



@article {3270,
	title = {Macrophages stimulate gastric and colorectal cancer invasion through EGFR Y 1086, c-Src, Erk1/2 and Akt phosphorylation and smallGTPase activity},
	journal = {Oncogene},
	volume = {33},
	year = {2014},
	note = {Cited By (since 1996):2Export Date: 21 November 2014},
	month = {2014},
	pages = {2123 - 2133},
	abstract = {The interactions between cancer cells and their microenvironment are crucial for malignant progression, as they modulate invasion-related activities. Tumor-associated macrophages are generally considered allies in the process of tumor progression in several types of cancer, although their role on gastric and colorectal carcinomas is still poorly understood. In this report, we studied the influence of primary human macrophages on gastric and colorectal cancer cells, considering invasion, motility/migration, proteolysis and activated intracellular signaling pathways. We demonstrated that macrophages stimulate cancer cell invasion, motility and migration, and that these effects depend on matrix metalloproteinase (MMP) activity and on the activation of epidermal growth factor receptor (EGFR) (at the residue Y 1086), PLC-γ (phospholipase C-gamma) and Gab1 (GRB2-associated binding protein-1), as evidenced by siRNA (small interference RNA) experiments. Epidermal growth factor (EGF)-immunodepletion impaired macrophage-mediated cancer cell invasion and motility, suggesting that EGF is the pro-invasive and pro-motile factor produced by macrophages. Macrophages also induced gastric and colorectal cancer cell phosphorylation of Akt, c-Src and ERK1/2, and led to an increase of RhoA and Cdc42 activity. Interestingly, whereas macrophage-mediated cancer cell c-Src and ERK1/2 phosphorylation occurred downstream EGFR activation, Akt phosphorylation seems to be a parallel event, taking place in an EGFR-independent manner. The involvement of EGF, EGFR-downstream signaling partners and MMPs in macrophage-mediated invasion provides novel insights into the molecular crosstalk established between cancer cells and macrophages, opening new perspectives for the design of new and more efficient therapeutic strategies to counteract cancer cell invasion. {\textcopyright} 2014 Macmillan Publishers Limited.},
	keywords = {cancer cell invasion, colon cancer, Gastric cancer, invasion-related signaling pathways, Macrophages, tumor microenvironment},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84899425243\&partnerID=40\&md5=beff5192ff42940c75fef8b48ebd3ae7},
	author = {Cardoso, A.P. and Pinto, M.L. and Pinto, A.T. and Oliveira, M.I. and Pinto, M.T. and Gon{\c c}alves, R. and Relvas, J.B. and Figueiredo, C. and Seruca, R. and Mantovani, A. and Mareel, M. and Barbosa, M.A. and Oliveira, M.J.}
}
@article {3291,
	title = {Neonatal human dermal fibroblasts immobilized in RGD-alginate induce angiogenesis},
	journal = {Cell Transplantation},
	volume = {23},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {945 - 957},
	abstract = {Promoting angiogenesis in a damaged tissue is a major challenge for tissue regeneration. Recent findings in tissue engineering suggest that fibroblasts (FBs) play an important role in orchestrating the angiogenic process. Fibroblasts maintain the structural integrity of connective tissue by continuously secreting growth factors and extracellular matrix precursors, which are essential for endothelial cell (EC) adhesion and spreading, thus playing a crucial role in angiogenesis. We hypothesized that FBs immobilized in alginate gels grafted with the RGD peptidic sequence could influence the recruitment of ECs to improve vascularization. In this work, the modulation of immobilized human FBs within the 3D synthetic extracellular matrix was assessed. Experiments using cocultures of ECs and FBs in indirect contact as well as angiogenic assays were performed to assess the influence of FBs immobilized in RGD-alginate in ECs{\textquoteright} viability, stabilization, sprouting, and assembly into capillary-like structures. This study demonstrates the ability of FBs immobilized within RGD-alginate microspheres to modulate and support capillary-like structures{\textquoteright} assembly. These findings indicate that the microenvironment created by these stromal cells in the scaffold modulates capillary morphogenesis, thus stimulating angiogenesis in situ and can potentially be used in regenerative medicine in clinical scenarios where vascularization is essential. {\textcopyright} 2014 Cognizant Comm. Corp.},
