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Evidence for p62 aggregate formation: role in cell survival
Michael G Paine1, J Ramesh Babu, M Lamar Seibenhener
1Program in Cell and Molecular Biosciences, Auburn University, AL 36849, USA.
FEBS Letters
|September 1, 2005
Summary
The protein p62 forms fibrillar aggregates in vitro, which may protect cells from apoptosis. These findings suggest p62 fibrils play a role in aggresome formation and influence cell viability.
Area of Science:
- Biochemistry
- Cell Biology
- Structural Biology
Background:
- The protein p62 is known to localize in disease-associated aggregates.
- Understanding the aggregation properties of p62 is crucial for disease research.
Purpose of the Study:
- To investigate the in vitro aggregation behavior of the p62 protein.
- To determine the structural characteristics of p62 aggregates.
- To explore the cellular consequences of p62 overexpression and aggregate formation.
Main Methods:
- Fourier-transform infrared (FTIR) spectroscopy to assess protein secondary structure.
- Thioflavin T (ThT) fluorescence assay to detect amyloid formation.
- Transmission electron microscopy (TEM) to visualize aggregate morphology.
- HEK cell culture to study p62 overexpression effects.
Main Results:
- p62 forms independent fibrillar aggregates in a time- and concentration-dependent manner in vitro.
- FTIR and ThT assays indicated an increase in beta-sheet content during aggregation.
- TEM confirmed the fibrillar nature of the p62 aggregates.
- Overexpression of p62 in HEK cells led to aggregate formation and potential protection against apoptosis.
Conclusions:
- p62 can form distinct fibrillar aggregates in vitro.
- These p62 fibrils exhibit increased beta-sheet structure.
- p62 aggregate formation in cells may influence cell viability and aggresome formation.
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