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Endogenous expression of FAD-linked PS1 impairs proliferation, neuronal differentiation and survival of adult hippocampal progenitors. Veeraraghavalu K, Choi SH, Zhang X, Sisodia SS1.
GSK3 beta forms a tetrameric complex with endogenous PS1-CTF/NTF and beta-catenin. Effects of the D257/D385A and FAD-linked mutations. Tesco G1, Tanzi RE.
PS1 and APP secretion. (A) The expression of the endogenous PS1 in B103 cells was determined by Western blot analysis. (B) Effects of ?-secretase inhibitors II (g-II) (50 µM), III (g-III) (50 µM), IV (g-IV) (5 µM), and V (g-V) (10 µM) on APP secretion and intracellular expression of COOH-terminal stubs in B103(APP695) and B103(APP695/MOCA) cells are shown. Effects of Calp III (100 µM), MG132 (10 µM), and lactacystin (Lact) (20 µM) were tested as well.
Moreover, in several lines of transgenic mice, processed human PS1 derivatives accumulate to saturable levels independent of the levels of PS1 mRNA (12). These observations have suggested that the cellular factor(s) involved in endoproteolysis or stabilization of PS1 derivatives may be limiting. Although little information is available regarding the molecular identity of the enzyme(s) responsible for PS1/PS2 endoproteolysis and factors responsible for fragment stability, we consider it unlikely that the regulated accumulation of PS fragments is dependent on competition for protease(s) responsible for cleavage. In support of this view, we demonstrate that expression of COOH-terminally truncated human PS1 polypeptides (PS1361? and PS1403?), which contain the proteolytic cleavage site but fail to be cleaved, do not influence accumulation of endogenous.
Endogenous Presenilin-1 Targets to Endocytic Rather Than Biosynthetic Compartments Lah, James J. ; Levey, Allan I. Presenilin-1 (PS1), which is linked to familial Alzheimer's disease, participates in the proteolytic processing of Notch and amyloid-β precursor protein (APP) by an unknown mechanism. Reports of PS1 localization to the endoplasmic reticulum (ER) and Golgi apparatus have focused attention on the early biosynthetic pathway as the site of PS1 function.
Abstract: We have previously shown that the endogenous C-terminal fragment of presenilin 1 coimmunoprecipitates with endogenous β-catenin. Since PS1 has been suggested to be involved in β-catenin stabilization, we further investigated whether GSK3β, responsible for β-catenin phosphorylation and degradation, is part of the PS1/β-catenin complex. In naïve H4 and CHO cells, PS1 co-immunoprecipitated with both endogenous β-catenin and GSK3β.