Synergistic enhancement of human bone marrow stromal cell proliferation and osteogenic differentiation on BMP-2-derived and RGD peptide concentration gradients.

Published

Journal Article

Rational design of bioactive tissue engineered scaffolds for directing bone regeneration in vivo requires a comprehensive understanding of cell interactions with the immobilized bioactive molecules. In the current study, substrates possessing gradient concentrations of immobilized peptides were used to measure the concentration-dependent proliferation and osteogenic differentiation of human bone marrow stromal cells. Two bioactive peptides, one derived from extracellular matrix protein (ECM), GRGDS, and one from bone morphogenic protein-2 (BMP-2), KIPKASSVPTELSAISTLYL, were found to synergistically enhance cell proliferation, up-regulate osteogenic mRNA markers bone sialoprotein (BSP) and Runt-related transcription factor 2, and produce mineralization at densities greater than 130 pmol cm(-2) (65 pmol cm(-2) for each peptide). In addition, COOH-terminated self-assembled monolayers alone led to up-regulated BSP mRNA levels at densities above 200 pmol cm(-2) and increased cell proliferation from day 3 to day 14. Taking further advantage of both the synergistic potentials and the concentration-dependent activities of ECM and growth-factor-derived peptides on proliferative activity and osteogenic differentiation, without the need for additional osteogenic supplements, will enable the successful incorporation of the bioactive species into biorelevant tissue engineering scaffolds.

Full Text

Duke Authors

Cited Authors

  • Moore, NM; Lin, NJ; Gallant, ND; Becker, ML

Published Date

  • May 2011

Published In

Volume / Issue

  • 7 / 5

Start / End Page

  • 2091 - 2100

PubMed ID

  • 21272672

Pubmed Central ID

  • 21272672

Electronic International Standard Serial Number (EISSN)

  • 1878-7568

International Standard Serial Number (ISSN)

  • 1742-7061

Digital Object Identifier (DOI)

  • 10.1016/j.actbio.2011.01.019

Language

  • eng