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Abnormal Sp1 transcription factor expression in Alzheimer disease and tauopathies

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Abnormal Sp1 transcription factor expression in Alzheimer disease and tauopathies. / Santpere, G; Nieto, M; Puig, B; Ferrer, I; Puig Martorell, Berta.

in: NEUROSCI LETT, Jahrgang 397, Nr. 1-2, 2005, S. 30-4.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Santpere, G, Nieto, M, Puig, B, Ferrer, I & Puig Martorell, B 2005, 'Abnormal Sp1 transcription factor expression in Alzheimer disease and tauopathies', NEUROSCI LETT, Jg. 397, Nr. 1-2, S. 30-4. https://doi.org/10.1016/j.neulet.2005.11.062

APA

Santpere, G., Nieto, M., Puig, B., Ferrer, I., & Puig Martorell, B. (2005). Abnormal Sp1 transcription factor expression in Alzheimer disease and tauopathies. NEUROSCI LETT, 397(1-2), 30-4. https://doi.org/10.1016/j.neulet.2005.11.062

Vancouver

Santpere G, Nieto M, Puig B, Ferrer I, Puig Martorell B. Abnormal Sp1 transcription factor expression in Alzheimer disease and tauopathies. NEUROSCI LETT. 2005;397(1-2):30-4. https://doi.org/10.1016/j.neulet.2005.11.062

Bibtex

@article{7b1a20fb4e9c496184d30a1182755984,
title = "Abnormal Sp1 transcription factor expression in Alzheimer disease and tauopathies",
abstract = "Sp1 transcription factor expression was examined by immunohistochemistry, immunofluorescence and confocal microscopy in Alzheimer disease (AD), Pick disease (PiD), progressive supranuclear palsy (PSP), Parkinson disease (PD) and Dementia with Lewy bodies (DLB). Sp1 partly co-localizes with hyper-phosphorylated tau deposits in neurofibrillary tangles, dystrophic neurites of senile plaques and neuropil threads in AD, and in neurons, astrocytes and oligodendrocytes bearing hyper-phosphorylated tau in PiD and PSP. Sp1 is not found in alpha-synuclein inclusions in PD and DLB. These modifications are not associated with changes in the total expression levels of Sp1, as revealed with gel electrophoresis and Western blotting of brain homogenates. Furthermore, no co-immunoprecipitation of Sp1 and phospho-tau was observed in AD and PiD cases. Since Sp1 binding sites are present in the promoters of several genes involved in amyloid and tau, and Sp1 is regulated by oxidative stress, the present findings suggest that Sp1 deposition in hyper-phosphorylated tau deposits may have functional consequences in the pathology of AD and other tauopathies.",
keywords = "Alzheimer Disease, Astrocytes, Blotting, Western, Case-Control Studies, Gene Expression, Humans, Immunohistochemistry, Immunoprecipitation, Neurofibrillary Tangles, Neurons, Pick Disease of the Brain, Postmortem Changes, Sp1 Transcription Factor, Tauopathies, tau Proteins",
author = "G Santpere and M Nieto and B Puig and I Ferrer and {Puig Martorell}, Berta",
year = "2005",
doi = "10.1016/j.neulet.2005.11.062",
language = "English",
volume = "397",
pages = "30--4",
journal = "NEUROSCI LETT",
issn = "0304-3940",
publisher = "Elsevier Ireland Ltd",
number = "1-2",

}

RIS

TY - JOUR

T1 - Abnormal Sp1 transcription factor expression in Alzheimer disease and tauopathies

AU - Santpere, G

AU - Nieto, M

AU - Puig, B

AU - Ferrer, I

AU - Puig Martorell, Berta

PY - 2005

Y1 - 2005

N2 - Sp1 transcription factor expression was examined by immunohistochemistry, immunofluorescence and confocal microscopy in Alzheimer disease (AD), Pick disease (PiD), progressive supranuclear palsy (PSP), Parkinson disease (PD) and Dementia with Lewy bodies (DLB). Sp1 partly co-localizes with hyper-phosphorylated tau deposits in neurofibrillary tangles, dystrophic neurites of senile plaques and neuropil threads in AD, and in neurons, astrocytes and oligodendrocytes bearing hyper-phosphorylated tau in PiD and PSP. Sp1 is not found in alpha-synuclein inclusions in PD and DLB. These modifications are not associated with changes in the total expression levels of Sp1, as revealed with gel electrophoresis and Western blotting of brain homogenates. Furthermore, no co-immunoprecipitation of Sp1 and phospho-tau was observed in AD and PiD cases. Since Sp1 binding sites are present in the promoters of several genes involved in amyloid and tau, and Sp1 is regulated by oxidative stress, the present findings suggest that Sp1 deposition in hyper-phosphorylated tau deposits may have functional consequences in the pathology of AD and other tauopathies.

AB - Sp1 transcription factor expression was examined by immunohistochemistry, immunofluorescence and confocal microscopy in Alzheimer disease (AD), Pick disease (PiD), progressive supranuclear palsy (PSP), Parkinson disease (PD) and Dementia with Lewy bodies (DLB). Sp1 partly co-localizes with hyper-phosphorylated tau deposits in neurofibrillary tangles, dystrophic neurites of senile plaques and neuropil threads in AD, and in neurons, astrocytes and oligodendrocytes bearing hyper-phosphorylated tau in PiD and PSP. Sp1 is not found in alpha-synuclein inclusions in PD and DLB. These modifications are not associated with changes in the total expression levels of Sp1, as revealed with gel electrophoresis and Western blotting of brain homogenates. Furthermore, no co-immunoprecipitation of Sp1 and phospho-tau was observed in AD and PiD cases. Since Sp1 binding sites are present in the promoters of several genes involved in amyloid and tau, and Sp1 is regulated by oxidative stress, the present findings suggest that Sp1 deposition in hyper-phosphorylated tau deposits may have functional consequences in the pathology of AD and other tauopathies.

KW - Alzheimer Disease

KW - Astrocytes

KW - Blotting, Western

KW - Case-Control Studies

KW - Gene Expression

KW - Humans

KW - Immunohistochemistry

KW - Immunoprecipitation

KW - Neurofibrillary Tangles

KW - Neurons

KW - Pick Disease of the Brain

KW - Postmortem Changes

KW - Sp1 Transcription Factor

KW - Tauopathies

KW - tau Proteins

U2 - 10.1016/j.neulet.2005.11.062

DO - 10.1016/j.neulet.2005.11.062

M3 - SCORING: Journal article

C2 - 16378688

VL - 397

SP - 30

EP - 34

JO - NEUROSCI LETT

JF - NEUROSCI LETT

SN - 0304-3940

IS - 1-2

ER -