Author Correction: Dynamic fibroblast contractions attract remote macrophages in fibrillar collagen matrix.

The original version of this Article contained an error in the spelling of the author Christopher A. McCulloch, which was incorrectly given as Christopher McCulloch. This has now been corrected in both the PDF and HTML versions of the Article.

Dynamic fibroblast contractions attract remote macrophages in fibrillar collagen matrix.

Macrophage (Mϕ)-fibroblast interactions coordinate tissue repair after injury whereas miscommunications can result in pathological healing and fibrosis. We show that contracting fibroblasts generate deformation fields in fibrillar collagen matrix that provide far-reaching physical cues for Mϕ. Within collagen deformation fields created by fibroblasts or actuated microneedles, Mϕ migrate towards the force source from several hundreds of micrometers away.

Contribution of collagen adhesion receptors to tissue fibrosis.

Fibrosis is the result of a wound-healing response that fails to restore normal tissue structure function. One of the critical hallmarks of fibrosis is disrupted collagen remodeling. In tissue homeostasis, the production, deposition and organization of collagen is balanced by the degradation and remodeling of collagen within the existing matrix.

Fibroblasts remodeling of type IV collagen at a biomaterials interface.

This paper describes the fate of adsorbed type IV collagen (Col IV) in contact with fibroblasts on model biomaterial surfaces, varying in wettability, chemistry and charge. We found that fibroblasts not only interact but also tend to remodel differently adsorbed Col IV employing two distinct mechanisms: mechanical reorganization and proteolytic degradation. Apart from the trend of adsorption -NH > CH > COOH > OH- the cells interact better with NH and OH surfaces -i.

Arrangement of type IV collagen on NH₂ and COOH functionalized surfaces.

Apart from the paradigm that cell-biomaterials interaction depends on the adsorption of soluble adhesive proteins we anticipate that upon distinct conditions also other, less soluble ECM proteins such as collagens, associate with the biomaterials interface with consequences for cellular response that might be of significant bioengineering interest. Using atomic force microscopy (AFM) we seek to follow the nanoscale behavior of adsorbed type IV collagen (Col IV)--a unique multifunctional matrix protein involved in the organization of basement membranes (BMs) including vascular ones. We have previously shown that substratum wettability significantly affects Col IV adsorption pattern, and in turn alters endothelial cells interaction.

Arrangement of type IV collagen and laminin on substrates with controlled density of -OH groups.

Collagen IV (Col IV) and laminin (Lam) are the main structural components of the basement membrane where they form two overlapping polymeric networks. We studied the adsorption pattern of these proteins on five model surfaces with tailored density of -OH groups obtained by copolymerization of different ratios ethyl acrylate (EA) and hydroxyl EA (HEA): X(OH)=0, X(OH)=0.3, X(OH)=0.