	keywords = {Alginate, angiogenesis, Endothelial cells (ECs), Fibroblasts (FBs), RGD peptide: Injectable biomaterials},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84905231059\&partnerID=40\&md5=8ca92aea469585cbf168cb6fbad9d3ad},
	author = {Guerreiro, S.G. and Oliveira, M.J. and Barbosa, M.A. and Soares, R. and Granja, P.L.}
}
@article {3293,
	title = {The predominance of M2-polarized macrophages in the stroma of low-hypoxic bladder tumors is associated with BCG immunotherapy failure},
	journal = {Urologic Oncology: Seminars and Original Investigations},
	volume = {32},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {449 - 457},
	abstract = {Objective: Bacillus Calmette-Gu{\'e}rin (BCG) immunotherapy is the gold standard treatment for superficial bladder tumors with intermediate/high risk of recurrence or progression. However, approximately 30\% of patients fail to respond to the treatment. Effective BCG therapy needs precise activation of the type 1 helper cells immune pathway. Tumor-associated macrophages (TAMs) often assume an immunoregulatory M2 phenotype and may directly interfere with the BCG-induced antitumor immune response. Thus, we aim to clarify the influence of TAMs, in particular of the M2 phenotype in stroma and tumor areas, in BCG treatment outcome. Patients and methods: The study included 99 patients with bladder cancer treated with BCG. Tumors resected before treatment were evaluated using immunohistochemistry for CD68 and CD163 antigens, which identify a lineage macrophage marker and a M2-polarized specific cell surface receptor, respectively. CD68+ and CD163+ macrophages were evaluated within the stroma and tumor areas, and high density of infiltrating cells spots were selected for counting. Hypoxia, an event known to modulate macrophage phenotype, was also assessed through hypoxia induced factor (HIF)-1α expression. Results: Patients in whom BCG failed had high stroma-predominant CD163+ macrophage counts (high stroma but low tumor CD163+ macrophages counts) when compared with the ones with a successful treatment (71\% vs. 47\%, P = 0.017). Furthermore, patients presenting this phenotype showed decreased recurrence-free survival (log rank, P = 0.008) and a clear 2-fold increased risk of BCG treatment failure was observed in univariate analysis (hazard ratio = 2.343; 95\% CI: 1.197-4.587; P = 0.013). Even when adjusted for potential confounders, such as age and therapeutic scheme, multivariate analysis revealed 2.6-fold increased risk of recurrence (hazard ratio = 2.627; 95\% CI: 1.340-5.150; P = 0.005). High stroma-predominant CD163+ macrophage counts were also associated with low expression of HIF-1α in tumor areas, whereas high counts of CD163+ in the tumor presented high expression of HIF-1α in tumor nests. Conclusions: TAMs evaluation using CD163 is a good indicator of BCG treatment failure. Moreover, elevated infiltration of CD163+ macrophages, predominantly in stroma areas but not in the tumor, may be a useful indicator of BCG treatment outcome, possibly owing to its immunosuppressive phenotype. {\textcopyright} 2014 Elsevier Inc.},
	keywords = {BCG immunotherapy, Bladder cancer, CD163, CD68, Tumor-associated macrophages},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84899473274\&partnerID=40\&md5=4716f90a43e05e83d41df6d643097edd},
	author = {Lima, L. and Oliveira, D. and Tavares, A. and Amaro, T. and Cruz, R. and Oliveira, M.J. and Ferreira, J.A. and Santos, L.}
}
@article {2888,
	title = {Characterization of human NLZ1/ZNF703 identifies conserved domains essential for proper subcellular localization and transcriptional repression},
	journal = {Journal of Cellular Biochemistry},
	volume = {114},
	year = {2013},
	note = {Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {120 - 133},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84869412286\&partnerID=40\&md5=e48a26e94d7ce0eddb65d8067fdc056c},
	author = {Pereira-Castro, I. and Costa, {\^A}.M.S. and Oliveira, M.J. and Barbosa, I. and Rocha, A.S. and Azevedo, L. and Da Costa, L.T.}
}
@article {2859,
	title = {Expression of ST3GAL4 Leads to SLex Expression and Induces c-Met Activation and an Invasive Phenotype in Gastric Carcinoma Cells},
	journal = {PLoS ONE},
	volume = {8},
	year = {2013},
