



@article {2237,
	title = {Pectin-based injectable biomaterials for bone tissue engineering},
	journal = {BiomacromoleculesBiomacromolecules},
	volume = {12},
	year = {2011},
	note = {Cited By (since 1996): 6Export Date: 21 November 2012Source: ScopusCODEN: BOMAFdoi: 10.1021/bm101110xPubMed ID: 21302960Language of Original Document: EnglishCorrespondence Address: Munarin, F.; Biomatlab, Bioengineering Department, Politecnico di Milano, Piazza Leonardo da Vinci 32, 20133, Milan, Italy; email: fabiola.munarin@mail.polimi.itChemicals/CAS: arginylglycylaspartic acid, 99896-85-2; osteocalcin, 136461-80-8; pectin, 9000-69-5; Biocompatible Materials; Oligopeptides; Pectins; arginyl-glycyl-aspartic acid, 99896-85-2; pectin, 9000-69-5References: Brown, M.J., Lester, J.N., (1980) Appl. Environ. Microbiol., 40, pp. 179-185;Knox, J.P., (2008) Curr. Opin. Plant Biol., 1, pp. 308-313; 
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},
	month = {2011///},
	pages = {568 - 577},
	abstract = {A variety of natural polymers and proteins are considered to be 3D cell culture structures able to mimic the extracellular matrix (ECM) to promote bone tissue regeneration. Pectin, a natural polysaccharide extracted from the plant cell walls and having a chemical structure similar to alginate, provides interesting properties as artificial ECM. In this work, for the first time, pectin, modified with an RGD-containing oligopeptide or not, is used as an ECM alternative to immobilize cells for bone tissue regeneration. The viability, metabolic activity, morphology, and osteogenic differentiation of immobilized MC3T3-E1 preosteoblats demonstrate the potential of this polysaccharide to keep immobilized cells viable and differentiating. Preosteoblasts immobilized in both types of pectin microspheres maintained a constant viability up to 29 days and were able to differentiate. The grafting of the RGD peptide on pectin backbone induced improved cell adhesion and proliferation within the microspheres. Furthermore, not only did cells grow inside but also theywere able to spread out from themicrospheres and to organize themselves in 3D structures producing a mineralized extracellular matrix. These promising results suggest that pectin can be proposed as an injectable cell vehicle for bone tissue regeneration. {\textcopyright} 2011 American Chemical Society.},
	keywords = {3-D Cell culture, 3D Structure, 3T3 Cells, Adhesion, Alginate, animal cell, Animals, arginylglycylaspartic acid, article, Biocompatible Materials, Biopolymers, Bone, Bone and Bones, Bone Regeneration, bone tissue, Bone tissue engineering, Bone tissue regeneration, carbohydrate analysis, cell adhesion, Cell culture, cell differentiation, cell growth, cell metabolism, cell proliferation, cell spreading, cell structure, cell viability, Cells, Chemical modification, Chemical structure, controlled study, Cryoelectron Microscopy, Extracellular matrices, extracellular matrix, gene expression, immobilized cell, Immobilized cells, Injectable biomaterials, Injections, MC3T3-E1, Metabolic activity, Mice, Microscopy, Electron, Scanning, microsphere, Microspheres, Mineralized extracellular matrixes, mouse, Natural polysaccharide, nonhuman, Oligopeptides, osteoblast, osteocalcin, Osteogenic differentiation, pectin, Pectins, Plant cell culture, Plant cell wall, Preosteoblasts, priority journal, RGD peptide, Three dimensional, Tissue engineering},
	isbn = {15257797 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-79955409005\&partnerID=40\&md5=277a7d5e91116f9a03f144aabda0dd96},
	author = {Munarin, F. and Guerreiro, S.G. and Grellier, M.A. and Tanzi, M.C. and Barbosa, M.A. and Petrini, P. and Granja, P.L.}
}
@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.}
}
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Palha, J.A., Hays, M.T., Morreale De Escobar, G., Episkopou, V., Gottesman, M.E., Saraiva, M.J., Transthyretin is not essential for thyroxine to reach the brain and other tissues in transthyretin-null mice (1997) Am J Physiol, 272, pp. 485-E493; 
Palha, J.A., Fernandes, R., De Escobar, G.M., Episkopou, V., Gottesman, M., Saraiva, M.J., Transthyretin regulates thyroid hormone levels in the choroid plexus, but not in the brain parenchyma: Study in a transthyretin-null mouse model (2000) Endocrinology, 141, pp. 3267-3272; 
