Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif

Amyloids are highly ordered, cross-β-sheet-rich protein/peptide aggregates associated with both human diseases and native functions. Given the well established ability of amyloids in interacting with cell membranes, we hypothesize that amyloids can serve as universal cell-adhesive substrates. Here,...

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Bibliographic Details
Published in:The Journal of biological chemistry 2016-03, Vol.291 (10), p.5278-5298
Main Authors: Jacob, Reeba S., George, Edna, Singh, Pradeep K., Salot, Shimul, Anoop, Arunagiri, Jha, Narendra Nath, Sen, Shamik, Maji, Samir K.
Format: Article
Language:English
Subjects:
3T3 Cells
adhesion
Amino Acid Motifs
amyloid
Amyloid - chemistry
Amyloid - metabolism
Amyloid - pharmacology
Animals
Binding Sites
Cell Adhesion
Erythrocytes - drug effects
Fibroblasts - drug effects
focal adhesions
Humans
integrin
Integrins - metabolism
Mice
Molecular Biophysics
PC12 Cells
Protein Binding
protein self-assembly
Rats
Static Electricity
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Summary:Amyloids are highly ordered, cross-β-sheet-rich protein/peptide aggregates associated with both human diseases and native functions. Given the well established ability of amyloids in interacting with cell membranes, we hypothesize that amyloids can serve as universal cell-adhesive substrates. Here, we show that, similar to the extracellular matrix protein collagen, amyloids of various proteins/peptides support attachment and spreading of cells via robust stimulation of integrin expression and formation of integrin-based focal adhesions. Additionally, amyloid fibrils are also capable of immobilizing non-adherent red blood cells through charge-based interactions. Together, our results indicate that both active and passive mechanisms contribute to adhesion on amyloid fibrils. The present data may delineate the functional aspect of cell adhesion on amyloids by various organisms and its involvement in human diseases. Our results also raise the exciting possibility that cell adhesivity might be a generic property of amyloids.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M115.678177