavage of the COOH-terminal fragment of APP (12, 13, 17, 18).
Factors influencing the processing and function of the amyloid β precursor protein - A potential therapeutic target in Alzheimer's disease?
2000, Pharmacology and TherapeuticsCitation Excerpt :While the γ-secretase enzyme has not been identified yet, its actions, which may be associated with multiple proteases, are determined by the location of the AβPP within the plasma membrane (Murphy et al., 1999). Furthermore, the γ-secretases, which generate Aβ40 and Aβ42 may be distinct enzymes, with the γ-40 secretase being a cysteine protease and γ-42 being a serine protease (Klafki et al., 1995; Citron et al., 1996; FigueiredoPereira et al., 1999), with the generation of Aβ40 and Aβ42 occurring within different compartments of the cell. It has been proposed that Aβ40 is generated in the TGN, while Aβ42 is produced both within the ER and the TGN with the Aβ generated in the TGN being localised in two distinct pools (Greenfield et al., 1999).
- 1
We thank D. Ristig for technical assistance and S. Frentzel for helpful discussions.