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Psen1 antibody

Hai-Ying Zhang, Yi-Heng Liu, Yuan Fu, Peng-Cheng Chen, Rui Lu, Jian-Xing Li, Ming-Hui Chen, Hao-Chi Yang, Yu-Sheng Zhang
OBJECTIVE: To study the effects of intrahippocampal injection of cellular prion protein (PrPC ) antibody on cognitive deficits of APPswe/PSEN1dE9 transgenic mice. METHODS: Eight-month-old male APPswe/PSEN1dE9 transgenic mice were subjected to bilateral intrahippocampal injection of a single dose (2 µL) of anti-PrPC monoclonal antibody (EP1802Y) or PBS, with wild-type C57Bl/6J mice serving as the control group. After two months, the mice were tested for cognitive behaviors using open filed (OF) test, Morris water maze (MWM) test, fear conditioning (FC) test, and novel object recognition (NOR) test, and immunohistochemistry was used to examine the changes in hippocampal expression of Aβ1-42 ...
April 20, 2018: Nan Fang Yi Ke da Xue Xue Bao, Journal of Southern Medical University
María-Salud García-Ayllón, Inmaculada Lopez-Font, Claudia P Boix, Juan Fortea, Raquel Sánchez-Valle, Alberto Lleó, José-Luis Molinuevo, Henrik Zetterberg, Kaj Blennow, Javier Sáez-Valero
This study assesses whether C-terminal fragments (CTF) of the amyloid precursor protein (APP) are present in cerebrospinal fluid (CSF) and their potential as biomarkers for Alzheimer's disease (AD). Immunoprecipitation and simultaneous assay by Western blotting using multiplex fluorescence imaging with specific antibodies against particular domains served to characterize CTFs of APP in human CSF. We demonstrate that APP-CTFs are detectable in human CSF, being the most abundant a 25-kDa fragment, probably resulting from proteolytic processing by η-secretase...
May 30, 2017: Scientific Reports
Teng Jiang, Ying-Dong Zhang, Qing Gao, Jun-Shan Zhou, Xi-Chen Zhu, Huan Lu, Jian-Quan Shi, Lan Tan, Qi Chen, Jin-Tai Yu
As the most common type of neurodegenerative disease, Alzheimer's disease (AD) is characterized by the accumulation of amyloid-β peptide (Aβ) within the brain. Triggering receptor expressed on myeloid cells (TREM) 1 is an immune receptor expressed by mononuclear phagocytes including monocytes and microglia, coupling with TYRO protein tyrosine kinase binding protein to regulate immune reactions. Emerging evidence indicates that rs6910730(G), an intronic variant of TREM1, is associated with an increased Aβ neuropathology in the brains of elderly subjects, but the underlying mechanisms remain unclear...
November 2016: Acta Neuropathologica
Jannik E Jakobsen, Marianne G Johansen, Mette Schmidt, Ying Liu, Rong Li, Henrik Callesen, Margarita Melnikova, Mette Habekost, Carmela Matrone, Yvonne Bouter, Thomas A Bayer, Anders Lade Nielsen, Monika Duthie, Paul E Fraser, Ida E Holm, Arne Lund Jørgensen
Mutations in the amyloid-β protein precursor gene (AβPP), the presenilin 1 gene (PSEN1) or the presenilin 2 gene (PSEN2) that increase production of the AβPP-derived peptide Aβ42 cause early-onset Alzheimer's disease. Rodent models of the disease show that further increase in Aβ42 production and earlier brain pathology can be obtained by coexpressing AβPP and PSEN1 mutations. To generate such elevated Aβ42 level in a large animal model, we produced Göttingen minipigs carrying in their genome one copy of a human PSEN1 cDNA with the Met146Ile (PSEN1M146I) mutation and three copies of a human AβPP695 cDNA with the Lys670Asn/Met671Leu (AβPPsw) double-mutation...
