Atomic force microscopic investigation on the potential early intermediate stages of fibrillogenesis of fibronectin within fibrils
                            Journal Article
                            ·
                            
                            · Biochemical and Biophysical Research Communications
                            
                        
                    - Department of Chemistry, Jinan University, Guangzhou, Guangdong 510632 (China) and Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, IL 60612 (United States)
- Department of Chemistry, Jinan University, Guangzhou, Guangdong 510632 (China)
To date, a large number of literature have focused on the mechanisms of fibronectin (FN) fibril initiation and elongation, discovering many binding sites on FN molecules that are required for FN fibril growth. However, it is still poorly understood how FN fibrils widen while elongating. Here, single molecules and polymers, FN fibrillogenesis, and FN fibril bundles around cells have all been investigated visually using atomic force microscopy. We found that the formation of ring-shaped and beaded-filament-like FN aggregates may be two early intermediate stages of FN fibrillogenesis within the fibrils away from cells, perhaps involving in the FN fibril widening/bundling.
- OSTI ID:
- 20991543
- Journal Information:
- Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 361; ISSN 0006-291X; ISSN BBRCA9
- Country of Publication:
- United States
- Language:
- English
Similar Records
                                
                                
                                    
                                        
                                        Fibronectin amyloid-like aggregation alters its extracellular matrix incorporation and promotes a single and sparsed cell migration
                                        
The N-terminal strand modulates immunoglobulin light chain fibrillogenesis
Anastellin, an FN3 Fragment with Fibronectin Polymerization Activity, Resembles Amyloid Fibril Precursors
                        
                                            Journal Article
                                            ·
                                            Mon Oct 15 00:00:00 EDT 2018
                                            · Experimental Cell Research
                                            ·
                                            OSTI ID:23082592
                                        
                                        
                                        
                                    
                                
                                    
                                        The N-terminal strand modulates immunoglobulin light chain fibrillogenesis
                                            Journal Article
                                            ·
                                            Thu Jan 09 23:00:00 EST 2014
                                            · Biochemical and Biophysical Research Communications
                                            ·
                                            OSTI ID:22242259
                                        
                                        
                                        
                                    
                                
                                    
                                        Anastellin, an FN3 Fragment with Fibronectin Polymerization Activity, Resembles Amyloid Fibril Precursors
                                            Journal Article
                                            ·
                                            Fri Aug 01 00:00:00 EDT 2003
                                            · Journal of Molecular Biology
                                            ·
                                            OSTI ID:15004681