Biomimetic collagen scaffolds for human bone cell growth and differentiation
Biomimetic collagen scaffolds for human bone cell growth and differentiation
Type I collagen provides a structural framework for connective tissues and plays a central role in the temporal cascade of events leading to the formation of new bone from progenitors. The aim of this study was to examine the ability of the cell-binding domain of type I collagen (P-15 peptide) to promote human bone marrow stromal cell adhesion, proliferation, and differentiation on three-dimensional scaffolds. Human bone marrow stromal cells were selected, expanded, and cultured on particulate microporous ABM ("pure" hydroxyapatite) phase adsorbed with or without P-15 under basal or osteogenic conditions. Immobilized P-15 increased alkaline phosphatase activity and bone morphogenetic protein 2 (BMP-2) gene expression after 1 and 5 days as determined by real-time polymerase chain reaction. P-15 promoted human bone marrow stromal cell attachment, spreading, and alignment on ABM as well as alkaline phosphatase-specific activity in basal and osteogenic cultures. The presence of mineralized bone matrix, extensive cell ingrowth, and cellular bridging between three-dimensional matrices adsorbed with P-15 was confirmed by confocal microscopy, scanning electron microscopy, and alizarin red staining. Negligible cell growth was observed on ABM alone. In vivo diffusion chamber studies using MF1-nu/nu mice showed bone matrix formation and organized collagen formation after 6 weeks. These studies indicate the potential of P-15 to generate appropriate biomimetic microenvironments for osteoblasts and demonstrate the potential for the exploitation of extracellular matrix cues for osteogenesis and, ultimately, bone regeneration.
1148-1159
Yang, X.B.
b0fbe86e-cb70-479b-a80a-4536b17afbdd
Bhatnagar, R.S.
11cf9b00-1d6e-495e-8726-7351151b1fed
Li, S.
be6d14e4-0c49-47a8-a6e0-1c99a64e1024
Oreffo, R.O.C.
ff9fff72-6855-4d0f-bfb2-311d0e8f3778
2004
Yang, X.B.
b0fbe86e-cb70-479b-a80a-4536b17afbdd
Bhatnagar, R.S.
11cf9b00-1d6e-495e-8726-7351151b1fed
Li, S.
be6d14e4-0c49-47a8-a6e0-1c99a64e1024
Oreffo, R.O.C.
ff9fff72-6855-4d0f-bfb2-311d0e8f3778
Yang, X.B., Bhatnagar, R.S., Li, S. and Oreffo, R.O.C.
(2004)
Biomimetic collagen scaffolds for human bone cell growth and differentiation.
Tissue Engineering, 10 (7), .
(doi:10.1089/ten.2004.10.1148).
Abstract
Type I collagen provides a structural framework for connective tissues and plays a central role in the temporal cascade of events leading to the formation of new bone from progenitors. The aim of this study was to examine the ability of the cell-binding domain of type I collagen (P-15 peptide) to promote human bone marrow stromal cell adhesion, proliferation, and differentiation on three-dimensional scaffolds. Human bone marrow stromal cells were selected, expanded, and cultured on particulate microporous ABM ("pure" hydroxyapatite) phase adsorbed with or without P-15 under basal or osteogenic conditions. Immobilized P-15 increased alkaline phosphatase activity and bone morphogenetic protein 2 (BMP-2) gene expression after 1 and 5 days as determined by real-time polymerase chain reaction. P-15 promoted human bone marrow stromal cell attachment, spreading, and alignment on ABM as well as alkaline phosphatase-specific activity in basal and osteogenic cultures. The presence of mineralized bone matrix, extensive cell ingrowth, and cellular bridging between three-dimensional matrices adsorbed with P-15 was confirmed by confocal microscopy, scanning electron microscopy, and alizarin red staining. Negligible cell growth was observed on ABM alone. In vivo diffusion chamber studies using MF1-nu/nu mice showed bone matrix formation and organized collagen formation after 6 weeks. These studies indicate the potential of P-15 to generate appropriate biomimetic microenvironments for osteoblasts and demonstrate the potential for the exploitation of extracellular matrix cues for osteogenesis and, ultimately, bone regeneration.
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Published date: 2004
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Local EPrints ID: 26141
URI: http://eprints.soton.ac.uk/id/eprint/26141
ISSN: 1076-3279
PURE UUID: b5809bac-1300-4624-a1ca-cb1cdf1e3931
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Date deposited: 12 Apr 2006
Last modified: 16 Mar 2024 03:11
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Author:
X.B. Yang
Author:
R.S. Bhatnagar
Author:
S. Li
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