July 14, 2016: Journal of Alzheimer's Disease: JAD
Hiroyuki Shimada
The DIAN observational study compared the pathophysiological markers between mutation carriers and non-carriers for autosomal dominant Alzheimer's disease. It has revealed the biomarker changes in the mutation carrier's brain started as early as 20, even 25 years prior to symptoms. The researchers of DIAN started the prevention trial(DIAN-TU) with two monoclonal antibodies. The API study is the clinical trial of the anti-amyloid monoclonal antibody therapy to the kindred of early onset familial AD (EOAD) who carry the PSEN1 E280A mutation...
March 2016: Nihon Rinsho. Japanese Journal of Clinical Medicine
Elena Vallino Costassa, Michele Fiorini, Gianluigi Zanusso, Simone Peletto, Pierluigi Acutis, Elisa Baioni, Cristiana Maurella, Fabrizio Tagliavini, Marcella Catania, Marina Gallo, Monica Lo Faro, Maria Novella Chieppa, Daniela Meloni, Antonio D'Angelo, Orlando Paciello, Roberta Ghidoni, Elisa Tonoli, Cristina Casalone, Cristiano Corona
Amyloid-β (Aβ) deposits are seen in aged individuals of many mammalian species that possess the same aminoacid sequence as humans. This study describes Aβ deposition in 102 clinically characterized cattle brains from animals aged 0 to 20 years. Extracellular and intracellular Aβ deposition was detected with 4G8 antibody in the cortex, hippocampus, and cerebellum. X-34 staining failed to stain Aβ deposits, indicating the non β-pleated nature of these deposits. Western blot analysis and surface-enhanced laser desorption/ionization time-of-flight (SELDI-TOF) mass spectrometry revealed in Tris, Triton, and formic acid fractions the presence of different Aβ peptides, characterized mainly by C-terminally truncated forms...
2016: Journal of Alzheimer's Disease: JAD
Eugene O'Hare, Ross Jeggo, Eun-Mee Kim, Bridgeen Barbour, Jean-Sebastien Walczak, Philip Palmer, Taylor Lyons, Deaglan Page, Donncha Hanna, Jolyon R Meara, David Spanswick, Jian-Ping Guo, Edith G McGeer, Patrick L McGeer, Peter Hobson
Bexarotene has been reported to reduce brain amyloid-β (Aβ) levels and to improve cognitive function in transgenic mouse models of Alzheimer's disease (AD). Four groups failed to fully replicate the primary results but the original authors claimed overall support for the general conclusions. Because of its potential clinical importance, the current work studied the effects of bexarotene using two animal species and highly relevant paradigms. Rats were tested for the ability of bexarotene to prevent changes induced by an Aβ challenge in the form intracerebroventricular (i...
January 2016: Neuropharmacology
Jochim Reinert, Henrik Martens, Melanie Huettenrauch, Tekla Kolbow, Lars Lannfelt, Martin Ingelsson, Anders Paetau, Auli Verkkoniemi-Ahola, Thomas A Bayer, Oliver Wirths
The pathogenesis of Alzheimer's disease (AD) is believed to be closely dependent on deposits of neurotoxic amyloid-β peptides (Aβ), which become abundantly present throughout the central nervous system in advanced stages of the disease. The different Aβ peptides existing are generated by subsequent cleavage of the amyloid-β protein precursor (AβPP) and may vary in length and differ at their C-terminus. Despite extensive studies on the most prevalent species Aβ40 and Aβ42, Aβ peptides with other C-termini such as Aβ38 have not received much attention...
2014: Journal of Alzheimer's Disease: JAD
Qinxi Guo, Hongmei Li, Allysa L Cole, Ji-Yeun Hur, Yueming Li, Hui Zheng
BACKGROUND: Alzheimer's disease (AD), the most common cause of dementia in the elderly, has two pathological hallmarks: Aβ plaques and aggregation of hyperphosphorylated tau (p-tau). Aβ is a cleavage product of Amyloid Precursor Protein (APP). Presenilin 1 (PS1) and presenilin 2 (PS2) are the catalytic subunit of γ-secretase, which cleaves APP and mediates Aβ production. Genetic mutations in APP, PSEN1 or PSEN2 can lead to early onset of familial AD (FAD). Although mutations in the tau encoding gene MAPT leads to a subtype of frontotemporal dementia and these mutations have been used to model AD tauopathy, no MAPT mutations have been found to be associated with AD...
