Related Experiment Video
Updated: Feb 25, 2026

11:57
Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans
Published on: November 26, 2017
9.2K
SIPS as a model to study age-related changes in proteolysis and aggregate formation
Christiane Ott1, Tobias Jung1, Tilman Grune2
1Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany.
Mechanisms of Ageing and Development
|July 31, 2017
Summary
Aging increases cellular damage and senescent cells. This review explores how protein aggregation and oxidation impact aging and senescence, using cell models to understand these age-related changes.
Area of Science:
- Cellular Biology
- Gerontology
- Biochemistry
Background:
- Aging leads to cellular damage accumulation and increased senescent cells.
- Senescence involves morphological changes, altered protein turnover, and aggregate buildup.
- The role of protein oxidation and aggregates in aging and senescence requires further investigation.
Purpose of the Study:
- To review the characteristics of replicative and premature senescence.
- To discuss methods for inducing common senescence models.
- To summarize current knowledge on age-related changes in proteolytic systems.
Main Methods:
- Review of existing literature on senescence and aging.
- Focus on cell culture models, particularly stress-induced premature senescence (SIPS).
- Analysis of age-related changes in protein aggregation and proteolytic systems.
Main Results:
- Senescence is a dynamic process with key hallmarks.
- SIPS models are valuable for studying aging mechanisms and proteolysis.
- Age-related decline in proteolysis and increased protein aggregation are significant.
Conclusions:
- Cellular damage and senescence are hallmarks of aging.
- Protein aggregation and oxidation are implicated in aging and senescence.
- Understanding these processes via cell models aids in unraveling aging mechanisms.
Related Concept Videos
The Proteasome
10.4K
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...
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...
10.4K
Protein Complex Assembly
16.9K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.9K

