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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif
Reeba S Jacob1, Edna George1, Pradeep K Singh1
1From the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai, Maharashtra 400076, India.
The Journal of Biological Chemistry
|January 9, 2016
Summary
Amyloid fibrils, protein aggregates, can act as universal cell-adhesive substrates. They promote cell attachment and spreading through integrin stimulation and immobilize red blood cells via charge interactions.
Area of Science:
- Biomaterials Science
- Cell Biology
- Protein Chemistry
Background:
- Amyloids are protein/peptide aggregates with cross-β-sheet structures.
- Amyloids are linked to human diseases and have native biological functions.
- Amyloids are known to interact with cell membranes.
Purpose of the Study:
- To investigate the potential of amyloids as universal cell-adhesive substrates.
- To explore the mechanisms underlying cell adhesion on amyloid fibrils.
- To assess the role of amyloids in cell attachment and red blood cell immobilization.
Main Methods:
- Utilizing various amyloid proteins/peptides as substrates.
- Assessing cell attachment and spreading on amyloid surfaces.
- Measuring integrin expression and focal adhesion formation.
- Investigating charge-based interactions for red blood cell immobilization.
Main Results:
- Amyloid fibrils support cell attachment and spreading, similar to collagen.
- Amyloids stimulate integrin expression and promote focal adhesion formation.
- Amyloid fibrils immobilize red blood cells through charge-based interactions.
- Both active (integrin-mediated) and passive (charge-based) mechanisms contribute to adhesion on amyloids.
Conclusions:
- Amyloids exhibit universal cell-adhesive properties.
- Cell adhesion on amyloids involves both active and passive mechanisms.
- Amyloid adhesivity may have implications in human diseases and biological functions.
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