Interaction of human skin fibroblasts with collagen fibrils - Index for evaluation of regulatory materials on cellular activity in the skin.

DOI

Bibliographic Information

Other Title
  • 皮膚線維芽細胞とコラーゲン線維の相互作用　　皮膚賦活剤評価の指標として
  • Index for evaluation of regulatory materials on cellular activity in the skin
  • 皮膚賦活剤評価の指標として

Abstract

Characteristic behavior of human skin fibroblasts in collagen gels has been investigated in order to clarify the interactions among the cells, collagen matrix, and diffusible factors. Dynamic behavior of fibroblasts in collagen gels was analyzed by video microscopy. Features that were observed include the development of extremely elongated cell shape and interactions between the cells and collagen fibrils. The interactions eventually resulted in the contraction of collagen gels. The contraction can be expressed in a quantitative way by size of the gel. It was stronger with human skin fibroblasts than with 3T3 established cells or with human fibrosarcoma cells. The intensity and rapidity of contraction increased with concentration of fetal bovine serum. Human skin fibroblasts in the contracted collagen gels stopped multiplying when density of collagen fibrils reached at more than 100μg/mm3. Fibroblasts under this condition had a smaller activity of protein synthesis than those in confluent monolayer culture. Growth response of fibroblasts in the contracted gels to epidermal growth factor was considerably retarded. These results suggest that human skin fibroblasts in collagen gels was in a resting state and in an environment more similar to in vivo tissue as compared to cells in conventional monolayer culture. The dynamic dehavior of fibroblasts in collagen gels, the ability of fibroblasts to contract the collagen gels, and the cellular activity in contracted collagen gels might be new indices for evaluation of regulatory materials on cellular activity in the skin.

Journal

Details 詳細情報について

  • CRID
    1390282679478060928
  • NII Article ID
    130004188587
  • DOI
    10.5107/sccj.21.111
  • ISSN
    18844146
    03875253
  • Text Lang
    ja
  • Data Source
    • JaLC
    • Crossref
    • CiNii Articles
  • Abstract License Flag
    Disallowed

Report a problem

Back to top