



@article {3315,
	title = {Role of sparc in bone remodeling and cancer-related bone metastasis},
	journal = {Journal of Cellular Biochemistry},
	volume = {115},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {17 - 26},
	abstract = {There is a growing socioeconomic recognition that clinical bone diseases such as bone infections, bone tumors and osteoporotic bone loss mainly associated with ageing, are major issues in today{\textquoteright}s society. SPARC (secreted protein, acidic and rich in cysteine), a matricellular glycoprotein, may be a promising therapeutic target for preventing or treating bone-related diseases. In fact, SPARC is associated with tissue remodeling, repair, development, cell turnover, bone mineralization and may also participate in growth and progression of tumors, namely cancer-related bone metastasis. Yet, the function of SPARC in such biological processes is poorly understood and controversial. The main objective of this work is to review the current knowledge related to the activity of SPARC in bone remodeling, tumorigenesis, and bone metastasis. Progress in understanding SPARC biology may provide novel strategies for bone regeneration and the development of anti-angiogenic, anti-proliferative, or counter-adhesive treatments specifically against bone metastasis. {\textcopyright} 2013 Wiley Periodicals, Inc. {\textcopyright} 2013 Wiley Periodicals, Inc.},
	keywords = {BONE METASTASIS, bone remodeling, SPARC, TUMORIGENESIS},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84887856025\&partnerID=40\&md5=bcb4dc43db0bb9be75051f4493c74d3d},
	author = {Ribeiro, N. and Sousa, S.R. and Brekken, R.A. and Monteiro, F.J.}
}
@article {2880,
	title = {Endothelialization of chitosan porous conduits via immobilization of a recombinant fibronectin fragment (rhFNIII7-10)},
	journal = {Acta Biomaterialia},
	volume = {9},
	year = {2013},
	note = {Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {5643 - 5652},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84873199566\&partnerID=40\&md5=f548695261ada2fc57ece26bff1f45d0},
	author = {Amaral, I.F. and Neiva, I. and Ferreira da Silva, F. and Sousa, S.R. and Piloto, A.M. and Lopes, C.D.F. and Barbosa, M.A. and Kirkpatrick, C.J. and P{\^e}go, A.P.}
}
@booklet {2179,
	title = {Endothelialization of chitosan porous conduits via immobilization of a recombinant fibronectin fragment (rhFNIII                    7-10)
},
	howpublished = {Acta BiomaterialiaActa Biomater.},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusArticle in Pressdoi: 10.1016/j.actbio.2012.10.029Language of Original Document: EnglishCorrespondence Address: Amaral, I.F.; INEB - Instituto de Engenharia Biom{\'e}dica, Universidade do Porto, Rua do Campo Alegre, 823, 41email: iamaral@ineb.up.pt},
	month = {2012///},
	abstract = {The present study aimed to develop a pre-endothelialized chitosan (CH) porous hollowed scaffold for application in spinal cord regenerative therapies. CH conduits with different degrees of acetylation (DA; 4\% and 15\%) were prepared, characterized (microstructure, porosity and water uptake) and functionalized with a recombinant fragment of human fibronectin (rhFNIII                        7-10). Immobilized rhFNIII 
                        7-10 was characterized in terms of amount ( 
                        125I-radiolabelling), exposure of cell-binding domains (immunofluorescence) and ability to mediate endothelial cell (EC) adhesion and cytoskeletal rearrangement. Functionalized conduits revealed a linear increase in immobilized rhFNIII 
                        7-10 with rhFNIII 
                        7-10 concentration, and, for the same concentration, higher amounts of rhFNIII 
                        7-10 on DA 4\% compared with DA 15\%. Moreover, rhFNIII 
                        7-10 concentrations as low as 5 and 20 μg ml 
},
	keywords = {Protein conformation, Protein radiolabelling, Spinal cord injury, Surface grafting, Three-dimensional scaffolds},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84868680582\&partnerID=40\&md5=6599fd2565f4511b94e944978afc8073},
	author = {Amaral, I.F. and Neiva, I. and Ferreira da Silva, F. and Sousa, S.R. and Piloto, A.M. and Lopes, C.D.F. and Barbosa, M.A. and Kirkpatrick, C.J. and P{\^e}go, A.P.}
}
@article {2284,
	title = {Effect of nanoscale topography on fibronectin adsorption, focal adhesion size and matrix organisation},
	journal = {Colloids and Surfaces B: BiointerfacesColloids Surf. B Biointerfaces},
	volume = {77},
	year = {2010},
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},
	month = {2010///},
	pages = {181 - 190},