Kingery, W.S., Offley, S.C., Guo, T.Z., Davies, M.F., Clark, J.D., Jacobs, C.R., A substance P receptor (NK1) antagonist enhances the widespread osteoporotic effects of sciatic nerve section (2003) Bone, 33, pp. 927-936; 
Hosaka, H., Nagata, A., Yoshida, T., Shibata, T., Nagao, T., Tanaka, T., Saito, Y., Tatsuno, I., Pancreatic polypeptide is secreted from and controls differentiation through its specific receptors in osteoblastic MC3T3-E1 cells (2008) Peptides, 29, pp. 1390-1395; 
Fleming, C.E., Saraiva, M.J., Sousa, M.M., Transthyretin enhances nerve regeneration (2007) J Neurochem, 103, pp. 831-839; 
Sainsbury, A., Cusin, I., Doyle, P., Rohner-Jeanrenaud, F., Jeanrenaud, B., Intracerebroventricular administration of neuropeptide y to normal rats increases obese gene expression in white adipose tissue (1996) Diabetologia, 39, pp. 353-356; 
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Marques, F., Sousa, J.C., Oliveira, P., Oliveira, H.C., Palha, J.A., The absence of transthyretin does not impair regulation of lipid and glucose metabolism (2007) Horm Metab Res, 39, pp. 529-533; 
Maniatopoulos, C., Sodek, J., Melcher, A.H., Bone formation in vitro by stromal cells obtained from bone marrow of young adult rats (1988) Cell Tissue Res, 254, pp. 317-330; 
Salingcarnboriboon, R., Tsuji, K., Komori, T., Nakashima, K., Ezura, Y., Noda, M., Runx2 is a target of mechanical unloading to alter osteoblastic activity and bone formation in vivo (2006) Endocrinology, 147, pp. 2296-2305
},
	month = {2010///},
	pages = {263 - 275},
	abstract = {To better understand the role of neuropeptide Y (NPY) in bone homeostasis, as its function in the regulation of bone mass is unclear, we assessed its expression in this tissue. By immunohistochemistry, we demonstrated, both at embryonic stages and in the adult, that NPY is synthesized by osteoblasts, osteocytes, and chondrocytes. Moreover, peptidylglycine α-amidating monooxygenase, the enzyme responsible for NPY activation by amidation, was also expressed in these cell types. Using transthyretin (TTR) KO mice as a model of augmented NPY levels, we showed that this strain has increased NPY content in the bone, further validating the expression of this neuropeptide by bone cells. Moreover, the higher amidated neuropeptide levels in TTR KO mice were related to increased bone mineral density and trabecular volume. Additionally, RT-PCR analysis established that NPY is not only expressed in MC3T3-E1 osteoblastic cells and bone marrow stromal cells (BMSCs), but is also detectable by RIA in BMSCs undergoing osteoblastic differentiation. In agreement with our in vivo observations, in vitro, TTR KO BMSCs differentiated in osteoblasts had increased NPY levels and exhibited enhanced competence in undergoing osteoblastic differentiation. In summary, this work contributes to a better understanding of the role of NPY in the regulation of bone formation by showing that this neuropeptide is expressed in bone cells and that increased amidated neuropeptide content is related to increased bone mass. {\textcopyright} 2009 FEBS.},
	keywords = {3T3 Cells, alpha amidating enzyme, Amidated neuropeptide, amidation, Amides, animal cell, animal tissue, Animals, article, Base Sequence, Bone Density, bone development, bone marrow cell, Bone Marrow Cells, Bone marrow stromal cells, bone mass, cartilage cell, cell differentiation, Cells, Cultured, Chondrocytes, controlled study, developmental stage, DNA Primers, embryo, embryo development, Homeostasis, immunohistochemistry, male, Mice, Mice, Knockout, mouse, Mus, neuropeptide Y, nonhuman, NPY, ossification, osteoblast, Osteoblastic differentiation, Osteoblasts, osteocyte, Osteocytes, peptide synthesis, prealbumin, priority journal, protein expression, protein function, radioimmunoassay, regulatory mechanism, reverse transcription polymerase chain reaction, RNA, Messenger, stroma cell, Stromal Cells, trabecular bone},
	isbn = {1742464X (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-73649127668\&partnerID=40\&md5=c25c87a8e1206fc9d2b878f9611581dd},
	author = {Nunes, A.F. and Liz, M.A. and Franquinho, F. and Teixeira, L. and Sousa, V. and Chenu, C. and Lamghari, M. and Sousa, M.M.}