	note = {Cited By (since 1996):1Export Date: 12 December 2013Source: ScopusArt. No.: e66737},
	month = {2013///},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84879165131\&partnerID=40\&md5=58617c0600b708de7a68556b87336112},
	author = {Gomes, C. and Os{\'o}rio, H. and Pinto, M.T. and Campos, D. and Oliveira, M.J. and Reis, C.A.}
}
@article {2889,
	title = {Loss of WNK2 expression by promoter gene methylation occurs in adult gliomas and triggers Rac1-mediated tumour cell invasiveness},
	journal = {Human Molecular Genetics},
	volume = {22},
	year = {2013},
	note = {Cited By (since 1996):2Export Date: 12 December 2013Source: ScopusArt. No.: dds405},
	month = {2013///},
	pages = {84 - 95},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84871200220\&partnerID=40\&md5=b2bfd70fb2a8a4e517e4ad698a2461cc},
	author = {Moniz, S. and Martinho, O. and Pinto, F. and Sousa, B. and Loureiro, C. and Oliveira, M.J. and Moita, L.F. and Honavar, M. and Pinheiro, C. and Pires, M. and Lopes, J.M. and Jones, C. and Costello, J.F. and Paredes, J. and Reis, R.M. and Jordan, P.}
}
@booklet {2867,
	title = {Macrophages stimulate gastric and colorectal cancer invasion through EGFR Y1086, c-Src, Erk1/2 and Akt phosphorylation and smallGTPase activity},
	howpublished = {Oncogene},
	year = {2013},
	note = {Cited By (since 1996):1Export Date: 12 December 2013Source: ScopusArticle in Press},
	month = {2013///},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84876908646\&partnerID=40\&md5=bcc2929bb93817db3dc0e3421c420722},
	author = {Cardoso, A.P. and Pinto, M.L. and Pinto, A.T. and Oliveira, M.I. and Pinto, M.T. and Gon{\c c}alves, R. and Relvas, J.B. and Figueiredo, C. and Seruca, R. and Mantovani, A. and Mareel, M. and Barbosa, M.A. and Oliveira, M.J.}
}
@article {2865,
	title = {Overexpression of tumour-associated carbohydrate antigen sialyl-Tn in advanced bladder tumours},
	journal = {Molecular Oncology},
	volume = {7},
	year = {2013},
	note = {Cited By (since 1996):1Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {719 - 731},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84878107131\&partnerID=40\&md5=52c1f1e8bc83224d947840df0f3dd539},
	author = {Ferreira, J.A. and Videira, P.A. and Lima, L. and Pereira, S. and Silva, M. and Carrascal, M. and Severino, P.F. and Fernandes, E. and Almeida, A. and Costa, C. and Vitorino, R. and Amaro, T. and Oliveira, M.J. and Reis, C.A. and Dall{\textquoteright}Olio, F. and Amado, F. and Santos, L.L.}
}
@article {2180,
	title = {Chitosan drives anti-inflammatory macrophage polarisation and pro-inflammatory dendritic cell stimulation.},
	journal = {European cells \& materialsEur Cell Mater},
	volume = {24},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusPubMed ID: 22828991Language of Original Document: EnglishCorrespondence Address: Oliveira, M.I.Chemicals/CAS: chitosan, 9012-76-4; Antigens, CD86; Biocompatible Materials; Chitosan, 9012-76-4; Histocompatibility Antigens Class II; IL10 protein, human; Interleukin-10, 130068-27-8; Transforming Growth Factor beta1; Tumor Necrosis Factor-alpha},
	month = {2012///},
	pages = {136 - 152; discussion 152-153},
	abstract = {Macrophages and dendritic cells (DC) share the same precursor and play key roles in immunity. Modulation of their behaviour to achieve an optimal host response towards an implanted device is still a challenge. Here we compare the differentiation process and polarisation of these related cell populations and show that they exhibit different responses to chitosan (Ch), with human monocyte-derived macrophages polarising towards an anti-inflammatory phenotype while their DC counterparts display pro-inflammatory features. Macrophages and DC, whose interactions with biomaterials are frequently analysed using fully differentiated cells, were cultured directly on Ch films, rather than exposed to the polymer after complete differentiation. Ch was the sole stimulating factor and activated both macrophages and DC, without leading to significant T cell proliferation. After 10 d on Ch, macrophages significantly down-regulated expression of pro-inflammatory markers, CD86 and MHCII. Production of pro-inflammatory cytokines, particularly TNF-α, decreased with time for cells cultured on Ch, while anti-inflammatory IL-10 and TGF-β1, significantly increased. Altogether, these results suggest an M2c polarisation. Also, macrophage matrix