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Updated: Jun 21, 2025

4D Imaging of Protein Aggregation in Live Cells
Published on: April 5, 2013
Protein folding, cellular stress and cancer
Armando Aranda-Anzaldo1, Myrna A R Dent1, Edith Segura-Anaya1
1Laboratorio de Biología Molecular y Neurociencias, Facultad de Medicina, Universidad Autónoma del Estado de México, Paseo Tollocan y Jesús Carranza s/n, Toluca, 50180, Edo. Méx., Mexico.
Cellular stress responses (CSRs) influence protein folding, leading to conformational heterogeneity. Sustained stress can epigenetically drive aberrant phenotypes and potentially lead to cancer.
Area of Science:
- Molecular Biology
- Cell Biology
- Epigenetics
Background:
- Proteins manifest genotype, with function dependent on native folding.
- Cellular protein folding is a variable process influenced by the intracellular environment.
- Chaperones and co-chaperones supervise protein folding, adapting to local conditions.
Purpose of the Study:
- To explore the role of cellular stress responses (CSRs) in protein folding and phenotypic adaptation.
- To investigate how sustained cellular stress and CSRs can lead to aberrant phenotypes.
- To propose a common epigenetic pathway to cancer via proteome and interactome modification.
Main Methods:
- The study presents a theoretical framework and argument based on existing biological principles.
- It integrates concepts of protein folding, cellular stress, and epigenetic regulation.
- No new experimental data was generated; it's a conceptual analysis.
Main Results:
- Environmental influences and CSRs cause protein conformational heterogeneity.
- Sustained cellular stress can epigenetically alter the proteome and interactome.
- This adaptation to stress can result in an aberrant cellular phenotype.
Conclusions:
- Protein folding is plastic and influenced by the cellular environment.
- Efficient CSRs under sustained stress can select for aberrant phenotypes.
- This process represents a potential epigenetic pathway contributing to cancer development.
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