	abstract = {Phase separation of PLLA/PS (50/50, w/w) solutions during a spin-casting process gives rise to well-defined nanotopographies of 14, 29 and 45. nm deep pits depending on the concentration of the solution. Their influence on the biological activity of fibronectin (FN) was investigated. FN adsorption was quantified by radiolabelling the protein. The amount of adsorbed FN was higher on the 14. nm deep pit nanotopography than on the other two surfaces. FN distribution between valleys and peaks was investigated by AFM combined with image analysis. FN tends to adsorb preferentially on the valleys of the nanotopography only for the 14. nm system and when adsorbed from solutions of concentration lower than 10μg/ml. Higher concentration of the FN solution leads to evenly distribution of the protein throughout the surface; moreover, there is no difference in the distribution of the protein between valleys and peaks for the other two systems (29 and 45. nm) irrespective of the concentration of the FN solution. The biological activity of the adsorbed protein layer was assessed by investigating MC3T3 osteoblast-like cells adhesion, FN reorganisation and late matrix formation on the different substrates. Even if initial cell adhesion is excellent for every substrate, the size of the focal adhesion plaques increases as the size of the pits in the nanotopography does. This is correlated to FN reorganisation, which only takes places on the 29 and 45. nm deep pits surfaces, where enhanced late matrix production was also found. {\textcopyright} 2010 Elsevier B.V.},
	keywords = {3T3 Cells, Adhesion, Adsorption, AFM, animal cell, Animals, article, Atomic force microscopy, Bioactivity, Biological activities, biological activity, Casting process, cell adhesion, Cell Line, concentration (parameters), Concentration (process), Concentration of, Deep pit, Different substrates, Electric currents, extracellular matrix, Fibronectin, Fibronectin adsorption, Fibronectins, focal adhesion, Focal adhesion plaques, Focal adhesions, Humans, Image analysis, Image Processing, Computer-Assisted, isotope labeling, Landforms, matrix, Matrix formation, Mice, Microscopy, Atomic Force, nanomaterial, Nanoscale topography, Nanotechnology, Nanotopographies, Nanotopography, nonhuman, osteoblast, Osteoblast-like cells, Osteoblasts, Phase separation, polylactic acid, polystyrene, priority journal, Protein adsorption, Protein layers, protein localization, Proteins, Radiolabelling, Reorganisation, Substrates, Surface Properties},
	isbn = {09277765 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77950863692\&partnerID=40\&md5=7fe3bdcc0f69cb64fb3ba7e86fe7a80a},
	author = {Gonz{\'a}lez-Garc{\'\i}a, C. and Sousa, S.R. and Moratal, D. and Rico, P. and Salmer{\'o}n-S{\'a}nchez, M.}
}
@article {2248,
	title = {Influence of crystallite size of nanophased hydroxyapatite on fibronectin and osteonectin adsorption and on MC3T3-E1 osteoblast adhesion and morphology},
	journal = {Journal of Colloid and Interface ScienceJ. Colloid Interface Sci.},
	volume = {351},
	year = {2010},
	note = {Cited By (since 1996): 12Export Date: 21 November 2012Source: ScopusCODEN: JCISAdoi: 10.1016/j.jcis.2010.08.013PubMed ID: 20810127Language of Original Document: EnglishCorrespondence Address: Ribeiro, N.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: nribeiro@ineb.up.ptChemicals/CAS: fibronectin, 86088-83-7; hydroxyapatite, 1306-06-5, 51198-94-8; osteonectin, 104052-78-0; protein, 67254-75-5; Ceramics; Durapatite, 1306-06-5; Fibronectins; OsteonectinReferences: Griffith, L.G., Naughton, G., (2002) Science, 295, p. 1009;Webster, T.J., Ergun, C., Doremus, R.H., Siegel, R.W., Bizios, R., (2000) J. Biomed. Mater. Res., 51, pp. 475-483; 
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},
	month = {2010///},
	pages = {398 - 406},
	abstract = {The characteristic topographical features (crystallite dimensions, surface morphology and roughness) of bioceramics may influence the adsorption of proteins relevant to bone regeneration. This work aims at analyzing the influence of two distinct nanophased hydroxyapatite (HA) ceramics, HA725 and HA1000 on fibronectin (FN) and osteonectin (ON) adsorption and MC3T3-E1 osteoblast adhesion and morphology. Both substrates were obtained using the same hydroxyapatite nanocrystals aggregates and applying the sintering temperatures of 725{\textdegree}C and 1000{\textdegree}C, respectively. The two proteins used in this work, FN as an adhesive glycoprotein and ON as a counter-adhesive protein, are known to be involved in the early stages of osteogenesis (cell adhesion, mobility and proliferation). The properties of the nanoHA substrates had an important role in the adsorption behavior of the two studied proteins and clearly affected the MC3T3-E1 morphology, distribution and metabolic activity. HA1000 surfaces presenting slightly larger grain size, higher root-mean-square roughness (Rq), lower surface area and porosity, allowed for higher amounts of both proteins adsorbed. These substrates also revealed increased number of exposed FN cell-binding domains as well as higher affinity for osteonectin. Regarding the osteoblast adhesion results, improved viability and cell number were found for HA1000 surfaces as compared to HA725 ones, independently of the presence or type of adsorbed protein. Therefore the osteoblast adhesion and metabolic activity seemed to be more sensitive to surfaces morphology and roughness than to the type of adsorbed proteins. {\textcopyright} 2010 Elsevier Inc.},
	keywords = {Adhesion, Adhesive proteins, Adsorption, Adsorption behavior, Animals, Apatite, article, Bioceramics, Biological materials, Biomaterials, bone development, Bone Regeneration, cell adhesion, Cell Count, cell metabolism, cell motility, Cell number, cell proliferation, cell strain 3T3, cell structure, Cell-binding domain, Cells, Cultured, cellular distribution, ceramics, controlled study, Crystallite dimension, Crystallite size, Crystallization, Durapatite, Fibronectin, Fibronectin adsorption, Fibronectins, glycoprotein, grain, Grain size, human, human cell, hydroxyapatite, Hydroxyapatite nanocrystals, MC3T3-E1, Metabolic activity, metabolism, Mice, morphology, Nano-HA, nanocrystal, nanoparticles, Nanophased hydroxyapatite, osteoblast, Osteoblast adhesion, Osteoblast morphology, Osteoblasts, Osteogenesis, osteonectin, Osteonectin adsorption, Particle Size, porosity, priority journal, protein, Proteins, Root mean square roughness, Sintering, Sintering temperatures, Surface area, Surface Properties, surface property, Surface roughness, temperature, Topographical features},
