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Low molecular weight species of tau in Alzheimer's disease are dependent on tau phosphorylation sites but not on delayed post-mortem delay in tissue processing

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Low molecular weight species of tau in Alzheimer's disease are dependent on tau phosphorylation sites but not on delayed post-mortem delay in tissue processing. / Santpere, Gabriel; Puig, Berta; Ferrer, Isidre; Puig Martorell, Berta.

in: NEUROSCI LETT, Jahrgang 399, Nr. 1-2, 15.05.2006, S. 106-10.

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

Harvard

Santpere, G, Puig, B, Ferrer, I & Puig Martorell, B 2006, 'Low molecular weight species of tau in Alzheimer's disease are dependent on tau phosphorylation sites but not on delayed post-mortem delay in tissue processing', NEUROSCI LETT, Jg. 399, Nr. 1-2, S. 106-10. https://doi.org/10.1016/j.neulet.2006.01.036

APA

Santpere, G., Puig, B., Ferrer, I., & Puig Martorell, B. (2006). Low molecular weight species of tau in Alzheimer's disease are dependent on tau phosphorylation sites but not on delayed post-mortem delay in tissue processing. NEUROSCI LETT, 399(1-2), 106-10. https://doi.org/10.1016/j.neulet.2006.01.036

Vancouver

Santpere G, Puig B, Ferrer I, Puig Martorell B. Low molecular weight species of tau in Alzheimer's disease are dependent on tau phosphorylation sites but not on delayed post-mortem delay in tissue processing. NEUROSCI LETT. 2006 Mai 15;399(1-2):106-10. https://doi.org/10.1016/j.neulet.2006.01.036

Bibtex

@article{94f22ca77675432fb2debfbc0c522947,
title = "Low molecular weight species of tau in Alzheimer's disease are dependent on tau phosphorylation sites but not on delayed post-mortem delay in tissue processing",
abstract = "Gel electrophoresis and Western blotting of sarkosyl-insoluble fractions enriched in hyper-phosphorylated tau in Alzheimer disease (AD) have been used to analyze the pattern of phospho-tau by using different antibodies directed to the amino-terminal, core and carboxyl terminus of tau, and by using samples with increased artificial post-mortem delay in order to gain understanding on the characteristics of the band pattern and its vulnerability to post-mortem degradation. In addition to the typical profile of three major bands of 68, 64 and 60 kDa, several bands of lower molecular weight have been distinguished in frontal cortex homogenates in four AD cases stage V of Braak and Braak in optimal samples with 2 h of post-mortem delay. Lower bands, ranging from 60 to 22 kDa, are best seen with antibodies directed to the core of tau protein and, particularly, to the carboxy-terminus, thus suggesting the presence of truncated or cleaved forms of tau containing the C-terminal region. This pattern is not the result of post-mortem degradation, as artificial post-mortem delay of the same sample does not reveal the appearance of new bands with time. On the contrary, tau degradation, manifested as a reduction in the number and intensity of the bands, may occur between 8 and 26 h post-mortem and is universal in samples with post-mortem delays of 50h.",
keywords = "Alzheimer Disease, Binding Sites, Brain, Humans, Molecular Weight, Phosphorylation, Postmortem Changes, Specimen Handling, Time Factors, tau Proteins",
author = "Gabriel Santpere and Berta Puig and Isidre Ferrer and {Puig Martorell}, Berta",
year = "2006",
month = may,
day = "15",
doi = "10.1016/j.neulet.2006.01.036",
language = "English",
volume = "399",
pages = "106--10",
journal = "NEUROSCI LETT",
issn = "0304-3940",
publisher = "Elsevier Ireland Ltd",
number = "1-2",

}

RIS

TY - JOUR

T1 - Low molecular weight species of tau in Alzheimer's disease are dependent on tau phosphorylation sites but not on delayed post-mortem delay in tissue processing

AU - Santpere, Gabriel

AU - Puig, Berta

AU - Ferrer, Isidre

AU - Puig Martorell, Berta

PY - 2006/5/15

Y1 - 2006/5/15

N2 - Gel electrophoresis and Western blotting of sarkosyl-insoluble fractions enriched in hyper-phosphorylated tau in Alzheimer disease (AD) have been used to analyze the pattern of phospho-tau by using different antibodies directed to the amino-terminal, core and carboxyl terminus of tau, and by using samples with increased artificial post-mortem delay in order to gain understanding on the characteristics of the band pattern and its vulnerability to post-mortem degradation. In addition to the typical profile of three major bands of 68, 64 and 60 kDa, several bands of lower molecular weight have been distinguished in frontal cortex homogenates in four AD cases stage V of Braak and Braak in optimal samples with 2 h of post-mortem delay. Lower bands, ranging from 60 to 22 kDa, are best seen with antibodies directed to the core of tau protein and, particularly, to the carboxy-terminus, thus suggesting the presence of truncated or cleaved forms of tau containing the C-terminal region. This pattern is not the result of post-mortem degradation, as artificial post-mortem delay of the same sample does not reveal the appearance of new bands with time. On the contrary, tau degradation, manifested as a reduction in the number and intensity of the bands, may occur between 8 and 26 h post-mortem and is universal in samples with post-mortem delays of 50h.

AB - Gel electrophoresis and Western blotting of sarkosyl-insoluble fractions enriched in hyper-phosphorylated tau in Alzheimer disease (AD) have been used to analyze the pattern of phospho-tau by using different antibodies directed to the amino-terminal, core and carboxyl terminus of tau, and by using samples with increased artificial post-mortem delay in order to gain understanding on the characteristics of the band pattern and its vulnerability to post-mortem degradation. In addition to the typical profile of three major bands of 68, 64 and 60 kDa, several bands of lower molecular weight have been distinguished in frontal cortex homogenates in four AD cases stage V of Braak and Braak in optimal samples with 2 h of post-mortem delay. Lower bands, ranging from 60 to 22 kDa, are best seen with antibodies directed to the core of tau protein and, particularly, to the carboxy-terminus, thus suggesting the presence of truncated or cleaved forms of tau containing the C-terminal region. This pattern is not the result of post-mortem degradation, as artificial post-mortem delay of the same sample does not reveal the appearance of new bands with time. On the contrary, tau degradation, manifested as a reduction in the number and intensity of the bands, may occur between 8 and 26 h post-mortem and is universal in samples with post-mortem delays of 50h.

KW - Alzheimer Disease

KW - Binding Sites

KW - Brain

KW - Humans

KW - Molecular Weight

KW - Phosphorylation

KW - Postmortem Changes

KW - Specimen Handling

KW - Time Factors

KW - tau Proteins

U2 - 10.1016/j.neulet.2006.01.036

DO - 10.1016/j.neulet.2006.01.036

M3 - SCORING: Journal article

C2 - 16488541

VL - 399

SP - 106

EP - 110

JO - NEUROSCI LETT

JF - NEUROSCI LETT

SN - 0304-3940

IS - 1-2

ER -