Osteoblast adhesion and morphology on TiO2 depends on the competitive preadsorption of albumin and fibronectin

• Type: Article in International Scientific Journal
• Date: 2008

Authors

SR Sousa (Author) FEUP; M Lamghari (Author) FEUP; P Sampaio (Author) Other; P Moradas-Ferreira (Author) Other; M.A. Barbosa (Author) FEUP

Journal

Title: Journal of Biomedical Materials Research - Part A

Vol. 84A No. 2

Pages: 281-290

ISSN: 1549-3296

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 62 Citations

ISI Web of Science

Scopus - 55 Citations

Scientific classification

FOS: Medical and Health sciences > Medical biotechnology

CORDIS: Technological sciences > Engineering > Biomaterial engineering

Other information

Authenticus ID: P-004-1T0

DOI: 10.1002/jbm.a.31201

Abstract (EN): This study aims at assessing the influence of the competitive preadsorption of liurnan serum albumin (HSA) and human plasma fibronectin (FN) from binary solutions and 10% plasma on MC3T3-E1 osteoblast adhesion and morphology on two types of TiO2 substrates. One was commercially pure titanium with a titanium oxide layer formed in an H2O2 solution and the other TiO2 sputtered on Si (Sousa et al., Langmuir 2004; 20:9745-9754.). The strategy applied in the present investigation was to compare osteoblast adhesion to surfaces preadsorbed with HSA, FN, HSA/FN = 1, HSA/FN = 200, and 10% plasma. The adsorption of proteins was evaluated measuring the amount and the effectiveness of binding with radiolabeled proteins, I-125-FN and I-125-HSA. Our results indicated that MC3T3-E1 osteoblast adhesion correlates well with the amounts of FN and HSA adsorbed on TiO2 surfaces. Also, we found that fewer osteoblasts adhered to both substrates preadsorbed with HSA, HSA/FN = 200, and 10% plasma, after 4 and 24 h, than to the surfaces preadsorbed with FN and HSA/FN = 1. For the latter, FN was able to compensate the inhibitory effect of HSA on osteoblast adhesion. Therefore, the presence of lower amounts of coadsorbed albumin may improve presentation of FN in a more integrin-recognized conformation, suggesting that some degree of molecular packing prevents loss of integrin-binding activity. FN reversibility does not seem to be dependent on the HSA/FN adsorption mass ratio in solution, suggesting that FN competitively adsorbs to TiO2 in a favorable conformation and does not suffers subsequent conformational changes allowing exchange with other FN molecules in solution. (c) 2007 Wiley Periodicals, Inc.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 10