We previously demonstrated that ultraviolet (UV) or dehydrothermal (DHT) crosslinking partially denatured fibers extruded from an insoluble type I collagen dispersion. In this study denaturation effects were evaluated by measuring collagen-fiber sensitivity to trypsin. Shrinkage-temperature measurem
Effect of crosslinking method on collagen fiber-fibroblast interactions
β Scribed by Lisa D. Bellincampi; Michael G. Dunn
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 154 KB
- Volume
- 63
- Category
- Article
- ISSN
- 0021-8995
No coin nor oath required. For personal study only.
β¦ Synopsis
Collagen, the major structural protein of the extracellular matrix in animals, is a versatile biomaterial used in various tissue engineering applications. Crosslinking influences the mechanical properties, resorption kinetics, and biocompatibility of collagen-based biomaterials. In this study, we evaluated the effects of crosslinking on collagen fiber-fibroblast interactions in vitro. Collagen fibers were left untreated or crosslinked by ultraviolet (UV) irradiation, dehydrothermal (DHT) treatment (3 or 5 days), or hexamethylenediisocyanate (HMDIC) exposure. The initial attachment, proliferation (through 8 days), and morphology of human dermal fibroblasts were evaluated on control and crosslinked bundles of 200 collagen fibers in vitro. Initial attachment (number of fibroblasts at day 0) was increased on UV and DHT5-treated collagen fiber bundles. Fibroblast proliferation was similar for control, UV crosslinked, and DHT crosslinked fibers. In contrast, fibroblast attachment was significantly decreased and proliferation was delayed on HMDIC crosslinked fibers. These results, coupled with our previous studies, suggest that UV crosslinking of collagen fibers provides a combination of biocompatibility, mechanical properties, and strength retention suitable for various tissue engineering applications.
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