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

Inborn Errors of Metabolism

Inborn Errors of Metabolism

Phenylketonuria (PKU) is a protein metabolism disorder characterized by high blood levels of the amino acid phenylalanine. This results from a mutation in the gene responsible for phenylalanine hydroxylase, an enzyme that converts phenylalanine into tyrosine. When this enzyme is deficient, phenylalanine builds up in the blood, leading to symptoms such as vomiting, rashes, seizures, growth deficiency, and severe mental retardation. An early diagnosis and a diet restricting phenylalanine intake...

Overview of Protein Metabolism

Overview of Protein Metabolism

Proteins are broken down into amino acids during digestion. Unlike fats and carbohydrates, which are stored for later use, proteins are not. Instead, amino acids are either used to produce ATP through oxidation or contribute to the creation of new proteins for the growth and repair of the body. Any surplus amino acids from the diet are converted into glucose or triglycerides rather than excreted.
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...

Glucose Transporters

Glucose Transporters

Glucose transporters facilitate the transport of glucose across the cell membrane. In addition to glucose, some glucose transporters can also aid the movement of other hexoses such as fructose, mannose, and galactose.
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes:

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...

Lysosomal Hydrolases

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...

Translation

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life

You might also read

Related Articles

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

Sort by

Same author

Early, sex-dependent and progressive proteomic imbalance in the amygdala during Alzheimer´s disease continuum.

Biology of sex differences·2026

Same author

The landscape of taste receptors in glioblastoma.

Biochemical pharmacology·2026

Same author

NeMO Analytics: a compendium of transcriptomic data for the exploration of neocortical development.

Nature neuroscience·2026

Same author

Adaptive evolution of gene regulatory networks in mammalian neocortex.

Nature·2026

Same author

Human-specific features of the cerebellum and ZP2-regulated synapse development.

Cell·2026

Same author

Proteomic profile of CSF obtained at the time of diagnosis determines amyotrophic lateral sclerosis progression and survival: CXCL7 levels in disease prognosis and survival.

Brain pathology (Zurich, Switzerland)·2026

Search research articles

Related Experiment Video

Updated: Jul 7, 2026

The Plant Infection Test: Spray and Wound-Mediated Inoculation with the Plant Pathogen Magnaporthe Grisea

The Plant Infection Test: Spray and Wound-Mediated Inoculation with the Plant Pathogen Magnaporthe Grisea

Published on: August 4, 2018

Argyrophilic grain disease.

Isidro Ferrer¹, Gabriel Santpere, Fred W van Leeuwen

¹Institut Neuropatologia, Servei Anatomia Patològica, IDIBELL-Hospital Universitari de Bellvitge, carrer Feixa LLarga sn, 08907 Hospitalet de Llobregat, Spain. 8082ifa@comb.cat

Brain : a Journal of Neurology

|February 1, 2008

Summary

Argyrophilic grain disease (AGD) involves hyperphosphorylated tau protein in brain cells, leading to neurodegeneration. Oxidative stress and impaired protein clearance contribute to its development, impacting cognitive function in older adults.

More Related Videos

Gibberella zeae Ascospore Production and Collection for Microarray Experiments.

Gibberella zeae Ascospore Production and Collection for Microarray Experiments.

Published on: November 30, 2006

Visualizing Early Infection Sites of Rice Blast Disease (Magnaporthe oryzae) on Barley (Hordeum vulgare) Using a Basic Microscope and a Smartphone

Visualizing Early Infection Sites of Rice Blast Disease (Magnaporthe oryzae) on Barley (Hordeum vulgare) Using a Basic Microscope and a Smartphone

Published on: March 17, 2023

Related Experiment Videos

Last Updated: Jul 7, 2026

The Plant Infection Test: Spray and Wound-Mediated Inoculation with the Plant Pathogen Magnaporthe Grisea

The Plant Infection Test: Spray and Wound-Mediated Inoculation with the Plant Pathogen Magnaporthe Grisea

Published on: August 4, 2018

Gibberella zeae Ascospore Production and Collection for Microarray Experiments.

Gibberella zeae Ascospore Production and Collection for Microarray Experiments.

Published on: November 30, 2006

Visualizing Early Infection Sites of Rice Blast Disease (Magnaporthe oryzae) on Barley (Hordeum vulgare) Using a Basic Microscope and a Smartphone

Visualizing Early Infection Sites of Rice Blast Disease (Magnaporthe oryzae) on Barley (Hordeum vulgare) Using a Basic Microscope and a Smartphone

Published on: March 17, 2023

Area of Science:

Neuroscience
Neuropathology
Gerontology

Background:

Argyrophilic grain disease (AGD) is a common neurodegenerative disorder in the elderly.
It is characterized by argyrophilic grains (AGs) and pre-tangle neurons containing hyperphosphorylated tau.
AGD accounts for approximately 5% of dementia cases.

Purpose of the Study:

To elucidate the pathogenesis of AGD and its associated tau pathology.
To investigate the role of oxidative stress, kinases, and protein degradation pathways in AGD.
To correlate AG distribution with clinical symptoms and other tauopathies.

Main Methods:

Golgi method for visualizing argyrophilic grains.
Immunohistochemistry to detect hyperphosphorylated tau, stress markers, kinases, and ubiquitin.
Analysis of tau protein patterns (64/68 kDa) and truncated forms.

Main Results:

AGs and pre-tangle neurons contain hyperphosphorylated 4R tau, truncated tau, and accumulate in limbic system neurons and glial cells.
Oxidative stress markers and activated stress kinases (SAPK, p38, GSK3beta) co-localize with hyperphosphorylated tau.
Impaired proteasome function, indicated by mutant ubiquitin (UBB(+1)), contributes to tau accumulation.

Conclusions:

Oxidative stress and activated stress kinases are key factors in tau hyperphosphorylation in AGD.
Impaired protein degradation pathways, including proteasome dysfunction, exacerbate tau accumulation.
AGD pathogenesis involves a complex interplay of oxidative stress, kinase activation, and disrupted protein homeostasis, contributing to neurodegeneration.