}
@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; 
Culp, L.A., Sukenik, C.N., Cell type-specific modulation of fibronectin adhesion functions on chemically-derivatized self-assembled monolayers (1998) J Biomater Sci Polym Ed, 9, pp. 1161-1176; 
Baugh, L., Vogel, V., Structural changes of fibronectin adsorbed to model surfaces probed by fluorescence resonance energy transfer (2004) J Biomed Mater Res A, 69, pp. 525-534; 
McClary, K.B., Ugarova, T., Grainger, D.W., Modulating fibroblast adhesion, spreading, and proliferation using self-assembled monolayer films of alkylthiolates on gold (2000) J Biomed Mater Res, 50, pp. 428-439; 
Sousa, S.R., Moradas-Ferreira, P., Melo, L.V., Saramago, B., Barbosa, M.A., Human serum albumin adsorption on TiO 2 from single protein solutions and from plasma (2004) Langmuir, 20, pp. 9745-9754; 
Gehanno, V., Freitas, P.P., Ferreira, J., Almeida, B., Sousa, J.B., Kling, A., Soares, J.C., Silva, M.F., Ion beam deposition of Mn-Ir spin valves (1999) IEEE Trans Magn, 35, pp. 4361-4367; 
Iodine-125. A Guide to Radioiodination Techniques. Little Chalfont, UK: Amersham Life Science; 1993. p 64Lima, J., Sousa, S.R., Ferreira, A., Barbosa, M.A., Interactions between calcium, phosphate, and albumin on the surface of titanium (2001) J Biomed Mater Res, 55, pp. 45-53; 
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Yang, Y.Z., Cavin, R., Ong, J.L., Protein adsorption on titanium surfaces and their effect on osteoblast attachment (2003) J Biomed Mater Res A, 67, pp. 344-349; 
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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; 
Scotchford, C.A., Gilmore, C.P., Cooper, E., Leggett, G.J., Downes, S., Protein adsorption and human osteoblast-like cell attachment and growth on alkylthiol on gold self-assembled monolayers (2002) J Biomed Mater Res, 59, pp. 84-99; 
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Steele, J.G., Johnson, G., Underwood, P.A., Role of serum vitronectin and fibronectin in adhesion of fibroblasts following seeding onto tissue-culture polystyrene (1992) J Biomed Mater Res, 26, pp. 861-884
},
	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 {2376,
	title = {Upregulation of bone cell differentiation through immobilization within a synthetic extracellular matrix},
	journal = {BiomaterialsBiomaterials},
	volume = {28},
	year = {2007},
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},
	month = {2007///},
	pages = {3644 - 3655},
	abstract = {There is a need for new therapeutic strategies to treat bone defects caused by trauma, disease or tissue loss. Injectable systems for cell transplantation have the advantage of allowing the use of minimally invasive surgical procedures, and thus for less discomfort to patients. In the present study, it is hypothesized that Arg-Gly-Asp (RGD)-coupled in a binary (low and high molecular weight) injectable alginate composition is able to influence bone cell differentiation in a three-dimensional (3D) structure. Viability, metabolic activity, cytoskeleton organization, ultrastructure and differentiation (alkaline phosphatase (ALP), von Kossa, alizarin red stainings and osteocalcin quantification) of immobilized cells were assessed. Cells within RGD-modified alginate microspheres were able to establish more interactions with the synthetic extracellular matrix as visualized by confocal laser scanning microscope and transmission electron microscopy imaging, and presented a much higher level of differentiation (more intense ALP and mineralization stainings and higher levels of osteocalcin secretion) when compared to cells immobilized within unmodified alginate microspheres. These findings demonstrate that peptides covalently coupled to alginate were efficient in influencing cell behavior within this 3D system, and may provide adequate preparation of osteoblasts for cell transplantation. {\textcopyright} 2007 Elsevier Ltd. All rights reserved.},
