title: Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif.
abstract: 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.
authors.affiliation: From the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai, Maharashtra 400076, India.
authors.forename: Reeba S
authors.initials: RS
authors.lastname: Jacob
authors.affiliation: From the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai, Maharashtra 400076, India.
authors.forename: Edna
authors.initials: E
authors.lastname: George
authors.affiliation: From the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai, Maharashtra 400076, India.
authors.forename: Pradeep K
authors.initials: PK
authors.lastname: Singh
authors.affiliation: From the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai, Maharashtra 400076, India.
authors.forename: Shimul
authors.initials: S
authors.lastname: Salot
authors.affiliation: From the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai, Maharashtra 400076, India.
authors.forename: Arunagiri
authors.initials: A
authors.lastname: Anoop
authors.affiliation: From the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai, Maharashtra 400076, India.
authors.forename: Narendra Nath
authors.initials: NN
authors.lastname: Jha
authors.affiliation: From the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai, Maharashtra 400076, India shamiks@iitb.ac.in.
authors.forename: Shamik
authors.initials: S
authors.lastname: Sen
authors.affiliation: From the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai, Maharashtra 400076, India samirmaji@iitb.ac.in.
authors.forename: Samir K
authors.initials: SK
authors.lastname: Maji
mesh_terms: D016475:3T3 Cells; D020816:Amino Acid Motifs; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D000818:Animals; D001665:Binding Sites; D002448:Cell Adhesion; D004912:Erythrocytes / Q000187:drug effects; D005347:Fibroblasts / Q000187:drug effects; D006801:Humans; D016023:Integrins / Q000378:metabolism*; D051379:Mice; D016716:PC12 Cells; D011485:Protein Binding; D051381:Rats; D055672:Static Electricity
chemical_list: D000682:Amyloid; D016023:Integrins
keywords: adhesion; amyloid; focal adhesions; integrin; protein self-assembly