metalloproteinase activity was augmented and cell motility was stimulated by Ch. Conversely, DC significantly enhanced CD86 expression, reduced IL-10 secretion and increased TNF-α and IL-1β levels. Our findings indicate that cells with a common precursor may display different responses, when challenged by the same biomaterial. Moreover, they help to further comprehend macrophage/DC interactions with Ch and the balance between pro- and anti-inflammatory signals associated with implant biomaterials. We propose that an overall pro-inflammatory reaction may hide the expression of anti-inflammatory cytokines, likely relevant for tissue repair/regeneration.},
	keywords = {antibody specificity, Antigens, CD86, article, Biocompatible Materials, biomaterial, biosynthesis, CD86 antigen, Cell culture, cell differentiation, cell motion, Cell Movement, Cells, Cultured, chitosan, cytology, dendritic cell, Dendritic Cells, drug effect, flow cytometry, Histocompatibility Antigens Class II, HLA antigen class 2, human, Humans, IL10 protein, human, immunology, interleukin 10, Interleukin-10, macrophage, Macrophages, metabolism, monocyte, Monocytes, Organ Specificity, transforming growth factor beta1, tumor necrosis factor alpha, Tumor Necrosis Factor-alpha},
	isbn = {14732262 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84868253478\&partnerID=40\&md5=5a496411709ccbe5d3d70de13b58b08a},
	author = {Oliveira, M.I. and Santos, S.G. and Oliveira, M.J. and Torres, A.L. and Barbosa, M.A.}
}
@article {2189,
	title = {E-cadherin dysfunction in gastric cancer - Cellular consequences, clinical applications and open questions},
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	year = {2012},
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},
	month = {2012///},
	pages = {2981 - 2989},
	abstract = {E-cadherin plays a major role in cell-cell adhesion and inactivating germline mutations in its encoding gene predispose to hereditary diffuse gastric cancer. Evidence indicates that aside from its recognized role in early tumourigenesis, E-cadherin is also pivotal for tumour progression, including invasion and metastization. Herein, we discuss E-cadherin alterations found in a cancer context, associated cellular effects and signalling pathways, and we raise new key questions that will impact in the management of GC patients and families. {\textcopyright} 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.},
	keywords = {Adhesion, Cadherins, cancer growth, cancer invasion, cancer patient, cancer susceptibility, cell adhesion, complex formation, conference paper, E-cadherin, embryo development, endocytosis, epigenetics, epithelial mesenchymal transition, Gastric cancer, gene mutation, gene silencing, genetic susceptibility, Germ-Line Mutation, HDGC, Helicobacter infection, Helicobacter Infections, Helicobacter pylori, histone deacetylase inhibitor, human, Humans, Invasion, metastasis, molecular pathology, nonhuman, priority journal, protein analysis, protein depletion, protein expression, protein function, protein structure, regulatory mechanism, signal transduction, Signalling, stomach cancer, stomach carcinogenesis, Stomach Neoplasms, Tumour, uvomorulin},
	isbn = {00145793 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84864922992\&partnerID=40\&md5=455ae054dc6c8f95dc9e81d77fec1ad9},
	author = {Carneiro, P. and Fernandes, M.S. and Figueiredo, J. and Caldeira, J. and Carvalho, J. and Pinheiro, H. and Leite, M. and Melo, S. and Oliveira, P. and Sim{\~o}es-Correia, J. and Oliveira, M.J. and Carneiro, F. and Figueiredo, C. and Paredes, J. and Oliveira, C. and Seruca, R.}
}
@article {2177,
	title = {Epithelial E- and P-cadherins: Role and clinical significance in cancer},
	journal = {Biochimica et Biophysica Acta - Reviews on CancerBiochim. Biophys. Acta Rev. Cancer},
	volume = {1826},
	year = {2012},
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},
	month = {2012///},
	pages = {297 - 311},
