PortalPublikationenConstitutive Dyrk1A is abnormally expressed in Alzheimer dis...

Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models

Standard

Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models. / Ferrer, Isidro; Barrachina, Marta; Puig, Berta; Martínez de Lagrán, M; Martí, Eulalia; Avila, Jesús; Dierssen, Mara; Puig Martorell, Berta.

in: NEUROBIOL DIS, Jahrgang 20, Nr. 2, 01.11.2005, S. 392-400.

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

Harvard

Ferrer, I, Barrachina, M, Puig, B, Martínez de Lagrán, M, Martí, E, Avila, J, Dierssen, M & Puig Martorell, B 2005, 'Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models', NEUROBIOL DIS, Jg. 20, Nr. 2, S. 392-400. https://doi.org/10.1016/j.nbd.2005.03.020

APA

Ferrer, I., Barrachina, M., Puig, B., Martínez de Lagrán, M., Martí, E., Avila, J., Dierssen, M., & Puig Martorell, B. (2005). Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models. NEUROBIOL DIS, 20(2), 392-400. https://doi.org/10.1016/j.nbd.2005.03.020

Vancouver

Ferrer I, Barrachina M, Puig B, Martínez de Lagrán M, Martí E, Avila J et al. Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models. NEUROBIOL DIS. 2005 Nov 1;20(2):392-400. https://doi.org/10.1016/j.nbd.2005.03.020

Bibtex

@article{6ecc05da2d594d0ab79ab2920616c8df,
title = "Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models",
abstract = "DYRK1A, dual-specificity tyrosine-regulated kinase 1A, maps to human chromosome 21 within the Down syndrome (DS) critical region. Dyrk1 phosphorylates the human microtubule-associated protein tau at Thr212 in vitro, a residue that is phosphorylated in fetal tau and hyper-phosphorylated in Alzheimer disease (AD) and tauopathies, including Pick disease (PiD). Furthermore, phosphorylation of Thr212 primes tau for phosphorylation by glycogen synthase kinase 3 (GSK-3). The present study examines Dyrk1A in the cerebral cortex of sporadic AD, adult DS with associated AD, and PiD. Increased Dyrk1A immunoreactivity has been found in the cytoplasm and nuclei of scattered neurons of the neocortex, entorhinal cortex, and hippocampus in AD, DS, and PiD. Dyrk1A is found in sarkosyl-insoluble fractions which are enriched in phosphorylated tau in AD brains, thus suggesting a possible association of Dyrk1A with neurofibrillary tangle pathology. Yet, no clear relationship has been observed between tau phosphorylation at Thr212, and GSK-3 and Dyrk1A expression in diseased brains. Transgenic mice bearing a triple tau mutation (G272V, P301L, and R406W) and expressing hyper-phosphoyrylated tau in neurons of the entorhinal cortex, hippocampus, and cerebral neocortex show increased expression of Dyrk1A in individual neurons in the same regions. However, transgenic mice over-expressing Dyrk1A do not show increased phosphorylation of tau at Thr212, thus suggesting that Dyrk1A over-expression does not trigger per se hyper-phosphorylation of tau at Thr212 in vivo. The present observations indicate modifications in the expression of constitutive Dyrk1A in the cytoplasm and nuclei of neurons in various neurodegenerative diseases associated with tau phosphorylation.",
keywords = "Adult, Aged, Aged, 80 and over, Alzheimer Disease, Animals, Cell Nucleus, Cerebral Cortex, Cytoplasm, Disease Models, Animal, Down Syndrome, Entorhinal Cortex, Female, Hippocampus, Humans, Immunohistochemistry, Male, Mice, Mice, Transgenic, Middle Aged, Neurons, Phosphorylation, Pick Disease of the Brain, Protein-Serine-Threonine Kinases, Protein-Tyrosine Kinases, tau Proteins",
author = "Isidro Ferrer and Marta Barrachina and Berta Puig and {Mart{\'i}nez de Lagr{\'a}n}, M and Eulalia Mart{\'i} and Jes{\'u}s Avila and Mara Dierssen and {Puig Martorell}, Berta",
year = "2005",
month = nov,
day = "1",
doi = "10.1016/j.nbd.2005.03.020",
language = "English",
volume = "20",
pages = "392--400",
journal = "NEUROBIOL DIS",
issn = "0969-9961",
publisher = "Academic Press Inc.",
number = "2",

