Regulated cleavage of alzheimer β-amyloid precursor protein in the absence of the cytoplasmic tail
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Cited by (67)
Role of tyrosine phosphorylation in the regulation of cleavage secretion of angiotensin-converting enzyme
2004, Journal of Biological ChemistryCitation Excerpt :The 8-kDa C-tail fragment that was left in the cell after the ectodomain of ACE was cleaved off was not tyrosine-phosphorylated, and the cleavage secretion of a cytoplasmic tail-deleted mutant ACE was also enhanced by pervanadate, indicating that the presence of the cytoplasmic tail is not essential for this response (Fig. 5). Similar to ACE shedding, transforming growth factor α, β-amyloid precursor protein, syndecan (37, 38), or L1 adhesion molecule shedding does not appear to depend on the cytoplasmic tail sequences (39). The cytoplasmic domain of l-selectin, on the contrary, seems to play a role in regulating its susceptibility to ectodomain shedding (40).
Monitoring protein phosphatase 1 isoform levels as a marker for cellular stress
2004, Neurotoxicology and TeratologyStimulation of β-amyloid precursor protein α-processing by phorbol ester involves calcium and calpain activation
2004, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Perhaps because phorbol esters are best known for PKC activation, many studies have focused on PKC as a key mediator. But earlier studies have found that although phorbol esters phosphorylate the intracellular domain of APP [39], deletion of this domain does not abolish the stimulated APP secretion [5,17]. In turn, more recent studies have looked beyond and suggested several new mechanisms.
Platelet-derived growth factor induces the β-γ-secretase-mediated cleavage of Alzheimer's amyloid precursor protein through a Src-Rac-dependent pathway
2003, Journal of Biological ChemistryCitation Excerpt :On the other hand, there are experimental results suggesting that phosphorylation of APP does not affect its processing. In fact, it was well documented that APP is phosphorylated on Ser and Thr in vitro and in vivo (59), but these post-translational modifications are not involved in the regulation of APP cleavage (60). APP is also phosphorylated at the level of Tyr-682 (APP695isoform numbering) of its intracellular domain (8).
Molecular basis for anti-amyloid therapy in the prevention and treatment of Alzheimer's disease
2002, Neurobiology of AgingCitation Excerpt :Okadaic acid, an inhibitor of protein phosphatases 1 and 2A, also increases APP proteolysis and release via the alpha-secretase pathway (Fig. 3; [9]), and it has recently been shown in primary neuronal cultures that protein phosphatase inhibition by okadaic acid is much more effective in lowering A-beta production than is PKC activation [27]. Thus, either stimulation of PKC or inhibition of protein phosphatases 1 and 2A is sufficient to produce a dramatic acceleration of nonamyloidogenic APP degradation and diminished generation of A-beta in virtually every situation tested to date, including primary neuronal cultures and rodent brain in vivo (Figs. 1–3; [10–31,56]). This phenomenon is sometimes referred to as “regulated cleavage of APP” or “reciprocal regulation of APP metabolism”; i.e. when certain signals are activated, alpha-secretase cleavage increases and (Asp1- and Glu11-beta-secretase cleavages decrease (Figs. 1–3).