W. Wasco

article

Phosphorylation of calsenilin at Ser63 regulates its cleavage by caspase-3

E.K. Choi, J.S. Miller, N.F. Zaidi, E. Salih, more

Molecular and Cellular Neuroscience > 2003 > 23 > 3 > 495-506

Calsenilin is a member of the neuronal calcium sensor (NCS) family of proteins that interacts with the presenilins. Calsenilin has been found to act as a Kv4α channel interactor and as a transcriptional repressor. We have recently shown that calsenilin can be cleaved by caspase-3 and that its cleavage separates the conserved calcium-binding domain from the variable N-terminal domain. Here, we demonstrate...

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Biochemical and immunocytochemical characterization of calsenilin in mouse brain

N.F. Zaidi, O. Berezovska, E.K. Choi, J.S. Miller, more

Neuroscience > 2002 > 114 > 1 > 247-263

Mutations in the presenilin 1 and 2 genes cause the majority of early onset familial forms of Alzheimer's disease. Here we describe the biochemical and immunohistochemical characterization of calsenilin, a novel calcium binding protein that we have previously shown to interact with presenilins 1 and 2, in mouse brain. The co-immunoprecipitation of endogenous calsenilin and presenilin 1 demonstrates...

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Calsenilin Enhances Apoptosis by Altering Endoplasmic Reticulum Calcium Signaling

C. Lilliehook, S. Chan, E.K. Choi, N.F. Zaidi, more

Molecular and Cellular Neuroscience > 2002 > 19 > 4 > 552-559

Calsenilin (also called DREAM and KChIP3), a member of the neuronal calcium sensor family, was isolated in a yeast two-hybrid screen using an apoptotic domain of presenilin 2 as bait. Calsenilin is a cytoplasmic protein, but interacts with the COOH-termini of both presenilin 1 and presenilin 2 at the endoplasmic reticulum and the Golgi apparatus. In this study, we have investigated calsenilin's effect...

article

The Genes Responsible for Familial Alzheimer's Disease: Toward a Common Etiological Pathway

R. Tanzi, D. Kovacs, TW. Kim, R. Moir, more

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1; Supplement > S150

Four different genes have been implicated to play a role in inherited AD. Mutations in the APP gene on chromosome 21 account for only 2-3 % of early-onset FAD. The second reported FAD gene is on chromosome 19 and codes for apolipoprotein E (APOE). The ApoE- 4 allele has been shown to be a risk factor for about 40 % of AD with onset over 60 years of age, but is not sufficient to cause AD. We have...

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Detection of wild-type and mutant forms of presenilin 1 in mammalian cell membranes

D.M. Kovacs, W. Wasco, R.E. Tanzi

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1; Supplement > S136

The large majority of familial Alzheimer's disease (FAD) forms are caused by mutations in one of two recently identified genes, the presenilin 1 (PS-1) and presenilin 2 (PS-2) genes. Both proteins encoded by these genes are predicted to contain at least 7 transmembrane domains.We have recently reported on our initial findings reguarding the expression pattern and intracellular localization of PS-1...

article

Phosphorylation of APLP2 in cell cycle-dependent manner

K. Ando, Y. Satoh, T. Isohara, M. Oishi, more

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1; Supplement > S97

Amyloid precursor-like protein 2, APLP2, is a member of the gene family which includes the Alzheimer amyloid precursor protein (APP). Our previous results demonstrated that APP is phosphorylated by cdc2 kinase in cell cycle-dependent manner in cultured cells, and the identical site, Thr668 (numbering for APP ₆ ₉ ₅ isoform), is phosphorylated in rat brain tissues. An identical potential...

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Proteolytic Processing of Wild-type and Mutant Forms of Presenilin 2

T.-W. Kim, O. G. Hallmark, W. Pettingell, W. Wasco, more

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1; Supplement > S155

The majority of early-onset familial Alzheimer's disease (FAD) appears to be caused by mutations in two recently identified genes: presenilin 1 (PS1) and presenilin 2 (PS2). These two novel genes, PS1, located on chromosome 14, and PS2, on chromosome 1, are significantly homologous to each other and are members of an evolutionarily conserved gene family. The predicted structures of PS1 and PS2 contain...