	abstract = {E-cadherin and P-cadherin are major contributors to cell-cell adhesion in epithelial tissues, playing pivotal roles in important morphogenetic and differentiation processes during development, and in maintaining integrity and homeostasis in adult tissues. It is now generally accepted that alterations in these two molecules are observed during tumour progression of most carcinomas. Genetic or epigenetic alterations in E- and P-cadherin-encoding genes (CDH1 and CDH3, respectively), or alterations in their proteins expression, often result in tissue disorder, cellular de-differentiation, increased invasiveness of tumour cells and ultimately in metastasis. In this review, we will discuss the major properties of E- and P-cadherin molecules, its regulation in normal tissue, and their alterations and role in cancer, with a specific focus on gastric and breast cancer models. {\textcopyright} 2012 Elsevier B.V.},
	keywords = {antineoplastic activity, antineoplastic agent, Breast, breast cancer, Cancer, cancer chemotherapy, cancer model, cancer survival, drug effect, E-cadherin, Gastric, gene expression regulation, gene function, gene location, gene overexpression, gene structure, genetic association, genetic code, Helicobacter infection, Hereditary diffuse gastric cancer, human, in vivo study, loss of function mutation, lymph node metastasis, malignant neoplastic disease, molecular dynamics, molecular pathology, molecularly targeted therapy, nonhuman, P cadherin, P cadherin gene, P-cadherin, pf 03732010, priority journal, protein expression, protein function, protein inhibitor, protein processing, review, signal transduction, stomach cancer, transcription regulation, tumor gene, unclassified drug, uvomorulin, uvomorulin gene, vasculotropin inhibitor},
	isbn = {0304419X (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84861800037\&partnerID=40\&md5=2d52be63f4168a561b1bda1315e1f429},
	author = {Paredes, J. and Figueiredo, J. and Albergaria, A. and Oliveira, P. and Carvalho, J. and Ribeiro, A.S. and Caldeira, J. and Costa, A.M. and Sim{\~o}es-Correia, J. and Oliveira, M.J. and Pinheiro, H. and Pinho, S.S. and Mateus, R. and Reis, C.A. and Leite, M. and Fernandes, M.S. and Schmitt, F. and Carneiro, F. and Figueiredo, C. and Oliveira, C. and Seruca, R.}
}
@article {2210,
	title = {Tumor cell-educated periprostatic adipose tissue acquires an aggressive cancer-promoting secretory profile},
	journal = {Cellular Physiology and BiochemistryCell. Physiol. Biochem.},
	volume = {29},
	year = {2012},
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},
	month = {2012///},
	pages = {233 - 240},
	abstract = {Background/Aims: The microenvironment produces important factors that are crucial to prostate cancer (PCa) progression. However, the extent to which the cancer cells stimulate periprostatic adipose tissue (PPAT) to produce these proteins is largely unknown. Our purpose was to determine whether PCa cell-derived factors influence PPAT metabolic activity. Methods: Primary cultures of human PPAT samples from PCa patients (adipose tissue organotypic explants and primary stromal vascular fraction, SVF) were stimulated with conditioned medium (CM) collected from prostate carcinoma (PC3) cells. Cultures without CM were used as control. We used multiplex analysis and ELISA for protein quantification, qPCR to determine mitochondrial DNA (mtDNA) copy number and zymography for matrix metalloproteinase activity, in order to evaluate the response of adipose tissue explants and SVFs to PC3 CM. Results: Stimulation of PPAT explants with PCa PC3 CM induced adipokines associated with cancer progression (osteopontin, tumoral necrosis factor alpha and interleukin-6) and reduced the expression of the protective adipokine adiponectin. Notably, osteopontin protein expression was 13-fold upregulated. Matrix metalloproteinase 9 activity and mitochondrial DNA copy number were higher after stimulation with cancer CM. Stromovascular cells from PPAT in culture were not influenced by tumor-derived factors. Conclusion: The modulation of adipokine expression by tumor CM indicates the pervasive extent to which tumor cells command PPAT to produce factors favorable to their aggressiveness. {\textcopyright} 2012 S. Karger AG, Basel.},
	keywords = {Adipokines, adiponectin, adipose tissue, adult, article, cancer cell, cancer growth, Cells, Cultured, clinical article, controlled study, Culture Media, Conditioned, culture medium, Cytokines, DNA, Mitochondrial, enzyme activity, enzyme linked immunosorbent assay, explant, gelatinase B, human, human cell, human tissue, Humans, interleukin 6, Interleukin-6, male, Matrix Metalloproteinase 2, Matrix Metalloproteinase 9, Middle Aged, mitochondrial DNA, Osteopontin, Periprostatic adipose tissue, priority journal, Prostate cancer, Prostatic Neoplasms, protein expression, protein induction, protein secretion, quantitative analysis, stroma cell, tissue metabolism, tumor necrosis factor alpha, Tumor Necrosis Factor-alpha},
