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Recombinant Collagen I Peptide Microcarriers for Cell Expansion and Their Potential Use As Cell Delivery System in a Bioreactor Model
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Recombinant Collagen I Peptide Microcarriers for Cell Expansion and Their Potential Use As Cell Delivery System in a Bioreactor Model

Published on: February 7, 2018

Perlecan domain I promotes fibroblast growth factor 2 delivery in collagen I fibril scaffolds

W D Yang1, R R Gomes, M Alicknavitch

  • 1Department of Biological Sciences, University of Delaware, Newark, Delaware 19716, USA.

Tissue Engineering
|March 2, 2005
PubMed

Insights

Perlecan domain I (PlnDI) with heparan sulfate integrates into collagen scaffolds, enhancing fibroblast growth factor 2 (FGF-2) binding. These scaffolds support osteoblastic and stromal cell growth, mimicking natural extracellular matrices for tissue regeneration.

Area of Science:

  • Biomaterials Science
  • Extracellular Matrix Biology
  • Tissue Engineering

Background:

  • Perlecan is a heparan sulfate proteoglycan vital for tissue development and physiological functions.
  • Heparan sulfate chains on perlecan bind and enhance growth factor activity, particularly FGF-2.
  • Domain I of perlecan (PlnDI) is known to possess significant biological activities.

Purpose of the Study:

  • To investigate the utility of recombinant, glycosaminoglycan-bearing PlnDI in creating collagen I-based scaffolds.
  • To assess the binding of PlnDI to collagen I fibrils and the role of heparan sulfate chains.
  • To evaluate the efficacy of PlnDI-containing scaffolds in supporting cell growth and mimicking the extracellular matrix.

Main Methods:

  • Recombinant PlnDI with glycosaminoglycans was used to create three-dimensional scaffolds with collagen I.
  • Binding affinity of PlnDI to collagen I fibrils, monomers, and denatured preparations was assessed.
  • Heparitinase digestion was employed to confirm the presence and importance of heparan sulfate chains on PlnDI.
  • Cell proliferation assays were performed using MG63 osteoblastic cells and human bone marrow stromal cells (hBMSCs).

Main Results:

  • Collagen I fibrils demonstrated superior binding of PlnDI compared to native monomers or heat-denatured collagen I.
  • Heparan sulfate chains on PlnDI were crucial for its integration into scaffolds and for FGF-2 binding and retention.
  • PlnDI and FGF-2 bound collagen I scaffolds significantly enhanced the growth of both MG63 cells and hBMSCs.

Conclusions:

  • Recombinant PlnDI effectively integrates into collagen I scaffolds, leveraging its heparan sulfate chains.
  • These PlnDI-modified scaffolds exhibit enhanced FGF-2 binding and retention capabilities.
  • The developed scaffolds effectively mimic natural extracellular matrices, supporting osteoblastic and stromal cell proliferation, indicating potential for regenerative medicine applications.

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