	keywords = {3T3 Cells, Alginate, Alginates, alginic acid, alkaline phosphatase, animal cell, Animals, arginylglycylaspartic acid, article, Bone, bone cell, Bone Regeneration, calvaria, cell adhesion, cell differentiation, Cell encapsulation, Cell immobilization, cell metabolism, cell proliferation, cell survival, cell ultrastructure, cell viability, confocal laser microscopy, controlled study, cytology, cytoskeleton, DNA, DNA content, ECM (extracellular matrix), enzyme activity, extracellular matrix, Glucuronic Acid, Hexuronic Acids, hydrogel, immobilized cell, metabolism, Mice, Microscopy, Confocal, Microscopy, Electron, Transmission, microsphere, Microspheres, nonhuman, Oligopeptides, osteoblast, Osteoblasts, osteocalcin, Patient treatment, priority journal, rat, RGD peptide, structure analysis, three dimensional imaging, Tissue engineering, transmission electron microscopy, Transplantation (surgical)},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-34249870130\&partnerID=40\&md5=4476a4b1ee80320328c1bf37054037bb},
	author = {Evangelista, M.B. and Hsiong, S.X. and Fernandes, R. and Sampaio, P. and Kong, H.-J. and Barrias, C.C. and Salema, R. and Barbosa, M.A. and Mooney, D.J. and Granja, P.L.}
}
@article {2473,
	title = {Protein electrostatic self-assembly on poly(DL-lactide) scaffold to promote osteoblast growth},
	journal = {Journal of Biomedical Materials Research - Part B Applied BiomaterialsJ. Biomed. Mater. Res. Part B Appl. Biomater.},
	volume = {71},
	year = {2004},
	note = {Cited By (since 1996): 14Export Date: 21 November 2012Source: ScopusCODEN: JBMRGdoi: 10.1002/jbm.b.30080PubMed ID: 15368240Language of Original Document: EnglishCorrespondence Address: Ji, J.; Dept. of Poly. Sci. and Engineering, Zhejiang University, Hangzhou 310027, China; email: jianji@mail.hz.zj.cnChemicals/CAS: DNA, 9007-49-2; gelatin, 9000-70-8; polyethyleneimine, 74913-72-7; polylactide, 26680-10-4; DNA, 9007-49-2; Gelatin, 9000-70-8; poly(lactide), 26969-66-4; PolyestersReferences: Anselme, K., Osteoblast adhesion on biomaterials (2000) Biomaterials, 21, pp. 667-681;Kim, B.S., Mooney, D.J., Development of biocompatible synthetic extracellular matrices for tissue engineering (1998) Trend Biotechnol, 16, pp. 224-230; 
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},
	month = {2004///},
	pages = {159 - 165},
	abstract = {The development of protein coating on 3D biodegradable scaffold based on electrostatic self-assembly (ESA) to promote osteoblast growth is reported. Poly (ethylenimine) (PEI) was employed to obtain a stable positively charged surface on poly(DL-lactide) (PDL-LA) substrate. An extracellular-matrix (ECM)-like biomacromolecule, gelatin, was chosen as the polyelectrolyte to deposit on the activated PDL-LA substrate via ESA technique. Osteoblast (MC3T3) was then cultured on unmodified and gelatin-modified PDL-LA scaffolds. Osteoblast testing regarding total intracellular protein content, total DNA content, cell activity, and cell morphology on the ECM-like multilayer-modified PDL-LA scaffold showed that osteoblast growth was promoted. It will be easy to replace the gelatin with osteoinductive proteins or other polyelectrolytes to promote specific osteoblast functions. In comparison with conventional coating methods, polyelectrolyte multilayers are easy and stable to prepare. They may be a good choice for the surface modification of complex biomedical devices, especially for the 3D tissue-engineering scaffold. These very flexible systems allow broad medical applications for drug delivery and tissue engineering. {\textcopyright} 2004 Wiley Periodicals, Inc.},
	keywords = {3T3 Cells, Absorbable Implants, Activation analysis, animal cell, Animals, article, Biodegradation, Biomedical engineering, cell activity, cell adhesion, Cell Division, cell growth, cell level, cell protein, cell structure, cell surface, Cell-material interactions, Cells, Coating techniques, DNA, DNA content, Drug products, Electrostatics, ethylene derivative, extracellular matrix, gelatin, Gelation, Growth (materials), Kinetics, macromolecule, materials testing, Mice, Microscopy, Confocal, mouse, nonhuman, osteoblast, Osteoblast growth, Osteoblast testing, Osteoblasts, polyelectrolyte, Polyelectrolytes, Polyesters, Polyethyleneimine, polylactide, polymer, protein assembly, Proteins, Surface modification, Tissue, Tissue engineering},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-4644230505\&partnerID=40\&md5=2c6499a5f15b19dfab9731021aa4639b},
	author = {Zhu, H. and Ji, J. and Barbosa, M.A. and Shen, J.}
}