}

RIS

TY - JOUR

T1 - Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models

AU - Ferrer, Isidro

AU - Barrachina, Marta

AU - Puig, Berta

AU - Martínez de Lagrán, M

AU - Martí, Eulalia

AU - Avila, Jesús

AU - Dierssen, Mara

AU - Puig Martorell, Berta

PY - 2005/11/1

Y1 - 2005/11/1

N2 - DYRK1A, dual-specificity tyrosine-regulated kinase 1A, maps to human chromosome 21 within the Down syndrome (DS) critical region. Dyrk1 phosphorylates the human microtubule-associated protein tau at Thr212 in vitro, a residue that is phosphorylated in fetal tau and hyper-phosphorylated in Alzheimer disease (AD) and tauopathies, including Pick disease (PiD). Furthermore, phosphorylation of Thr212 primes tau for phosphorylation by glycogen synthase kinase 3 (GSK-3). The present study examines Dyrk1A in the cerebral cortex of sporadic AD, adult DS with associated AD, and PiD. Increased Dyrk1A immunoreactivity has been found in the cytoplasm and nuclei of scattered neurons of the neocortex, entorhinal cortex, and hippocampus in AD, DS, and PiD. Dyrk1A is found in sarkosyl-insoluble fractions which are enriched in phosphorylated tau in AD brains, thus suggesting a possible association of Dyrk1A with neurofibrillary tangle pathology. Yet, no clear relationship has been observed between tau phosphorylation at Thr212, and GSK-3 and Dyrk1A expression in diseased brains. Transgenic mice bearing a triple tau mutation (G272V, P301L, and R406W) and expressing hyper-phosphoyrylated tau in neurons of the entorhinal cortex, hippocampus, and cerebral neocortex show increased expression of Dyrk1A in individual neurons in the same regions. However, transgenic mice over-expressing Dyrk1A do not show increased phosphorylation of tau at Thr212, thus suggesting that Dyrk1A over-expression does not trigger per se hyper-phosphorylation of tau at Thr212 in vivo. The present observations indicate modifications in the expression of constitutive Dyrk1A in the cytoplasm and nuclei of neurons in various neurodegenerative diseases associated with tau phosphorylation.

AB - DYRK1A, dual-specificity tyrosine-regulated kinase 1A, maps to human chromosome 21 within the Down syndrome (DS) critical region. Dyrk1 phosphorylates the human microtubule-associated protein tau at Thr212 in vitro, a residue that is phosphorylated in fetal tau and hyper-phosphorylated in Alzheimer disease (AD) and tauopathies, including Pick disease (PiD). Furthermore, phosphorylation of Thr212 primes tau for phosphorylation by glycogen synthase kinase 3 (GSK-3). The present study examines Dyrk1A in the cerebral cortex of sporadic AD, adult DS with associated AD, and PiD. Increased Dyrk1A immunoreactivity has been found in the cytoplasm and nuclei of scattered neurons of the neocortex, entorhinal cortex, and hippocampus in AD, DS, and PiD. Dyrk1A is found in sarkosyl-insoluble fractions which are enriched in phosphorylated tau in AD brains, thus suggesting a possible association of Dyrk1A with neurofibrillary tangle pathology. Yet, no clear relationship has been observed between tau phosphorylation at Thr212, and GSK-3 and Dyrk1A expression in diseased brains. Transgenic mice bearing a triple tau mutation (G272V, P301L, and R406W) and expressing hyper-phosphoyrylated tau in neurons of the entorhinal cortex, hippocampus, and cerebral neocortex show increased expression of Dyrk1A in individual neurons in the same regions. However, transgenic mice over-expressing Dyrk1A do not show increased phosphorylation of tau at Thr212, thus suggesting that Dyrk1A over-expression does not trigger per se hyper-phosphorylation of tau at Thr212 in vivo. The present observations indicate modifications in the expression of constitutive Dyrk1A in the cytoplasm and nuclei of neurons in various neurodegenerative diseases associated with tau phosphorylation.

KW - Adult

KW - Aged

KW - Aged, 80 and over

KW - Alzheimer Disease

KW - Animals

KW - Cell Nucleus

KW - Cerebral Cortex

KW - Cytoplasm

KW - Disease Models, Animal

KW - Down Syndrome

KW - Entorhinal Cortex

KW - Female

KW - Hippocampus

KW - Humans

KW - Immunohistochemistry

KW - Male

KW - Mice

KW - Mice, Transgenic

KW - Middle Aged

KW - Neurons

KW - Phosphorylation

KW - Pick Disease of the Brain

KW - Protein-Serine-Threonine Kinases

KW - Protein-Tyrosine Kinases

KW - tau Proteins

U2 - 10.1016/j.nbd.2005.03.020

DO - 10.1016/j.nbd.2005.03.020

M3 - SCORING: Journal article

C2 - 16242644

VL - 20

SP - 392

EP - 400

JO - NEUROBIOL DIS

JF - NEUROBIOL DIS

SN - 0969-9961

IS - 2

ER -