Integrin-mediated adhesion of human mesenchymal stem cells to extracellular matrix proteins adsorbed to polymer surfaces
2012 (English)In: Biomedical Materials, ISSN 1748-6041, Vol. 7, no 3, 035011- p.Article in journal (Refereed) Published
In vitro, degradable aliphatic polyesters are widely used as cell carriers for bone tissue engineering, despite their lack of biological cues. Their biological active surface is rather determined by an adsorbed layer of proteins from the surrounding media. Initial cell fate, including adhesion and proliferation, which are key properties for efficient cell carriers, is determined by the adsorbed layer of proteins. Herein we have investigated the ability of human bone marrow derived stem cells (hBMSC) to adhere to extracellular matrix (ECM) proteins, including fibronectin and vitronectin which are present in plasma and serum. hBMSC expressed integrins for collagens, laminins, fibronectin and vitronectin. Accordingly, hBMSC strongly adhered to these purified ECM proteins by using the corresponding integrins. Although purified fibronectin and vitronectin adsorbed to aliphatic polyesters to a lower extent than to cell culture polystyrene, these low levels were sufficient to mediate adhesion of hBMSC. It was found that plasma- and serum-coated polystyrene adsorbed significant levels of both fibronectin and vitronectin, and fibronectin was identified as the major adhesive component of plasma for hBMSC; however, aliphatic polyesters adsorbed minimal levels of fibronectin under similar conditions resulting in impaired cell adhesion. Altogether, the results suggest that the efficiency of aliphatic polyesters cell carriers could be improved by increasing their ability to adsorb fibronectin.
Place, publisher, year, edition, pages
2012. Vol. 7, no 3, 035011- p.
Marrow Stromal Cells, Osteoblast-Like Cells, Osteogenic Differentiation, In-Vitro, Bone Regeneration, Ligand-Binding, Collagen-I, Scaffolds, Laminin, Expression
Biomaterials Science Polymer Chemistry Cell Biology
IdentifiersURN: urn:nbn:se:kth:diva-47596DOI: 10.1088/1748-6041/7/3/035011ISI: 000303667600011ScopusID: 2-s2.0-84871506788OAI: oai:DiVA.org:kth-47596DiVA: diva2:455714
FunderEU, European Research Council
QC 20120531. Updated from manuscript to article in journal.2011-11-112011-11-112012-06-07Bibliographically approved