Open AccessChemotactic attraction of human fibroblasts to type I, II, and III collagens and collagen-derived peptides.
Author(s) -
Arnold E. Postlethwaite,
Jerome M. Seyer,
Andrew H. Kang
Publication year - 1978
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.2.871
Subject(s) - chemotaxis , collagenase , in vitro , tripeptide , hydroxyproline , chemistry , biochemistry , fibroblast , type i collagen , microbiology and biotechnology , inflammation , peptide , biology , immunology , enzyme , endocrinology , receptor
The chemotactice response of human dermal fibroblasts of type I, II, and III human collagens and collagen-derived peptides was quantitated by an in vitro assay. All three native human collagens and constituent alpha chains can serve as chemoattractants for fibroblasts in vitro. When type I, II, and III collagens were digested by bacterial collagenase, the resulting peptides were also chemotactic. In addition, synthetic di- and tripeptides containing hydroxyproline were also chemotactic for fibroblasts. Since collagen is degraded and remodeled at sites of tissue injury and inflammation, these findings suggest that collagen and collagen-degradation peptides might function as chemotactic stimuli for fibroblasts in vivo and attract these cells to effect repair of damaged tissue.