	isbn = {10158987 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84859829669\&partnerID=40\&md5=a76be7e5c0037e77140c1fc9aca48a5a},
	author = {Ribeiro, R.J.T. and Monteiro, C.P.D. and Cunha, V.F.P.M. and Azevedo, A.S.M. and Oliveira, M.J. and Monteiro, R. and Fraga, A.M. and Pr{\'\i}ncipe, P. and Lobato, C. and Lobo, F. and Morais, A. and Silva, V. and Sanches-Magalh{\~a}es, J. and Oliveira, J. and Guimar{\~a}es, J.T. and Lopes, C.M.S. and Medeiros, R.M.}
}
@article {2235,
	title = {Molecularly designed alginate hydrogels susceptible to local proteolysis as three-dimensional cellular microenvironments},
	journal = {Acta BiomaterialiaActa Biomater.},
	volume = {7},
	year = {2011},
	note = {Cited By (since 1996): 9Export Date: 21 November 2012Source: Scopusdoi: 10.1016/j.actbio.2010.12.029PubMed ID: 21193068Language of Original Document: EnglishCorrespondence Address: Barrias, C. C.; 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: ccbarrias@ineb.up.ptChemicals/CAS: alginic acid, 28961-37-7, 29894-36-8, 9005-32-7, 9005-38-3; gelatin, 9000-70-8; gelatinase A, 146480-35-5; Alginates; Glucuronic Acid, 576-37-4; Hexuronic Acids; Hydrogels; Matrix Metalloproteinases, 3.4.24.-; Peptides; alginic acid, 9005-32-7References: Lukashev, M.E., Werb, Z., ECM signalling: Orchestrating cell behaviour and misbehaviour (1998) Trends in Cell Biology, 8 (11), pp. 437-441. , DOI 10.1016/S0962-8924(98)01362-2, PII S0962892498013622;Bosman, F.T., Stamenkovic, I., Functional structure and composition of the extracellular matrix (2003) Journal of Pathology, 200 (4), pp. 423-428. , DOI 10.1002/path.1437; 
Lutolf, M.P., Hubbell, J.A., Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering (2005) Nature Biotechnology, 23 (1), pp. 47-55. , DOI 10.1038/nbt1055; 
Lutolf, M.P., Gilbert, P.M., Blau, H.M., Designing materials to direct stem-cell fate (2009) Nature, 462 (7272), pp. 433-441; 
Tibbitt, M.W., Anseth, K.S., Hydrogels as extracellular matrix mimics for 3D cell culture (2009) Biotechnol Bioeng, 103 (4), pp. 655-663; 
Augst, A.D., Kong, H.J., Mooney, D.J., Alginate hydrogels as biomaterials (2006) Macromolecular Bioscience, 6 (8), pp. 623-633. , DOI 10.1002/mabi.200600069; 
Evangelista, M.B., Hsiong, S.X., Fernandes, R., Sampaio, P., Kong, H.-J., Barrias, C.C., Salema, R., Granja, P.L., Upregulation of bone cell differentiation through immobilization within a synthetic extracellular matrix (2007) Biomaterials, 28 (25), pp. 3644-3655. , DOI 10.1016/j.biomaterials.2007.04.028, PII S014296120700347X; 
Grellier, M., Granja, P.L., Fricain, J.C., Bidarra, S.J., Renard, M., Bareille, R., The effect of the co-immobilization of human osteoprogenitors and endothelial cells within alginate microspheres on mineralization in a bone defect (2009) Biomaterials, 30 (19), pp. 3271-3278; 
Bidarra, S.J., Barrias, C.C., Barbosa, M.A., Soares, R., Granja, P.L., Immobilization of human mesenchymal stem cells within RGD-grafted alginate microspheres and assessment of their angiogenic potential (2010) Biomacromolecules, 11 (8), pp. 1956-1964; 
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Chau, Y., Tan, F.E., Langer, R., Synthesis and characterization of dextran-peptide-methotrexate conjugates for tumor targeting via mediation by matrix metalloproteinase II and matrix metalloproteinase IX (2004) Bioconjugate Chemistry, 15 (4), pp. 931-941. , DOI 10.1021/bc0499174; 
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Oliveira, S.M., Barrias, C.C., Almeida, I.F., Costa, P.C., Pena Ferreira, M.R., Bahia, M.F., Injectability of a bone filler system based on hydroxyapatite microspheres and a vehicle with in situ gel-forming ability (2008) J Biomed Mater Res B Appl Biomater, 87 (1), pp. 49-58; 
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Lee, K.Y., Rowley, J.A., Eiselt, P., Moy, E.M., Bouhadir, K.H., Mooney, D.J., Controlling mechanical and swelling properties of alginate hydrogels independently by cross-linker type and cross-linking density (2000) Macromolecules, 33 (11), pp. 4291-4294; 