	isbn = {00219797 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77957328472\&partnerID=40\&md5=c4a13ccec89e04dbfe1920fd42fec3f5},
	author = {Ribeiro, N. and Sousa, S.R. and Monteiro, F.J.}
}
@article {2297,
	title = {Fibronectin-mediated endothelialisation of chitosan porous matrices},
	journal = {BiomaterialsBiomaterials},
	volume = {30},
	year = {2009},
	note = {Cited By (since 1996): 8Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2009.06.056PubMed ID: 19615736Language of Original Document: EnglishCorrespondence Address: Amaral, I.F.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: iamaral@ineb.up.ptChemicals/CAS: chitosan, 9012-76-4; fibronectin, 86088-83-7; Biocompatible Materials; Chitosan, 9012-76-4; FibronectinsReferences: Moon, J.J., West, J.L., Vascularization of engineered tissues: approaches to promote angiogenesis in biomaterials (2008) Current Topics in Medicinal Chemistry, 8 (4), pp. 300-310;Blitterswijk, C.A., Moroni, L., Rouwkema, J., Siddappa, R., Sohier, J., Tissue engineering - an introduction (2008) Tissue engineering, , Blitterswijk C.A. (Ed), Elsevier; 
Ehrbar, M., Zeisberger, S.M., Raeber, G.P., Hubbell, J.A., Schnell, C., Zisch, A.H., The role of actively released fibrin-conjugated VEGF for VEGF receptor 2 gene activation and the enhancement of angiogenesis (2008) Biomaterials, 29 (11), pp. 1720-1729; 
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},
	month = {2009///},
	pages = {5465 - 5475},
	abstract = {Chitosan (Ch) porous matrices were investigated regarding their ability to be colonized by human microvascular endothelial cells (HPMEC-ST1.6R cell line) and macrovascular endothelial cells namely HUVECs. Specifically we assessed if previous incubation of Ch in a fibronectin (FN) solution was effective in promoting endothelial cell (EC) adhesion to Ch matrices with different degrees of acetylation (DAs). Upon FN physiadsorption, marked differences were found between the two DAs investigated, namely DA 4\% and 15\%. While cell adhesion was impaired on Ch with DA 15\%, ECs were able to not only adhere to Ch with DA 4\%, but also to spread and colonize the scaffolds, with retention of the EC phenotype and angiogenic potential. To explain the observed differences between the two DAs, protein adsorption studies using                        125I-FN and immunofluorescent labelling of FN cell-binding domains were carried out. In agreement with the higher cell numbers found, scaffolds with DA 4\% revealed a higher number of exposed FN cell-binding domains as well as greater ability to adsorb FN and to retain and exchange adsorbed FN in the presence of competitive proteins. These findings suggest that the DA is a key parameter modulating EC adhesion to FN-coated Ch by influencing the adsorbed protein layer. {\textcopyright} 2009 Elsevier Ltd. All rights reserved.
},
	keywords = {Acetylation, Adhesion, Adsorption, angiogenesis, article, Biocompatible Materials, Blood vessel prostheses, cell adhesion, Cell culture, cell invasion, Cell Line, Cell lines, Cell membranes, Cell number, cell proliferation, Cell size, cell spreading, cell survival, Cell-binding domain, Chitin, Chitin/chitosan, chitosan, colony formation, controlled study, Degrees of acetylation, Electric conductivity measurement, Electric currents, Endothelial cell, Endothelial Cells, Endothelialisation, endothelium, endothelium cell, epithelization, Fibronectin, Fibronectins, human, human cell, Human microvascular endothelial cells, Humans, immunofluorescence test, Key parameters, Labels, materials testing, Matrix algebra, Neovascularization, Physiologic, phenotype, porosity, Porous matrixs, priority journal, Protein adsorption, Protein layers, Scaffold, Scaffolds, Self assembly, Tissue engineering, tissue scaffold, umbilical vein},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-68549107574\&partnerID=40\&md5=9babb57c1a4f2ae6eb7e7e0643bffe48},
	author = {Amaral, I.F. and Unger, R.E. and Fuchs, S. and Mendon{\c c}a, A.M. and Sousa, S.R. and Barbosa, M.A. and P{\^e}go, A.P. and Kirkpatrick, C.J.}
}
@article {2359,
	title = {Osteoblast adhesion and morphology on TiO                    2 depends on the competitive preadsorption of albumin and fibronectin
},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {84},
	year = {2008},
	note = {Cited By (since 1996): 34Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.31201PubMed ID: 17607748Language of Original Document: EnglishCorrespondence Address: Sousa, S.R.; INEB - Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomaterials, R. do Campo Alegre, 823, 4150-180 Porto, Portugal; email: ssousa@ibmc.up.ptChemicals/CAS: fibronectin, 86088-83-7; human serum albumin, 9048-49-1; hydrogen peroxide, 7722-84-1; iodine 125, 14158-31-7, 22822-81-7; titanium dioxide, 1317-70-0, 1317-80-2, 13463-67-7, 51745-87-0; Albumins; Coloring Agents; Fibronectins; Iodine Radioisotopes; Neutral Red, 553-24-2; titanium dioxide, 13463-67-7; Titanium, 7440-32-6References: Anselme, K., Osteoblast adhesion on biomaterials (2000) Biomaterials, 21, pp. 667-681;Tidwell, C.D., Ertel, S.I., Ratner, B.D., Tarasevich, B.J., Atre, S., Allara, D.L., Endothelial cell growth and protein adsorption on terminally functionalized, self-assembled monolayers of alkane-thiolates on gold (1997) Langmuir, 13, pp. 3404-3413; 
