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Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
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Smooth muscle titin forms in vitro amyloid aggregates
Alexandr G Bobylev1, Oxana V Galzitskaya2, Roman S Fadeev3
1Laboratory of Structure and Functions of Muscle Proteins, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russian Federation bobylev1982@gmail.com.
Bioscience Reports
|April 30, 2016
Summary
Smooth muscle titin (SMT) forms amyloid aggregates in vitro, potentially contributing to smooth muscle amyloidosis. These titin amyloids exhibit cytotoxic effects on smooth muscle cells, disrupting cellular structure.
Area of Science:
- Biochemistry
- Cell Biology
- Protein Aggregation
Background:
- Amyloid aggregates are linked to neurodegenerative diseases and amyloidosis.
- Smooth muscle titin (SMT) is a large protein found in muscle tissue.
Purpose of the Study:
- To investigate the in vitro amyloid formation of smooth muscle titin (SMT).
- To assess the cytotoxic effects of SMT amyloid aggregates on smooth muscle cells.
Main Methods:
- Electron microscopy (EM)
- Thioflavin T (ThT) and Congo red (CR) fluorescence spectroscopy
- X-ray diffraction
- Dynamic light scattering (DLS)
- Confocal microscopy
Main Results:
- Chicken gizzard SMT forms amyloid aggregates in vitro, confirmed by EM, ThT, CR, and X-ray diffraction.
- DLS data indicated rapid formation of SMT amyloid aggregates with hydrodynamic radii ranging from 700-4500 nm.
- SMT amyloid aggregates demonstrated cytotoxicity towards bovine aorta smooth muscle cells, causing actin cytoskeleton disorganization and cell damage.
Conclusions:
- Titin has the potential to form amyloid aggregates in vitro.
- SMT amyloid aggregates exhibit cytotoxic effects on smooth muscle cells.
- Titin may play a role in the pathogenesis of smooth muscle amyloidosis.
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