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Ries, C., Egea, V., Karow, M., Kolb, H., Jochum, M., Neth, P., MMP-2, MT1-MMP, and TIMP-2 are essential for the invasive capacity of human mesenchymal stem cells: Differential regulation by inflammatory cytokines (2007) Blood, 109 (9), pp. 4055-4063. , http://bloodjournal.hematologylibrary.org/cgi/reprint/109/9/4055, DOI 10.1182/blood-2006-10-051060; 
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Barbolina, M.V., Adley, B.P., Ariztia, E.V., Liu, Y., Stack, M.S., Microenvironmental regulation of membrane type 1 matrix metalloproteinase activity in ovarian carcinoma cells via collagen-induced EGR1 expression (2007) Journal of Biological Chemistry, 282 (7), pp. 4924-4931. , http://www.jbc.org/cgi/reprint/282/7/4924, DOI 10.1074/jbc.M608428200
},
	month = {2011///},
	pages = {1674 - 1682},
	abstract = {The development of sophisticated three-dimensional (3-D) cell culture microenvironments that recreate some of the complexity of the natural extracellular matrix (ECM) remains a challenging task. Here, the modification of alginate through partial crosslinking with a matrix metalloproteinase (MMP) cleavable peptide (proline-valine-glycine-leucine-isoleucine-glycine, PVGLIG) is described, and its use in the preparation of injectable, in situ crosslinkable hydrogel-like matrices is proposed. PVGLIG-grafted alginates were synthesized by carbodiimide chemistry and characterized. Their biological performance was evaluated by comparing the response of 3-D cultured mesenchymal stem cells (MSCs) to alginate hydrogels containing only cell-adhesion peptides (RGD-alginate) or both peptides (PVGLIG/RGD-alginate). After 1 week, cells remained essentially round within RGD-alginate, while they exhibited an elongated morphology within PVGLIG/RGD-alginate hydrogels, forming cellular networks. This suggests that cells were able to structurally reorganize the matrix, through enzymatic hydrolysis of PVGLIG residues, overcoming biophysical hydrogel resistance. As shown by gelatine-zymography, MSC presented higher activity of MMP-2 when cultured within alginate functionalized with MMP-sensitive peptide, suggesting that the cell{\textquoteright}s proteolytic phenotype was modulated by the matrix composition. Additionally, PVGLIG/RGD-alginate hydrogels were clearly degraded in cell culture. Taken together, the results demonstrate that the co-incorporation of MMP-labile peptides in cell-adhesive RGD-alginate hydrogels improved their performance as ECM analogues, providing a more dynamic and physiological 3-D cellular microenvironment. {\textcopyright} 2010 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.},
	keywords = {3-D Cell culture, Alginate, Alginates, alginic acid, Amino Acid Sequence, article, cell adhesion, cell composition, Cell Count, Cell culture, Cell Culture Techniques, Cell Shape, cell structure, cell survival, cell viability, Cells, Cultured, controlled study, Enzyme Activation, enzyme activity, extracellular matrix, Extracellular matrix (ECM), gelatin, gelatinase A, Glucuronic Acid, Hexuronic Acids, human, human cell, Humans, hydrogel, Hydrogels, hydrolysis, matrix metalloproteinase, Matrix Metalloproteinases, Matrix metalloproteinases (MMPs), Mesenchymal stem cell, Mesenchymal Stem Cells, Molecular Sequence Data, morphology, peptide derivative, Peptides, phenotype, priority journal, prolylvalylglycylleucylisoleucylglycine, Protease-sensitive, protein cleavage, protein degradation, Protein Processing, Post-Translational, Subcellular Fractions, tumor microenvironment, unclassified drug, zymography},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-79952189303\&partnerID=40\&md5=191596b948bd4cc2569264a992052b88},
	author = {Fonseca, K.B. and Bidarra, S.J. and Oliveira, M.J. and Granja, P.L. and Barrias, C.C.}
}
@article {2268,
	title = {Bioactivity of immobilized EGF on self-assembled monolayers: Optimization of the immobilization process},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {94},
	year = {2010},
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},
	month = {2010///},
	pages = {576 - 585},