Malmsten, M., Lassen, B., Competitive adsorption at hydrophobic surfaces from binary protein systems (1994) J Colloid Interface Sci, 166, pp. 490-498; 
Koenig, A.L., Gambillara, V., Grainger, D.W., Correlating fibronectin adsorption with endothelial cell adhesion and signaling on polymer substrates (2003) J Biomed Mater Res A, 64, pp. 20-37; 
Horbett, T.A., The role of adsorbed proteins in animal cell adhesion (1994) Colloids Surf B, 2, pp. 225-240; 
Huang, H.H., Ho, C.T., Lee, T.H., Lee, T.L., Liao, K.K., Chen, F.L., Effect of surface roughness of ground titanium on initial cell adhesion (2004) Biomol Eng, 21, pp. 93-97; 
Vitte, J., Benoliel, A.M., Pierres, A., Bongrand, P., Is there a predictable relationship between surface physical-chemical properties and cell behaviour at the interface? (2004) Eur Cell Mater, 7, pp. 52-63; 
Tsai, W.B., Grunkemeier, J.M., McFarland, C.D., Horbett, T.A., Platelet adhesion to polystyrene-based surfaces preadsorbed with plasmas selectively depleted in fibrinogen, fibronectin, vitronectin, or von Willebrand{\textquoteright}s factor (2002) J Biomed Mater Res, 60, pp. 348-359; 
Grainger, D.W., Pavon-Djavid, G., Migonney, V., Josefowicz, M., Assessment of fibronectin conformation adsorbed to polytetrafluoroethylene surfaces from serum protein mixtures and correlation to support of cell attachment in culture (2003) J Biomater Sci Polym Ed, 14, pp. 973-988; 
Goncalves, I.C., Martins, M.C.L., Barbosa, M.A., Ratner, B.D., Protein adsorption on 18-alkyl chains immobilized on hydroxyl-terminated self-assembled monolayers (2005) Biomaterials, 26, pp. 3891-3899; 
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Amaral, I.F., Lamghari, M., Sousa, S.R., Sampaio, P., Barbosa, M.A., Rat bone marrow stromal cell osteogenic differentiation and fibronectin adsorption on chitosan membranes: The effect of the degree of acetylation (2005) J Biomed Mater Res A, 75, pp. 387-397; 
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},
	month = {2008///},
	pages = {281 - 290},
	abstract = {This study aims at assessing the influence of the competitive preadsorption of human 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 TiO                        2 substrates. One was commercially pure titanium with a titanium oxide layer formed in an H
                        2O
                        2 solution and the other TiO
                        2 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, 
                        125I-FN and 
                        125I-HSA. Our results indicated that MC3T3-E1 osteoblast adhesion correlates well with the amounts of FN and HSA adsorbed on TiO
                        2 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 TiO
                        2 in a favorable conformation and does not suffers subsequent conformational changes allowing exchange with other FN molecules in solution. {\textcopyright} 2007 Wiley Periodicals, Inc.
},
	keywords = {2, 3T3 Cells, Adsorption, Albumins, animal cell, Animals, article, binding kinetics, cell adhesion, Coloring Agents, Competitive protein adsorption, controlled study, cytoskeleton, Data Interpretation, Statistical, Fibronectin, Fibronectins, FN, HSA, human serum albumin, hydrogen peroxide, iodine 125, Iodine Radioisotopes, isotope labeling, Mice, Microscopy, Confocal, mouse, neutral red, nonhuman, osteoblast, Osteoblast adhesion, Osteoblasts, Protein radiolabeling, Proteins, Radiology, Solutions, Sterilization, surface property, TiO, Titanium, Titanium dioxide},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-38049002555\&partnerID=40\&md5=dd5a4dee91d3fe1e9eb9a6ba31553c0a},
	author = {Sousa, S.R. and Lamghari, M. and Sampaio, P. and Moradas-Ferreira, P. and Barbosa, M.A.}
}
@article {2444,
	title = {Rat bone marrow stromal cell osteogenic differentiation and fibronectin adsorption on chitosan membranes: The effect of the degree of acetylation},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {75},
	year = {2005},
	note = {Cited By (since 1996): 25Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.30436PubMed ID: 16092111Language of Original Document: EnglishCorrespondence Address: Amaral, I.F.; INEB-Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: iamaral@ineb.up.ptChemicals/CAS: chitosan, 9012-76-4; fibronectin, 86088-83-7; polystyrene, 9003-53-6; Chitosan, 9012-76-4; Coated Materials, Biocompatible; FibronectinsReferences: VandeVord, P.J., Matthew, H.W.T., DeSilva, S.P., Mayton, L., Wu, B., Wooley, P.H., Evaluation of the biocompatibility of a chitosan scaffold in mice (2002) J Biomed Mater Res, 59 (3), pp. 585-590;Muzzarelli, R.A.A., Human enzymatic activities related to the therapeutic administration of chitin derivatives (1997) Cell Mol Life Sci, (53), pp. 131-140; 
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},
	month = {2005///},
	pages = {387 - 397},