2013: PloS One
Hiroyuki Shimada
The DIAN study compared the pathophysiological markers between carriers and non-carriers of mutation for autosomal dominant Alzheimer's disease (AD). They used the participant's age at baseline assessment and the parent's age at the onset of symptoms of AD to calculate the estimated delay in symptom onset. The study revealed that the biomarker change, which is the reduction of Aβ42 in the CSF of the carrier's brain, started approximately 15-20 years prior to the onset of symptoms. Subsequently, a chronological series of events took place: deposition of fibrillar Aβ as measured by positron emission tomography with the use of Pittsburgh compound B, increase in tau protein in the CSF, hippocampal atrophy and hypometabolism of FDG-PET, and cognitive and clinical changes...
October 2013: Brain and Nerve, Shinkei Kenkyū No Shinpo
David J Irwin, Todd J Cohen, Murray Grossman, Steven E Arnold, Elisabeth McCarty-Wood, Vivianna M Van Deerlin, Virginia M-Y Lee, John Q Trojanowski
We have recently shown acetylation of tau at lysine residue 280 (AC-K280) to be a disease-specific modification in Alzheimer disease (AD), corticobasal degeneration, and progressive supranuclear palsy, likely representing a major regulatory tau modification. Herein, we extend our observations using IHC with a polyclonal antibody specific for AC-K280. Thirty brain regions were examined in argyrophilic grain disease (AGD; n = 5), tangle-predominant senile dementia (TPSD; n = 5), Pick disease (n = 4), familial AD (FAD; n = 2; PSEN1 p...
August 2013: American Journal of Pathology
Lucas Restrepo, Phillip Stafford, Stephen Albert Johnston
A practical diagnostic test is needed for early Alzheimer's disease (AD) detection. Immunosignaturing, a technology that employs antibody binding to a random-sequence peptide microarray, generates profiles that distinguish transgenic mice engineered with familial AD mutations (APPswe/PSEN1-dE9) from non-transgenic littermates. It can also detect an AD-like signature in humans. Here, we assess the changes in the immunosignature at different time points of the disease in mice and humans. We also evaluate the accuracy of the late-stage signature as a test to discriminate between young mice with familial AD mutations from non-transgenic littermates...
January 15, 2013: Journal of Neuroimmunology
John M Ringman, Andrew T Fithian, Karen Gylys, Jeffrey L Cummings, Giovanni Coppola, David Elashoff, Domenico Pratico, Jackob Moskovitz, Gal Bitan
BACKGROUND: Convergent evidence suggests that oxidative stress plays a central role in the pathology of Alzheimer's disease (AD). We asked if consequently, oxidation of methionine residues to methionine sulfoxide (MetO) was increased in plasma proteins of persons carrying familial AD (FAD) mutations. METHODS: Plasma was collected from 31 persons from families harboring PSEN1 or APP mutations. Using Western blot analysis with a novel anti-MetO polyclonal antibody, MetO levels were measured and compared between FAD mutation carriers (MCs) and non-mutation carrying (NCs) kin...
2012: Dementia and Geriatric Cognitive Disorders
Baoxi Qu, Roger N Rosenberg, Liping Li, Philip J Boyer, Stephen A Johnston
BACKGROUND: The amyloid-beta (Abeta) peptide has a central role in the neurodegeneration of Alzheimer disease (AD). Immunization of AD transgenic mice with Abeta(1-42) (Abeta(42)) peptide reduces both the spatial memory impairments and AD-like neuropathologic changes in these mice. Therapeutic immunization with Abeta in patients with AD was shown to be effective in reducing Abeta deposition, but studies were discontinued owing to the development of an autoimmune, cell-mediated meningoencephalitis...
