Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Neural Regulation

Neural Regulation

Digestion begins with a cephalic phase that prepares the digestive system to receive food. When our brain processes visual or olfactory information about food, it triggers impulses in the cranial nerves innervating the salivary glands and stomach to prepare for food.

Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...

Alzheimer Disease l: Introduction

Alzheimer Disease l: Introduction

Alzheimer disease is a chronic, progressive, and irreversible neurodegenerative disorder and the most common cause of dementia in older adults. It leads to gradual neuronal loss, causing cognitive decline, behavioral changes, and loss of functional independence.Risk Factors and EtiologyThe disease is multifactorial. Age is the strongest risk factor, with prevalence doubling every 5 years after age 65. Genetic factors include mutations in genes such as APP, PSEN1, and PSEN2, which are associated...

Alzheimer Disease ll: Pathophysiology

Alzheimer Disease ll: Pathophysiology

Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

The temporal and stimuli-specific effects of LPS and IFNγ on microglial activation.

Frontiers in aging neuroscience·2026

Same author

Biomarkers.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2025

Same author

Fluid biomarkers for neurodegenerative diseases: a comprehensive update.

Alzheimer's research & therapy·2025

Same author

Cerebrospinal fluid markers link to synaptic plasticity responses and Alzheimer's disease genetic pathways.

Molecular neurodegeneration·2025

Same author

Reference proteins to improve Core 1 and Core 2 Alzheimer's disease CSF and plasma biomarkers.

Brain : a journal of neurology·2025

Same author

Reversible tau hyperphosphorylation in hibernation: a blood biomarker and brain tissue study.

Acta neuropathologica·2025

Search research articles

Related Experiment Video

Updated: Jun 19, 2026

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting

Published on: April 10, 2014

Tau protein profiling in tauopathies: a human brain study.

Juan Lantero-Rodriguez^1,2, Elena Camporesi^1,2, Laia Montoliu-Gaya^1,2

¹Department of Psychiatry & Neurochemistry, Institute of Neuroscience and Physiology, The Sahlgrenska Academy at the University of Gothenburg, Mölndal, Sweden.

Molecular Neurodegeneration

|July 18, 2024

Summary

This study reveals distinct tau protein profiles in various tauopathies, finding that Alzheimer's disease (AD) shows significantly higher levels of tau phosphorylation and aggregation compared to other tauopathies like PSP, PiD, and CBD.

Keywords:

Brain Mass spectrometry Phosphorylation Tau Tauopathies

More Related Videos

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

Published on: May 23, 2019

Related Experiment Videos

Last Updated: Jun 19, 2026

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting

Published on: April 10, 2014

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

Published on: May 23, 2019

Area of Science:

Neuroscience
Biochemistry
Pathology

Background:

Tauopathies, including Alzheimer's disease (AD), are characterized by abnormal tau protein accumulation.
Cerebrospinal fluid (CSF) tau biomarkers are specific for AD but not all tauopathies (e.g., PSP, PiD, CBD).
Understanding tau proteoform differences across tauopathies is crucial for diagnosis and treatment.

Purpose of the Study:

To develop and apply a multiplex assay for quantifying tau proteoforms in different tauopathies.
To compare non-phosphorylated and phosphorylated tau peptide profiles across AD, PSP, PiD, CBD, and control brain tissues.
To identify unique tau pathology signatures distinguishing AD from other tauopathies.

Main Methods:

Developed a multiplex assay combining immunoprecipitation and high-resolution mass spectrometry.
Analyzed soluble and insoluble brain tissue fractions from autopsy-confirmed tauopathy cases (AD, PSP, PiD, CBD) and controls.
Quantified tau isoforms, non-phosphorylated tau peptides (especially MTBR-containing), and 23 different phosphorylated peptides.

Main Results:

Non-phosphorylated tau profiles differed across tauopathies, with AD showing 12-72 times higher levels of MTBR-containing aggregates in insoluble fractions.
Tau isoform distribution varied: 3R tau predominated in PiD, while 4R tau was more abundant in CBD and PSP (insoluble fractions).
All investigated phosphorylated peptides increased in AD insoluble fractions; doubly and triply phosphorylated peptides also increased in AD soluble fractions, unlike other tauopathies.

Conclusions:

Abnormal tau phosphorylation and aggregation occur in non-AD tauopathies but are significantly more pronounced in Alzheimer's disease.
The developed multiplex assay effectively differentiates tau proteoform profiles across various tauopathies.
Distinct tau phosphorylation and aggregation patterns, particularly in AD, highlight potential diagnostic and therapeutic targets.