	abstract = {Cell adhesion, migration, and proliferation of a few anchorage-dependent cells cultured on chitosan (Ch) matrices are influenced by the degree of N-acetylation (DA) of Ch. In the present work, we examined the influence of the DA on the attachment, spreading, proliferation, and osteogenic differentiation of rat bone marrow stromal cells (rBM-SCs). Ch membranes were characterized in terms of surface morphology, roughness, and wettability, and in terms of adsorption of an adhesive protein, fibronectin (Fn). Chs with DAs in the range of 4 to 49\% were used. Among the Ch samples, the DA of 4\% led to the highest Fn surface concentration, both from single protein solution and from diluted serum. Furthermore, the levels of Fn adsorbed from serum found for this DA were threefold higher than for the tissue culture polystyrene control, indicating that in the presence of competitive proteins Ch is more specific toward Fn adsorption than tissue culture polystyrene. rBMSCs cultured on Ch carrying a DA of 4\% were able to spread, proliferate, and differentiate, reaching a higher level of osteogenic differentiation than on the control, despite the lower cell attachment observed for all Ch samples. Because the Ch sample with a DA of 4\% showed the highest Fn adsorption from serum, we suggest that cell adhesion, spreading, and osteogenic differentiation of rBMSCs on Ch may be mediated by the adsorbed layer of Fn. {\textcopyright} 2005 Wiley Periodicals, Inc.},
	keywords = {Acetylation, Adhesion, Adsorption, animal cell, Animals, article, artificial membrane, binding affinity, binding competition, Bone, bone development, bone marrow cell, Bone Marrow Cells, Bone marrow stomal cells, Bone marrow stromal cells, cell adhesion, cell anchorage, Cell culture, cell differentiation, Cell membranes, cell migration, cell proliferation, Cell Shape, cell spreading, chitosan, Coated Materials, Biocompatible, controlled study, cytoskeleton, Degree of acetylation, Fibronectin, Fibronectins, male, materials testing, morphology, nonhuman, polystyrene, Proteins, rat, Rats, Rats, Wistar, roughness, stroma cell, Stromal Cells, Surface Properties, surface property, Tissue culture, wettability},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-26844551535\&partnerID=40\&md5=fa91e3e29d946053ae7bb231b6a2640e},
	author = {Amaral, I.F. and Lamghari, M. and Sousa, S.R. and Sampaio, P. and Barbosa, M.A.}
}
@article {2431,
	title = {TiO                    2 type influences fibronectin adsorption
},
	journal = {Journal of Materials Science: Materials in MedicineJ. Mater. Sci. Mater. Med.},
	volume = {16},
	year = {2005},
	note = {Cited By (since 1996): 28Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1007/s10856-005-4725-4Language of Original Document: EnglishCorrespondence Address: Sousa, S.R.; INEB, Instituto de Engenharia Biom{\'e}dica, Lab. Biomateriais, R. do Campo Alegre, 823, 4150-180 Porto, Portugal; email: ssousa@ibmc.up.ptChemicals/CAS: fibronectin, 86088-83-7; titanium dioxide, 1317-70-0, 1317-80-2, 13463-67-7, 51745-87-0; titanium, 7440-32-6; hydrogen peroxide, 7722-84-1; iodine 125, 14158-31-7, 22822-81-7; Fibronectins; Solutions; titanium dioxide, 13463-67-7; Titanium, 7440-32-6References: Horbett, T.A., (1994) Colloids and Surfaces B: Biointerfaces, 2, p. 225;Amaral, I.F., Lamghari, M., Sousa, S.R., Sampaio, P., Barbosa, M.A., (2005) J Biomed Mater Res., 75 A, p. 387; 
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},
	month = {2005///},
	pages = {1173 - 1178},
	abstract = {Human fibronectin (FN) plays a key role in the biointegration of implants as the success depends on adsorption of proteins like FN [1]. Indeed FN can be an intermediary between the biomaterial surface and cells. The adsorption of human fibronectin (FN) on commercially pure titanium with a titanium oxide layer formed in a H                        2O
                        2 solution (TiO
                        2 cp) and TiO
                        2 sputtered on Si (TiO
                        2 sp) was studied. Adsorption isotherms and the work of adhesion were assessed by wettability studies, X-ray photoelectron spectroscopy (XPS), and by radiolabelling of FN with 
                        125I, 
                        125I-FN. Exchangeability of bound FN by free FN, was also evaluated by the radiolabelling technique. Contact angle determinations have shown that FN displays higher affinity for the TiO
                        2 cp surface than for the TiO
                        2 sp. As expected from the surface free energy values, the work of adhesion of FN is higher for the TiO
                        2 cp substrate, the more hydrophilic one, and lower for the TiO
                        2 sp substrate, the more hydrophobic one. The adsorption isotherms were evaluated by two different techniques: radiolabelling of FN (
                        125I-FN) and XPS. TiO
                        2 cp adsorbs more FN than the TiO
                        2 sp surfaces as shown by the radiolabelling data. FN molecules are also more strongly attached to the former surface as indicated by the work of adhesion and by the exchangeability studies. Results using 
                        125I-FN also suggests that FN adsorbs as a multilayer for FN concentrations in solution higher than 100 μg/mL. {\textcopyright} 2005 Springer Science + Business Media, Inc.
