Expression of embryonic tau protein isoforms persist during adult neurogenesis in the hippocampus

Hippocampus ◽  
2007 ◽  
Vol 17 (2) ◽  
pp. 98-102 ◽  
Author(s):  
Torsten Bullmann ◽  
Rohan de Silva ◽  
Max Holzer ◽  
Hiroshi Mori ◽  
Thomas Arendt
Keyword(s):  
Adult Neurogenesis ◽  
Tau Protein ◽  
Protein Isoforms ◽  
Tau Protein Isoforms

Tau Isoform Profile in Essential Tremor Diverges From Other Tauopathies

2021 ◽  
Author(s):  
Soong Ho Kim ◽  
Kurt Farrell ◽  
Stephanie Cosentino ◽  
Jean-Paul G Vonsattel ◽  
Phyllis L Faust ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Essential Tremor ◽  
Tau Protein ◽  
Protein Isoforms ◽  
Cortical Tissue ◽  
Total Tau ◽  
Microtubule Binding Domain ◽  
Tau Isoforms ◽  
Tau Protein Isoforms ◽  
Pick Disease

Abstract Patients with essential tremor (ET) frequently develop concurrent dementia, which is often assumed to represent co-morbid Alzheimer disease (AD). Autopsy studies have identified a spectrum of tau pathologies in ET and tau isoforms have not been examined in ET. We performed immunoblotting using autopsy cerebral cortical tissue from patients with ET (n = 13), progressive supranuclear palsy ([PSP], n = 10), Pick disease ([PiD], n = 2), and AD (n = 7). Total tau in ET samples was similar to that in PSP and PiD but was significantly lower than that in AD. Abnormal tau levels measured using the AT8 phospho-tau specific (S202/T205/S208) monoclonal antibody in ET were similar to those in PSP but were lower than in PiD and AD. In aggregates, tau with 3 microtubule-binding domain repeats (3R) was significantly higher in AD than ET, while tau with 4 repeats (4R) was significantly higher in PSP. Strikingly, the total tau without N-terminal inserts in ET was significantly lower than in PSP, PiD, and AD, but total tau with other N-terminal inserts was not. Monomeric tau with one insert in ET was similar to that in PSP and PiD was lower than in AD. Thus, ET brains exhibit an expression profile of tau protein isoforms that diverges from that of other tauopathies.

A quantitative CE method to analyse tau protein isoforms using coated fused silica capillaries

2010 ◽  
Vol 33 (8) ◽  
pp. 1090-1098 ◽  
Author(s):  
Diego Bohoyo ◽  
Isabelle Le Potier ◽  
Céline Rivière ◽  
Hans Klafki ◽  
Jens Wiltfang ◽  
...  
Keyword(s):  
Tau Protein ◽  
Fused Silica ◽  
Protein Isoforms ◽  
Fused Silica Capillaries ◽  
Silica Capillaries ◽  
Tau Protein Isoforms

Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work.

2000 ◽  
Vol 33 (1) ◽  
pp. 95-130 ◽  
Author(s):  
Luc Buée ◽  
Thierry Bussière ◽  
Valérie Buée-Scherrer ◽  
André Delacourte ◽  
Patrick R. Hof
Keyword(s):  
Tau Protein ◽  
Protein Isoforms ◽  
Tau Protein Isoforms

Argyrophilic grain disease and Alzheimer's disease are distinguished by their different distribution of tau protein isoforms

2002 ◽  
Vol 104 (4) ◽  
pp. 425-434 ◽  
Author(s):  
Markus Tolnay ◽  
Nicolas Sergeant ◽  
Antoine Ghestem ◽  
Sonia Chalbot ◽  
Rob A. de Vos ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tau Protein ◽  
Protein Isoforms ◽  
Argyrophilic Grain Disease ◽  
Argyrophilic Grain ◽  
Tau Protein Isoforms

