Biological activity of extracellular matrix-associated BMP-2

F Philipp Seib; Babette Lanfer; Martin Bornhäuser; Carsten Werner

doi:10.1002/term.240

Biological activity of extracellular matrix-associated BMP-2

F Philipp Seib, Babette Lanfer, Martin Bornhäuser, Carsten Werner

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

Abstract

The critical requirement for matrix-associated bone morphogenetic proteins (BMPs) during induction of bone formation in vivo has long been recognized. However, the role of extracellular matrix (ECM) physisorbed BMPs in inducing the differentiation of resident mesenchymal stem cells into osteoblasts has been ill-defined. We therefore used BMP-responsive C2C12s to study the biological activity of collagen type I physisorbed BMP-2. Fibrillar collagen type I scaffolds were loaded with 75 ng BMP-2/microg collagen. Under cell culture conditions, 40% of loaded (125)I-labelled BMP-2 was released within 24 h, whereas the remaining BMP-2 was stably physisorbed for > 7 days. Using these systems suggested that physisorbed BMP-2 is more active than diffusible BMP-2. Thus, the current clinical practice of immobilizing BMPs on collagen type I scaffolds not only prolongs local delivery of the morphogen but could also enhance biological activity at the cellular level.

Original language	English
Pages (from-to)	324-327
Number of pages	4
Journal	Journal of Tissue Engineering and Regenerative Medicine
Volume	4
Issue number	4
DOIs	https://doi.org/10.1002/term.240
Publication status	Published - Jun 2010

Keywords

extracellular matrix
bone morphogenetic protein
osteogenesis
physisorption

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10.1002/term.240

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abstract = "The critical requirement for matrix-associated bone morphogenetic proteins (BMPs) during induction of bone formation in vivo has long been recognized. However, the role of extracellular matrix (ECM) physisorbed BMPs in inducing the differentiation of resident mesenchymal stem cells into osteoblasts has been ill-defined. We therefore used BMP-responsive C2C12s to study the biological activity of collagen type I physisorbed BMP-2. Fibrillar collagen type I scaffolds were loaded with 75 ng BMP-2/microg collagen. Under cell culture conditions, 40% of loaded (125)I-labelled BMP-2 was released within 24 h, whereas the remaining BMP-2 was stably physisorbed for > 7 days. Using these systems suggested that physisorbed BMP-2 is more active than diffusible BMP-2. Thus, the current clinical practice of immobilizing BMPs on collagen type I scaffolds not only prolongs local delivery of the morphogen but could also enhance biological activity at the cellular level.",

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T1 - Biological activity of extracellular matrix-associated BMP-2

AU - Seib, F Philipp

AU - Lanfer, Babette

AU - Bornhäuser, Martin

AU - Werner, Carsten

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AB - The critical requirement for matrix-associated bone morphogenetic proteins (BMPs) during induction of bone formation in vivo has long been recognized. However, the role of extracellular matrix (ECM) physisorbed BMPs in inducing the differentiation of resident mesenchymal stem cells into osteoblasts has been ill-defined. We therefore used BMP-responsive C2C12s to study the biological activity of collagen type I physisorbed BMP-2. Fibrillar collagen type I scaffolds were loaded with 75 ng BMP-2/microg collagen. Under cell culture conditions, 40% of loaded (125)I-labelled BMP-2 was released within 24 h, whereas the remaining BMP-2 was stably physisorbed for > 7 days. Using these systems suggested that physisorbed BMP-2 is more active than diffusible BMP-2. Thus, the current clinical practice of immobilizing BMPs on collagen type I scaffolds not only prolongs local delivery of the morphogen but could also enhance biological activity at the cellular level.

KW - extracellular matrix

KW - bone morphogenetic protein

KW - osteogenesis

KW - physisorption

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DO - 10.1002/term.240

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Biological activity of extracellular matrix-associated BMP-2

Abstract

Keywords

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