},
	keywords = {Adsorption, adsorption kinetics, article, binding affinity, Biointegration, Biomaterials, Cells, chemistry, conference paper, Contact angles, Fibronectin, Fibronectins, human, Human fibronectin (FN), Humans, hydrogen peroxide, hydrophilicity, hydrophobicity, Implants (surgical), iodine 125, isotherm, Isotherms, isotope labeling, physical chemistry, priority journal, protein binding, Proteins, Radiolabelling, solution and solubility, Solutions, surface property, Titanium, Titanium dioxide, wettability, X ray photoelectron spectroscopy},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-29144439699\&partnerID=40\&md5=f98f8448d034d8f8627d752516e3afbd},
	author = {Sousa, S.R. and Moradas-Ferreira, P. and Barbosa, M.A.}
}
@article {2472,
	title = {Human serum albumin adsorption on TiO                    2 from single protein solutions and from plasma
},
	journal = {LangmuirLangmuir},
	volume = {20},
	year = {2004},
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Williams, R.L., Williams, D.F., (1988) J. Colloid Interface Sci., 126, pp. 596-603; 
Serro, A.P.V.A., Fernandes, A.C., Saramago, B.D.V., Norde, W., (1999) J. Biomed. Mater. Res., 46, pp. 376-381; 
Norde, W., Anusiem, A.C.I., (1992) Colloids Surf., 86, pp. 73-80; 
Young, B.R., Pitt, W.G., Cooper, S.L., (1988) J. Colloid Interface Sci., 125, pp. 246-260; 
Feng, L., Andrade, J.D., (1994) Biomaterials, 5, pp. 323-333; 
Norde, W., (1986) Adv. Colloid Interface Sci., 25, pp. 267-340; 
Kurrat, R., Prenosil, J.E., Ramsden, J.J., (1987) J. Colloid Interface Sci., 186, pp. 1-8; 
Brash, J.L., Uniyal, S., Samak, Q., (1974) Trans. Am. Soc. Artif. Intern. Organs, 20 A, pp. 69-76
},
	month = {2004///},
	pages = {9745 - 9754},
	abstract = {In the present work, the adsorption of human serum albumin (HSA) on commercially pure titanium with a titanium oxide layer formed in a H                        2O
                        2 solution (TiO
                        2 cp) and on TiO
                        2 sputtered on Si (TiO
                        2 sp) was analyzed. Adsorption isotherms, kinetic studies, and work of adhesion determinations were carried out. HSA exchangeability was also evaluated. Surface characterization was performed by atomic force microscopy (AFM), X-ray photoelectron spectroscopy (XPS), and wettability studies. The two TiO
                        2 surfaces have very distinct roughnesses, the TiO
                        2 sp having a mean R
                        a value 14 times smaller than the one of TiO
                        2 cp. XPS analysis revealed consistent peaks representative of TiO
                        2 on sputtered samples as well as on Ti cp substrate after 48 h of H
                        2O
                        2 immersion. Nitrogen was observed as soon as protein was present, while sulfur, present in disulfide bonds in HSA, was observed for concentrations of protein higher than 0.30 mg/mL. The work of adhesion was determined from contact angle measurements. As expected from the surface free energy values, the work of adhesion of HSA solution is higher for the TiO
                        2 cp substrate, the more hydrophilic one, and lower for the TiO
                        2 sp substrate, the more hydrophobic one. The work of adhesion between plasma and the substrates assumed even higher values for the TiO
                        2 cp surface, indicating a greater interaction between the surface and the complex protein solutions. Adsorption studies by radiolabeling of albumin (
                        125I-HSA) suggest that rapid HSA adsorption takes place on both surfaces, reaching a maximum value after ~60 min of incubation. For the higher HSA concentrations in solution, a multilayer coverage was observed on both substrates. After the adsorption step from single HSA solutions, the exchangeability of adsorbed HSA molecules by HSA in solution was evaluated. The HSA molecules adsorbed on TiO
                        2 sp seem to be more easily exchanged by HSA itself than those adsorbed on TiO
                        2 cp after 24 h. In contrast, after 72 h, nearly all the adsorbed albumin molecules effectively exchange with other albumin molecules.
},
	keywords = {Adsorption, article, Atomic force microscopy, Blood, chemistry, human, Human serum albumin (HSA), Humans, hydrophobicity, Multilayers, plasma, Plasmas, Plastic surgery, Proteins, Radiolabeling, Serum Albumin, solution and solubility, Solutions, Substrates, Surface characterization, Surface Properties, surface property, Titanium, Titanium dioxide, X ray photoelectron spectroscopy},
	isbn = {07437463 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-8344221996\&partnerID=40\&md5=60496aebf9155224cadbbb1456ff8a25},
	author = {Sousa, S.R. and Moradas-Ferreira, P. and Saramago, B. and Viseu Melo, L. and Barbosa, M.A.}
}
@article {2625,
	title = {Effect of hydroxyapatite thickness on metal ion release from Ti6Al4V substrates},
	journal = {BiomaterialsBIOMATERIALS},
	volume = {17},
	year = {1996},
	note = {Cited By (since 1996): 62Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/0142-9612(96)89655-4PubMed ID: 8938233Language of Original Document: EnglishCorrespondence Address: Sousa, S.R.; INEB, Praca do Coronel Pacheco 1, 4050 Porto, PortugalChemicals/CAS: Alloys; Biocompatible Materials; Durapatite, 1306-06-5; titanium alloy (TiAl6V4), 12743-70-3; Titanium, 7440-32-6References: Barbosa, M.A., Electrochemical impedance studies on calcium phosphate-metal interfaces (1991) Bioceramics, 4, pp. 325-333. , Bonfield W, Hastings GW, Tanner KE, eds. London: Butterworth-Heinemann;Sousa, S.R., Barbosa, M.A., Electrochemistry of AISI 316L stainless steel in calcium phosphate and protein solutions (1991) J Mater Sci: Mater Med, 2, pp. 19-26; 
Sousa, S.R., Barbosa, M.A., Corrosion resistance of titanium cp in saline physiological solutions with calcium phosphate and proteins (1993) Clin Mater, 14, pp. 287-294; 
Li, P., De Groot, K., Calcium phosphate formation within sol-gel prepared titania in vitro and in vivo (1993) J Biomed Mater Res, 27, pp. 1495-1500; 
Li, P., Kangasniemi, I., De Groot, K., Bonelike hydroxyapatitc induction by a gel-derived titania and a titanium substrate (1994) J Am Ceram Soc, 77, pp. 1307-1312; 