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The Presenilin 1 and 2 mutations linked to familial Alzheimer's disease increase the extracellular concentration of amyloid β protein (Aβ) ending at Aβ42(43)

S. Younkin, D. Scheuner, Song X., C. Eckman, more

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1; Supplement > S38

To determine whether the extracellular concentration of Aβ is affected by the Presenilin 1 (PS1) and Presenilin 2 (PS2) mutations recently linked to familial AD (FAD), we performed a blinded comparison in carriers and controls of the concentrations of Aβ in plasma and in skin fibroblast conditioned medium. Overall, we made 15 comparative measurements of (AβX-42(43)/βAPP synthesis) in control fibroblasts...

article

546 Detection of wild-type and mutant forms of presenilin 1 in mammalian cell membranes

D.M. Kovacs, W. Wasco, R.E. Tanzi

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1 > S136

article

149 The Presenilin 1 and 2 mutations linked to familial Alzheimer's Disease increase the extracellular concentration of amyloid 0 protein (Aβ) ending at Aβ42(43)

S. Younkin, D. Scheuner, X. Song, C. Eckman, more

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1 > S38

article

Characterization and Analysis of Presenilin 2 in Mammalian Cells: Normal Role and Effect of FAD-Associated Mutations.

W. Wasco, D.M. Kovacs, T.-W. Kim, R.E. Tanzi

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1; Supplement > S136

Genetic factors play a major role in the etiology and rate of pathogenesis of a significant percentage of Alzheimer's disease (AD). Mutations in two recently identified six to nine transmembrane domain proteins have been found to be responsible for the majority of early-onset familial AD (FAD). These FAD-associated genes, presenilin 1 (PS1) and presenilin 2 (PS2), are located on chromosomes 14 and...

article

602 The genes responsible for familial Alzheimer's disease: Toward a common etiological pathway

R. Tanzi, D. Kovacs, T.W. Kim, R. Moir, more

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1 > S150

article

624 Proteolytic processing of wild-type and mutant forms of presenilin 2

T.-W. Kim, O.G. Hallmark, W. Pettingell, W. Wasco, more

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1 > S155

article

545 Characterization and analysis of presenilin 2 in mammalian cells: Normal role and effect of FAD-associated mutations

W. Wasco, D.M. Kovacs, T.-W. Kim, R.E. Tanzi

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1 > S136

article

389 Phosphorylation of APLP2 in cell cycle-dependent manner

K. Andoo, Y. Satoh, T. Isohara, M. Oishi, more

Neurobiology of Aging > 1996 > 17 > 4 Supplement 1 > S97

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Search results for: W. Wasco

Phosphorylation of calsenilin at Ser63 regulates its cleavage by caspase-3

Biochemical and immunocytochemical characterization of calsenilin in mouse brain

Calsenilin Enhances Apoptosis by Altering Endoplasmic Reticulum Calcium Signaling

The Genes Responsible for Familial Alzheimer's Disease: Toward a Common Etiological Pathway

Detection of wild-type and mutant forms of presenilin 1 in mammalian cell membranes

Phosphorylation of APLP2 in cell cycle-dependent manner

Proteolytic Processing of Wild-type and Mutant Forms of Presenilin 2

The Presenilin 1 and 2 mutations linked to familial Alzheimer's disease increase the extracellular concentration of amyloid β protein (Aβ) ending at Aβ42(43)

546 Detection of wild-type and mutant forms of presenilin 1 in mammalian cell membranes

149 The Presenilin 1 and 2 mutations linked to familial Alzheimer's Disease increase the extracellular concentration of amyloid 0 protein (Aβ) ending at Aβ42(43)

Characterization and Analysis of Presenilin 2 in Mammalian Cells: Normal Role and Effect of FAD-Associated Mutations.

602 The genes responsible for familial Alzheimer's disease: Toward a common etiological pathway

624 Proteolytic processing of wild-type and mutant forms of presenilin 2

545 Characterization and analysis of presenilin 2 in mammalian cells: Normal role and effect of FAD-associated mutations

389 Phosphorylation of APLP2 in cell cycle-dependent manner

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