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Additional resources for Alzheimer's Disease: Advances in Genetics, Molecular and Cellular Biology
Although the sequences around the two aspartates, YD and GLGD, do not ﬁt with the motifs of canonical aspartic proteases (D(T/S)G(T/S)), the active site of PS is similar to the catalytic sites of the bacterial type-4 prepilin peptidase (TFPP) (Steiner et al. 2000). TFPP has an eight TM structure with active sites close to the transmembrane regions. Direct support for the hypothesis that PS were catalytical active proteases came from studies showing that several γ -secretase inhibitors bound to presenilin (Esler et al.
2. APP Biology, Processing and Function 21 It appears that none of the aforementioned secretases have unique substrate speciﬁcity towards APP. Besides APP, several transmembrane proteins such as pro-TNFα and pro-TGFα undergo ectodomain shedding by enzymes with α-secretase activity. The relatively low afﬁnity of BACE1 toward APP led to the suggestion that APP is not its sole physiological substrate. In support of this idea, α2,6-sialyltransferase and low density lipoprotein receptor-related protein (LRP) have been identiﬁed as additional substrates that are processed by BACE1.
Although it was initially felt that AICD must enter the nucleus with Fe65, subsequent study showed that nuclear translocation of AICD is not required but may be indirect through Fe65 (Cao and Sudhof, 2004). An alternative approach to address this question is to look for AICD activated candidate genes. , 2005). The latter pathway is particularly interesting because it suggests that γ -secretase release of AICD can regulate the degradation of Aβ in the extracellular space. If this is true, it will be important to know the feedback pathways that modulate γ -secretase activity to regulate neprilysin expression.