Impact of Source and Manufacturing of Collagen Matrices on Fibroblast Cell Growth and Platelet Aggregation

Abstract

Abstract:Collagen is a main component of the extracellular matrix. It is often used in medical applications to support tissue regeneration, hemostasis, or wound healing. Due to different sources of collagen, the properties and performance of available products can vary significantly. In this in vitro study, a comparison of seven different collagen matrices derived from bovine, equine, and porcine sources was performed. As performance indicators, the scaffold function for fibroblasts and platelet aggregation were used. We found strong variation in platelet aggregation and fibroblast growth on the different collagen materials. The observed variations could not be attributed to species differences alone, but were highly dependent on differences in the manufacturing process.

Sources of Collagen for Biomaterials in Skin Wound Healing

“…Upon injection into a wound site, the gel forms a collagen-fibrin matrix capable of triggering cellular recruitment, adhesion and proliferation [85]. The addition of platelet-rich plasma results in platelet-derived growth factor and vascular endothelial growth factor production within the matrix, further enhancing the proliferation of fibroblasts and vascular recruitment [84,85,86]. In vivo research indicates that wounds treated with rhCOL type I synthesized by a tobacco recombinant system significantly accelerate wound closure, when compared to animal-derived collagen flowable gels [84].…”

The influence of animal species, gender and tissue on the structural, biophysical, biochemical and biological properties of collagen sponges

“…Despite the significant advancements in the field, collagen remains an animal by-product and, as such, variability is frequently encountered between different collagen preparations, as a function of species, tissue and extraction method [ 7 , 8 ], which subsequently influence the properties and performance of the produced scaffolds [ 9 – 11 ]. For example, the properties of extruded collagen fibres have been shown to be species (bovine Achilles tendon versus rat tail tendon) and extraction method (acid versus pepsin) dependent [ 12 ].…”

Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

“…Type I collagen fibrils are of extreme importance in the regulation of cell morphology, spreading and motility, cell communication, proliferation and apoptosis [5][6][7]. In recent years, many studies have been focused on collagen fibrils reconstituted by a large number of monomeric collagen molecules in vitro.…”