Ducheyne, P., Healy, K.E., The effect of plasma-sprayed calcium phosphate ceramic coatings on the metal ion release from porous titanium and cobalt-chromium alloys (1988) J Biomed Mater Res, 22, pp. 1137-1163; 
Weng, J., Liu, X., Zhang, X., Li, X., Thermal decomposition of hydroxyapatite structure induced by titanium and its dioxide (1994) J Mater Sci Lett, 13, pp. 159-161; 
Castro Ribeiro, C., Barbosa, M.A., Influence of metal ions on the dissolution behaviour of hydroxyapatite (1991) Bioceramics, 4, pp. 145-153. , Bonfield W, Hastings GW, Tanner KE, eds. Butterworth-Heinemann; 
ASTM G61-86, standard test method for: Conducting cyclic potentiodynamic polarization measurements for localized corrosion susceptibility of iron, nickel, or cobalt based alloys (1989) Annual Book of ASTM Standards, pp. 345-361. , 03.02. Philadelphia, PA: American Society for Testing and Materials; 
ASTM G 31-72 e1, standard practice for: Laboratory immersion corrosion testing of metals (1989) Annual Book of ASTM Standards, pp. 176-186. , 03.02. Philadelphia, PA: American Society for Testing and Materials; 
Barbosa, M.A., Surface layers and the reactivity of metallic implants (1992) Biomaterials - Hard Tissue Repair and Replacement, pp. 257-283. , Muster D et al. ed. Amsterdam: Elsevier Science Publishers BV; 
Rivero, D.P., Fox, J., Skipor, A.K., Urban, R.M., Galante, J.O., Calcium phosphate-coated porous titanium implants for enhanced skeletal fixation (1988) J Biomed Mater Res, 22, pp. 191-201; 
Oonishi, H., Yamamoto, M., Ishimaru, H., The effect of hydroxyapatite coating on bone growth into porous titanium alloy implants (1989) J Bone Joint Surg, 71 B, pp. 213-216; 
Bourne, R.B., Rorabeck, C.H., Burkar, B., Kirk, P.G., Ingrowth surfaces - Plasma spray coating to titanium alloy hip replacements (1994) Clin Orthop Rel Res, 298, pp. 37-46; 
Oonishi, H., Noda, T., Ito, S., Effect of hydroxyapatite coatings on bone growth into porous titanium alloy implants under loaded conditions (1994) J Appl Biomater, 5, pp. 23-37; 
Moroni, A., Caja, V.L., Egger, E.L., Trinchese, L., Chao, E.Y.S., Histomorphometry of hydroxyapatite coated and uncoated porous titanium bone implants (1994) Biomaterials, 15, pp. 926-930; 
Bloebaum, R.D., DuPont, J.A., Osteolysis from a press-fit hydroxyapatite-coated implant (1993) J Arthroplasty, 8, pp. 195-202; 
Bloebaum, R.D., Beeks, D., Dorr, L.D., Savory, C.G., DuPont, J.A., Hofmann, A.A., Complications with hydroxyapatite particulate separation in total hip arthroplasty (1994) Clin Orthop, 298, pp. 19-26; 
Klein, C.P.A.T., Patka, P., Wolke, J.G.C., De Blieck-Hogervorst, J.M.A., De Groot, K., Long-term in vivo study of plasma-sprayed coatings on titanium alloys of tetracalcium phosphate, hydroxyapatite and α-tricalcium phosphate (1994) Biomaterials, 15, pp. 146-160; 
Reis, R.L., Monteiro, F.J., Hastings, G.W., Stability of hydroxyapatite plasma-sprayed coated Ti-6Al-4V under cyclic bending in simulated physiological solutions (1994) J Mater Sci: Mater Med, 5, pp. 457-462; 
Wang, B.C., Lee, T.M., Chang, E., Yang, C.Y., The shear strength and the failure mode of plasma-sprayed hydroxyapatite coating to bone: The effect of coating thickness (1993) J Biomed Mater Res, 27, pp. 1315-1327; 
Tranquilli Leali, P., Merolli, A., Palmacci, O., Gabbi, C., Cacchiolo, A., Gonizzi, G., Evaluation of different preparations of plasma-spray hydroxyapatite coating on titanium alloy and duplex stainless steel in the rabbit (1994) J Mater Sci: Mater Med, 5, pp. 345-349
},
	month = {1996///},
	pages = {397 - 404},
	publisher = {Elsevier Science Ltd},
	abstract = {The electrochemical dissolution behaviour of Ti6Al4V alloy coated with hydroxyapatite (HA) by plasma spraying was studied in Hank{\textquoteright}s balanced salt solution (HBSS) and compared with that of polished and grit-blasted passivated surfaces. Two different nominal thicknesses of HA (50 and 200 μm) were used. Taking a polished passivated surface as reference, grit blasting of the substrate increased the electrical charge used in the oxidation of Ti6Al4V alloy at constant potential, as a result of increased surface area. However, only HA coatings with a thickness of 200 μm were capable of reducing the charge to values lower than those measured for polished surfaces. Electrochemical impedance spectroscopy has also shown that only 200 μm thick coatings are effective in reducing the oxidation rate of the substrate. Furthermore, in potentiostatic experiments the 50 μm thick coating detached from the substrate, which did not occur with the 200 μm thick coating. However, after 6 months immersion in HBSS, detachment occurred in some regions of both coatings. No titanium, aluminium or vanadium were detected in solution by electrothermal atomic absorption spectroscopy. These data indicate that HA is an effective barrier to metal ion release, even for the thinner coatings, due to formation of metal phosphates or to incorporation of metal ions in the HA structure.The electrochemical dissolution behaviour of Ti6Al4V alloy coated with hydroxyapatite (HA) by plasma spraying was studied in Hank{\textquoteright}s balanced salt solution (HBSS) and compared with that of polished and grit-blasted passivated surfaces. Two different nominal thicknesses of HA (50 and 200 μm) were used. Taking a polished passivated surface as reference, grit blasting of the substrate increased the electrical charge used in the oxidation of Ti6Al4V alloy at constant potential, as a result of increased surface area. However, only HA coatings with a thickness of 200 μm were capable of reducing the charge to values lower than those measured for polished surfaces. Electrochemical impedance spectroscopy has also shown that only 200 μm thick coatings are effective in reducing the oxidation rate of the substrate. Furthermore, in potentiostatic experiments the 50 μm thick coating detached from the substrate, which did not occur with the 200 μm thick coating. However, after 6 months immersion in HBSS, detachment occurred in some regions of both coatings. No titanium, aluminium or vanadium were detected in solution by electrothermal atomic absorption spectroscopy. These data indicate that HA is an effective barrier to metal ion release, even for the thinner coatings, due to formation of metal phosphates or to incorporation of metal ions in the HA structure.