Biosensing MAPs as “roadblocks”: kinesin-based functional analysis of tau protein isoforms and mutants using suspended microtubules (sMTs)

Lab on a Chip ◽  
2013 ◽  
Vol 13 (16) ◽  
pp. 3217 ◽  
Author(s):  
Mehmet C. Tarhan ◽  
Yslam Orazov ◽  
Ryuji Yokokawa ◽  
Stanislav L. Karsten ◽  
Hiroyuki Fujita
Keyword(s):  
Functional Analysis ◽  
Tau Protein ◽  
Protein Isoforms ◽  
Tau Protein Isoforms

Different distribution of phosphorylated tau protein isoforms in Alzheimer's and Pick's diseases

FEBS Letters ◽  
1997 ◽  
Vol 412 (3) ◽  
pp. 578-582 ◽  
Author(s):  
N Sergeant ◽  
J.-P David ◽  
D Lefranc ◽  
P Vermersch ◽  
A Wattez ◽  
...  
Keyword(s):  
Tau Protein ◽  
Protein Isoforms ◽  
Phosphorylated Tau ◽  
Tau Protein Isoforms ◽  
Phosphorylated Tau Protein

P1-127: MASS SPECTROMETRIC QUANTIFICATION OF TAU PROTEIN ISOFORMS IN HUMAN CEREBROSPINAL FLUID

2006 ◽  
Vol 14 (7S_Part_5) ◽  
pp. P320-P320
Author(s):  
Yusaku Hioki ◽  
Naoki Kaneko ◽  
Ritsuko Yoda ◽  
Sadanori Sekiya ◽  
Shinichi Iwamoto ◽  
...  
Keyword(s):  
Cerebrospinal Fluid ◽  
Tau Protein ◽  
Mass Spectrometric ◽  
Protein Isoforms ◽  
Human Cerebrospinal Fluid ◽  
Tau Protein Isoforms

P3-306: Differential distribution of tau protein isoforms in sporadic FTLD and FTDP-17

2006 ◽  
Vol 2 ◽  
pp. S465-S465
Author(s):  
Rohan de Silva ◽  
Tammaryn Lashley ◽  
Catherine Strand ◽  
Anna-Maria Shiarli ◽  
Tamas Revesz ◽  
...  
Keyword(s):  
Tau Protein ◽  
Protein Isoforms ◽  
Differential Distribution ◽  
Tau Protein Isoforms

Distribution of c-protein isoforms in sarcomeres of developing chick skeletal muscle

1988 ◽  
Vol 46 ◽  
pp. 226-227
Author(s):  
D. A. Fischman ◽  
J. E. Dennis ◽  
T. Obinata ◽  
H. Takano-Ohmuro
Keyword(s):  
Skeletal Muscles ◽  
Thick Filament ◽  
Protein Isoforms ◽  
Actin Binding ◽  
Striated Muscles ◽  
C Protein ◽  
Sarcomeric Protein ◽  
Thick Filaments ◽  
Cross Bridges ◽  
Bridge Bearing

C-protein is a 150 kDa protein found within the A bands of all vertebrate cross-striated muscles. By immunoelectron microscopy, it has been demonstrated that C-protein is distributed along a series of 7-9 transverse stripes in the medial, cross-bridge bearing zone of each A band. This zone is now termed the C-zone of the sarcomere. Interest in this protein has been sparked by its striking distribution in the sarcomere: the transverse repeat between C-protein stripes is 43 nm, almost exactly 3 times the 14.3 nm axial repeat of myosin cross-bridges along the thick filaments. The precise packing of C-protein in the thick filament is still unknown. It is the only sarcomeric protein which binds to both myosin and actin, and the actin-binding is Ca-sensitive. In cardiac and slow, but not fast, skeletal muscles C-protein is phosphorylated. Amino acid composition suggests a protein of little or no αhelical content. Variant forms (isoforms) of C-protein have been identified in cardiac, slow and embryonic muscles.

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