December 2004: Archives of Neurology
Masaki Takao, Bernardino Ghetti, Isao Hayakawa, Eiji Ikeda, Yasuo Fukuuchi, Leticia Miravalle, Pedro Piccardo, Jill R Murrell, Bradley S Glazier, Atsuo Koto
We report a family of Japanese origin that has five individuals from two generations affected by an illness characterized by dementia, a stooped posture and an antiflexion gait with an onset in the fourth or fifth decade of life. Two siblings had a clinical phenotype characterized by dementia and Parkinsonism with stooped posture, rigidity and bradykinesia. Neuropathological alterations in both patients included numerous 'cotton wool' plaques (CWPs), senile plaques, severe amyloid angiopathy, neurofibrillary tangles, neuronal rarefaction and gliosis...
August 2002: Acta Neuropathologica
Hwa Jeong Lee, Yun Zhang, Chunni Zhu, Karen Duff, William M Pardridge
Abeta 1-40 is a potential peptide radiopharmaceutical that could be used to image the brain Abeta amyloid of Alzheimer disease in vivo, should this peptide be made transportable through the blood-brain barrier in vivo. The blood-brain barrier transport of [ 125 I]-Abeta 1-40 in a transgenic mouse model was enabled by conjugation to the rat 8D3 monoclonal antibody to the mouse transferrin receptor. The Abeta 1-40 -8D3 conjugate is a bifunctional molecule that binds the blood-brain barrier TfR and undergoes transport into brain and binds the Abeta amyloid plaques of Alzheimer disease...
February 2002: Journal of Cerebral Blood Flow and Metabolism
I Vanderhoeven, P Cras, J J Martin, C Van Broeckhoven, C De Jonghe
Presenilin-1 (PSEN1) mutations I143T and G384A give rise to severe early onset Alzheimers's disease in two extensively studied Belgian families, AD/A and AD/B. In this study we investigated the influence of the I143T and G384A mutations on PSEN1 proteolytic processing. Hereto we analyzed PSEN1 processing in lymphoblasts by immunodetection with PSEN1-specific antibodies and densitometric analysis of the immunoreactive banding pattern. No differences were observed between presymptomatic mutation carriers, patients or escapees, demonstrating that the PSEN1 mutations I143T and G384A do not alter PSEN1 proteolytic processing in lymphoblasts...
October 29, 1999: Neuroscience Letters
G Van Gassen, C De Jonghe, S Pype, W Van Criekinge, A Julliams, I Vanderhoeven, S Woodrow, R Beyaert, D Huylebroeck, C Van Broeckhoven
Proteolytic processing and degradation tightly regulate the amount of stable, functional presenilin 1 (PSEN1) in the cell. The approximately 46-kDa PSEN1 holoprotein is cleaved into a approximately 30-kDa N-terminal fragment (NTF) and a approximately 20-kDa C-terminal fragment (CTF) by an unknown protease. The fragments are stabilized in a high molecular weight complex and nonincorporated fragments and excess holoprotein are degraded by the 26S proteasome. The tight balance between, on the one hand, processing and incorporation into the stable complex and, on the other hand, proteolytic degradation of excess PSEN1, indicates that minor changes in one of these two processes could be pathologically relevant...
October 1999: Neurobiology of Disease
A Julliams, I Vanderhoeven, S Kuhn, C Van Broeckhoven, C De Jonghe
Presenilin1 (PSEN1) 1143T and G384A mutations give rise to severe early-onset Alzheimer's disease in two extensively studied Belgian families. In the present study, we examined the effect of PSEN1 1143T and G384A mutations on tau phosphorylation in human SH-SY5Y and mouse Neuro-2a neuroblastoma cell lines that were transiently transfected with wild type (WT) or mutant PSEN1. With a phosphorylation independent antibody, no alteration in the electrophoretic mobility of tau was observed between wild type and mutant PSEN1 transfectants...
July 9, 1999: Neuroscience Letters
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