},
	keywords = {Absorption spectroscopy, Alloys, Aluminum, article, Atomic spectroscopy, balanced salt solution, Bioactive coatings, Biocompatible Materials, Biomaterials, Calcium Compounds, Dissolution, Durapatite, Electric charge, Electrochemical dissolution, Electrochemical impedance spectroscopy, electrochemistry, Electrothermal atomic absorption spectroscopy, Hank balanced salt solution, hydroxyapatite, Ion release, Ions, metal ion, Metal ion release, Metal phosphates, Microscopy, Electron, Scanning, Oxidation, Plasma spraying, potentiometry, priority journal, Spectrophotometry, Atomic, Spectroscopy, Substrates, thickness, Thickness effect, Time Factors, Titanium, Titanium alloys, vanadium},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0030087995\&partnerID=40\&md5=ec5e4bddc601b37b0dbe58029dd679d4},
	author = {Sousa, S.R. and Barbosa, M.A.}
}
@article {2630,
	title = {The effect of hydroxyapatite thickness on metal ion release from stainless steel substrates},
	journal = {Journal of Materials Science: Materials in MedicineJ. MATER. SCI. MATER. MED.},
	volume = {6},
	year = {1995},
	note = {Cited By (since 1996): 18Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1007/BF00134324Language of Original Document: EnglishCorrespondence Address: Sousa, S.R.; INEB, Instituto Engenharia Biomedica, Praca do Coronel Pacheco, 1, 4050 Porto, Portugal},
	month = {1995///},
	pages = {818 - 823},
	publisher = {Chapman \& Hall Ltd},
	abstract = {The corrosion behaviour of 350 stainless steel coated with hydroxyapatite, HA, by plasma spraying was studied in Hank{\textquoteright}s Balanced Salt Solution, HBSS, and compared with that of polished passivated surfaces. Two different nominal thicknesses, 50 μm and 200 μm, corresponding to what one might consider a thin and a thick coating, respectively, were used. Only HA coatings with a thickness of 200 μm were capable of reducing the electrical charge consumed at constant potential to values lower than those measured for polished surfaces. However, no HA detachment occurred for both thicknesses, as opposed to what has been found in a previous work with Ti6A14V alloy coated with 50 μm HA. No iron, chromium or nickel were detected in solution by Atomic Absorption Spectroscopy with electrothermal atomization (ET-AAS). These elements were also absent from the bulk of the HA coating, both after a 6 month immersion period and electrochemical accelerated tests. The data indicate that in spite of the relatively low corrosion resistance of stainless steel as compared to that of titanium alloys, a thin (50 μm) HA coating prevents the release of metal ions, while remaining adherent to the substrate.The corrosion behaviour of 350 stainless steel coated with hydroxyapatite, HA, by plasma spraying was studied in Hank{\textquoteright}s Balanced Salt Solution, HBSS, and compared with that of polished passivated surfaces. Two different nominal thicknesses, 50 μm and 200 μm, corresponding to what one might consider a thin and a thick coating, respectively, were used. Only HA coatings with a thickness of 200 μm were capable of reducing the electrical charge consumed at constant potential to values lower than those measured for polished surfaces. However, no HA detachment occurred for both thicknesses, as opposed to what has been found in a previous work [1] with Ti6Al4V alloy coated with 50 μm HA. No iron, chromium or nickel were detected in solution by Atomic Absorption Spectroscopy with electrothermal atomization (ET-AAS). These elements were also absent from the bulk of the HA coating, both after a 6 month immersion period and electrochemical accelerated tests. The data indicate that in spite of the relatively low corrosion resistance of stainless steel as compared to that of titanium alloys, a thin (50 μm) HA coating prevents the release of metal ions, while remaining adherent to the substrate.
},
	keywords = {Absorption spectroscopy, atomic absorption spectrometry, Atomic absorption spectroscopy, Atomic spectroscopy, balanced salt solution, Calcium Compounds, Chromium, comparative study, conference paper, Corrosion, Corrosion behaviour, Electric charge, electrochemistry, Hank balanced salt solution, hydroxyapatite, immersion, Inorganic coatings, Ions, Iron, metal ion, Metal ion release, Nickel, Plasma spraying, priority journal, Stainless steel, Stainless steel substrates, Substrates, thickness, Thickness effect, Titanium, Titanium alloys},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0029616612\&partnerID=40\&md5=d2be2280e7407eb6232225ae459f896f},
	author = {Sousa, S.R. and Barbosa, M.A.}
}
