Related Experiment Video
Updated: Jul 3, 2025
11:04
Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
Published on: June 23, 2018
7.3K
Protein aggregation and biomolecular condensation in hypoxic environments (Review)
Chaoqun Li1, Bingjie Hao2, Haiguang Yang2
1School of Exercise and Health, Shanghai University of Sport, Shanghai 200438, P.R. China.
International Journal of Molecular Medicine
|February 16, 2024
Summary
Hypoxic stress disrupts protein homeostasis, causing aggregation and impacting diseases. Understanding these changes in protein aggregation and biomolecular condensation under hypoxia offers new therapeutic strategies.
Area of Science:
- Biochemistry and Molecular Biology
- Cellular Biology
- Pathology
Background:
- Protein homeostasis is crucial for cellular function and is disrupted by aging and environmental stressors like hypoxia.
- Uncontrolled protein aggregation is linked to various diseases, including neurodegenerative disorders, cardiovascular disease, hypoxic brain injury, and cancer.
- Biomolecular condensates, though distinct from aggregates, dynamically balance with them and play regulatory roles in cellular survival under hypoxic conditions.
Approach:
- This review summarizes mechanisms of aggregate assembly and dissolution induced by hypoxia.
- It addresses recent breakthroughs in understanding the role of protein aggregates in hypoxia-related diseases.
- The review explores hypotheses regarding hypoxia-induced phase changes in macromolecular assemblages and the role of ATP depletion.
Key Points:
- Hypoxia promotes the transition of macromolecular assemblages from a liquid to a solid phase.
- Adenosine triphosphate (ATP) depletion and inactivation of ATP-dependent protein chaperones are critical in hypoxia-induced aggregation.
- Understanding these processes is vital for developing treatments for hypoxia-related pathologies.
Conclusions:
- A deeper understanding of hypoxic stress, protein aggregation, and biomolecular condensation is essential for clinical applications.
- Investigating cellular adaptation to hypoxic environments may lead to improved patient survival and novel therapeutic strategies.
- Targeting protein aggregation and biomolecular condensation pathways could offer new avenues for treating hypoxia-related diseases.
Related Concept Videos
03:03Amyloid Fibrils
9.5K
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,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.5K
03:00Molecular Chaperones and Protein Folding
18.0K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
18.0K
01:25Protein Folding
8.0K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.0K
02:41Protein Complex Assembly
10.6K
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...
10.6K
01:28Protein Denaturation
4.2K
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
4.2K
01:57Gene Families
8.8K
Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
8.8K