+1 Recommend
0 collections
      • Record: found
      • Abstract: found
      • Article: not found

      Promotion of fibroblast adhesion by triple-helical peptide models of type I collagen-derived sequences.

      The Journal of Biological Chemistry

      Receptors, Collagen, Amino Acid Sequence, Cell Adhesion, drug effects, Collagen, chemistry, metabolism, Fibroblasts, cytology, Humans, Integrin alpha1beta1, Integrins, Molecular Sequence Data, Peptides, pharmacology, Protein Conformation

      Read this article at

          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.


          The dissection of the activities mediated by type I collagen requires an approach by which the influence of triple-helical conformation can be evaluated. The alpha 1 beta 1 and alpha 2 beta 1 integrin binding sites within type I collagen are dependent upon triple-helical conformation and contained within residues 14-822 from alpha 1(I). Seven alpha 1(I)-derived triple-helical peptides (THPs) were synthesized based on charge clustering (alpha 1(I)256-270, alpha 1(I)385-396, alpha 1(I)406-417, alpha 1(I)415-423, alpha 1(I)448-456, alpha 1(I)496-507, and alpha 1(I)526-537). Three additional THPs were synthesized (alpha 1(I)85-96, alpha 1(I)433-441, and alpha 1(I)772-786) based on previously described or proposed activities (Kleinman, H. K., McGoodwin, E.B., Martin, G. R., Klebe, R. J., Fietzek, P. P., and Wooley, D. E. (1978) J. Biol. Chem. 253, 5642-5646; Staatz, W. D., Foik, K. F., Zutter, M. M., Adams, S. P., Rodriquez, B. A., and Santoro, S. A. (1991) J. Biol. Chem. 266, 7363-7367; San Antonio, J. D., Lander, A. D., Karnovsky, M. J., and Slayter, H. S. (1994) J. Cell Biol. 125, 1179-1188). Of the ten THPs, alpha 1(I)772-786 THP had the greatest activity, with half-maximal normal dermal fibroblast adhesion occurring at a peptide concentration of 1.6 microM. Triple-helicity was essential for activity of this sequence, as the non-triple-helical peptide analog (alpha 1(I)772-786 SSP) exhibited considerably lower levels of cell adhesion promotion even at peptide concentrations as high as 100 microM. Within the sequence itself, residues 784-786 (Gly-Leu-Hyp) were important for cellular recognition, as the alpha 1(I)772-783 THP had greatly reduced cell adhesion activity compared with alpha 1(I)772-786 THP. Preliminary studies indicate that the beta 1 integrin subunit mediates fibroblast adhesion to alpha 1(I)772-786 THP. The identification of fibroblast integrin binding sites within type I collagen may have important implications for understanding collagen metabolism.

          Related collections

          Author and article information



          Comment on this article