Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Effect of Aging on Tissues01:19

The Effect of Aging on Tissues

Several body functions deteriorate with age. The external signs of aging are easily identifiable. For example, the skin becomes dry, less elastic, and thins out, forming wrinkles. The skin of the face begins to appear looser due to a decrease in the levels of elastic and collagen fibers in the connective tissue. Additionally, melanin production in the hair follicle decreases with age, resulting in gray hair. Moreover, the senses of sight and hearing decline, so glasses and hearing aids may...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...

You might also read

Related Articles

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

Sort by
Same author

Small-molecule dissolution of stress granules by redox modulation benefits ALS models.

Nature chemical biology·2025
Same author

A safety mechanism enables tissue-specific resistance to protein aggregation during aging in C. elegans.

PLoS biology·2023
Same author

Targeted protein degradation: from small molecules to complex organelles-a Keystone Symposia report.

Annals of the New York Academy of Sciences·2022
Same author

Extracellular proteostasis prevents aggregation during pathogenic attack.

Nature·2020
Same author

Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in <i>Caenorhabditis elegans</i>.

eLife·2019
Same author

Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans.

Journal of visualized experiments : JoVE·2017
Same journal

Potential role of the <i>Trpv4 c.1491+1G>A</i> mutation in pulmonary fibrosis in a gene-edited mouse model.

Frontiers in genetics·2026
Same journal

Utilization of whole exome sequencing to identify hereditary mutations in Palestinian families with hereditary cancers.

Frontiers in genetics·2026
Same journal

Research of N-acetyl-L-cysteine on CD40-CD40L pathway in pulmonary fibrosis induced by silicon dioxide.

Frontiers in genetics·2026
Same journal

Novel variants in LSS related hypotrichosis simplex 14.

Frontiers in genetics·2026
Same journal

Network-based analysis identifies shared mechanisms between ischemic stroke and myocardial infarction and therapeutic ingredients of Buyang Huanwu Decoction.

Frontiers in genetics·2026
Same journal

GWAS analysis of a depression cohort defined by an EHR-phenotyping algorithm reveals the role of immune regulations in depression risk.

Frontiers in genetics·2026
See all related articles

Related Experiment Video

Updated: May 16, 2026

Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans
11:57

Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans

Published on: November 26, 2017

Aging and the aggregating proteome.

Della C David1

  • 1German Center for Neurodegenerative Diseases (DZNE) Tübingen, Germany.

Frontiers in Genetics
|November 28, 2012
PubMed
Summary
This summary is machine-generated.

Aging causes a breakdown in protein homeostasis, leading to widespread protein aggregation. This review explores the causes, consequences, and neuronal differences in age-related protein aggregation and its link to disease.

Keywords:
C. elegansagingchaperonesneurodegenerationprotein aggregationprotein homeostasis

More Related Videos

Measurement of Protein Turnover Rates in Senescent and Non-Dividing Cultured Cells with Metabolic Labeling and Mass Spectrometry
08:52

Measurement of Protein Turnover Rates in Senescent and Non-Dividing Cultured Cells with Metabolic Labeling and Mass Spectrometry

Published on: April 6, 2022

Related Experiment Videos

Last Updated: May 16, 2026

Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans
11:57

Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans

Published on: November 26, 2017

Measurement of Protein Turnover Rates in Senescent and Non-Dividing Cultured Cells with Metabolic Labeling and Mass Spectrometry
08:52

Measurement of Protein Turnover Rates in Senescent and Non-Dividing Cultured Cells with Metabolic Labeling and Mass Spectrometry

Published on: April 6, 2022

Area of Science:

  • Cellular Biology
  • Neuroscience
  • Aging Research

Background:

  • Protein homeostasis (proteostasis) is crucial for cellular function and resource optimization across all organisms.
  • Aging is increasingly linked to a decline in proteostasis, resulting in non-disease protein aggregation.
  • Understanding age-related proteostasis collapse is vital for addressing cellular dysfunction.

Purpose of the Study:

  • To review the evidence for age-related protein aggregation.
  • To discuss the causes and consequences of physiological protein aggregation during aging.
  • To highlight differences in proteostasis and aggregation susceptibility between neurons and other cells.

Main Methods:

  • Literature review of recent findings on aging and protein homeostasis.
  • Analysis of studies investigating protein aggregation in aging models.
  • Synthesis of research on neuronal protein quality control mechanisms.

Main Results:

  • Accumulating evidence indicates a collapse of protein homeostasis with age, leading to widespread protein aggregation.
  • Neurons exhibit distinct protein quality control mechanisms and aggregation susceptibility compared to other cell types.
  • Cell-non-autonomous coordination of proteostasis by neurons plays a significant role.

Conclusions:

  • Age-related protein aggregation is a significant physiological event with potential links to disease pathogenesis.
  • Neuronal differences in proteostasis are critical for understanding age-related neurodegeneration.
  • Further research into neuronal coordination of proteostasis may reveal therapeutic targets.