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Porcine collagen crosslinking, degradation and its capability for fibroblast adhesion and proliferation


Reference:

Jarman-Smith, M. L., Bodamyali, T., Stevens, C., Howell, J. A., Horrocks, M. and Chaudhuri, J. B., 2004. Porcine collagen crosslinking, degradation and its capability for fibroblast adhesion and proliferation. Journal of Materials Science: Materials in Medicine, 15 (8), pp. 925-932.

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Abstract

Porcine dermal collagen permanently crosslinked with hexamethylene diisocyanate was investigated for its suitability as a dermal tissue engineering matrix. It was found that the chemically crosslinked collagen had far fewer free lysine groups per collagen molecule than did the uncrosslinked matrix. The ability of the matrix to support human primary fibroblast outgrowth from explants was compared for matrices that had been presoaked in various solutions, including fibroblast media, cysteine and phosphate buffered saline (PBS). It was found that superior cell outgrowth was obtained after soaking with fibroblast media and PBS. The fibroblast attachment properties of the matrix were compared against tissue culture plastic and PET. The collagen matrix showed the least amount of cell retention compared to the other to matrices, however, the general trends were similar for all three scaffolds. Longer term cultures on the collagen showed fibroblasts covering the matrix stacking up on each other and bridging natural hair follicles. However, it was also observed that the fibroblasts were not able to penetrate into the matrix structure. This was believed to result from the chemical crosslinking, as shown by the resistance of the matrix to degradation by collagenases. (C) 2004 Kluwer Academic Publishers.

Details

Item Type Articles
CreatorsJarman-Smith, M. L., Bodamyali, T., Stevens, C., Howell, J. A., Horrocks, M. and Chaudhuri, J. B.
DepartmentsFaculty of Humanities & Social Sciences > Health
RefereedYes
StatusPublished
ID Code6639
Additional InformationID number: ISI:000222967400012

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