	abstract = {Last trends in Biomaterials focus the mimic of cellular environments capable to control cellular responses. Epidermal growth factor (EGF) is a pleiotropic cytokine known to regulate cell proliferation, differentiation, and death. This study aims to optimize the immobilization of EGF on 11-mercapto-1-undecyl-tetra(ethylene)glycol (EG4) - self-assembled monolayers (SAMs) and to establish a new model surface to study EGF-mediated signaling. Gold substrates were modified with a monolayer of EG4 and N,N'- carbonyldiimidazole (CDI) was used to activate hydroxyl terminated groups of EG4-SAMs. EGF was then immobilized on activated EG4-SAMs at pH 7.4, 4{\textdegree}C, and 100 rpm. Different immobilization reaction times were tested as well as different CDI concentrations to optimize the reaction conditions and obtain a range of immobilized EGF concentrations on the surfaces. Surface characterization of EGF-SAMs was performed using radiolabeling, water contact angle measurements, X-ray photoelectron spectroscopy, and ELISA. Phosphorylation of EGFR on BT-20 breast cancer cell line by EGF-SAMs was tested by immunostaining. EGF was successfully immobilized on EG4-SAMs, at 4{\textdegree}C and pH 7.4 in a range of concentrations from 3.6 {\textpm} 0.8 to 17.6 {\textpm} 1.5 ng/cm                        2. The concentration of EGF increases with immobilization time and with the CDI concentration reaching the maximum for surfaces activated with 30 mg/mL of CDI after 48 h. The bioactivity of EGF-SAMs was confirmed by immunostaining of phospho-EGFR of BT-20 cells. This study described EGF immobilization on EG4-SAMs at different concentrations, which could be important surface models to study specific protein interactions at the molecular level evolving EGF-family of proteins. {\textcopyright} 2010 Wiley Periodicals, Inc. J.
},
	keywords = {Adsorption, Angle measurement, article, Biocompatible Materials, Biological materials, Breast cancer cells, cancer cell culture, Carbonyldiimidazole, Cell culture, Cell immobilization, Cell Line, Tumor, cell proliferation, Cellular environment, Cellular response, Concentration (process), Concentration of, Contact angle, controlled study, Cytokines, EGF, Electron energy levels, enzyme linked immunosorbent assay, Enzyme-Linked Immunosorbent Assay, epidermal growth factor, Epidermal growth factors, Ethylene, Glycols, gold, Gold substrates, human, human cell, Humans, Hydroxyl-terminated, Imidazoles, Immobilization process, Immobilization reaction, immunofluorescence, immunohistochemistry, Immunostaining, Molecular levels, Nanostructured materials, Nanostructured surface, Nanostructured surfaces, New model, Optimization, Phosphorylation, Photoelectron spectroscopy, Polyethylene Glycols, Protein adsorption, protein immobilization, protein interaction, protein phosphorylation, Proteins, Radiolabeling, Radioligand Assay, Reaction conditions, reaction optimization, Receptor, Epidermal Growth Factor, Sams, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, Sulfhydryl Compounds, Surface characterization, Surface functionalization, Surface models, Surface Properties, Water contact angle measurement, X ray photoelectron spectroscopy},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77953815323\&partnerID=40\&md5=7b54d717bbba475933dd86cc62659acc},
	author = {Gon{\c c}alves, R. and Martins, M.C.L. and Oliveira, M.J. and Almeida-Porada, G. and Barbosa, M.A.}
}
@article {2307,
	title = {Cancer invasion and metastasis: Interacting ecosystems},
	journal = {Virchows ArchivVirchows Arch.},
	volume = {454},
	year = {2009},
	note = {Cited By (since 1996): 20Export Date: 21 November 2012Source: ScopusCODEN: VARCEdoi: 10.1007/s00428-009-0784-0PubMed ID: 19471961Language of Original Document: EnglishCorrespondence Address: Madani, I.; Department of Radiotherapy, Ghent University Hospital, De Pintelaan 185, 9000 Ghent, Belgium; email: indira.madani@ugent.beReferences: Tarin, D., New insights into the pathogenesis of breast cancer metastasis (2006) Breast Disease, 26 (1), pp. 13-25;Stafford, L.J., Vaidya, K.S., Welch, D.R., Metastasis suppressors genes in cancer (2008) Int J Biochem Cell Biol, 40, pp. 874-891; 
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},
	month = {2009///},
	pages = {599 - 622},
	abstract = {Malignant tumors invade and metastasize. They consist of cancer cells, evolving through genetic and epigenetic modulation, mixed with tumor-associated host cells, emerging from resident or bone marrow-derived precursors. These cells establish ecosystems to activate cellular programs for local invasion and distant metastasis. Characteristic of such malignancy-related activities is communication inside ecosystems between cells, ligands, receptor protein complexes, and signaling pathways as well as between ecosystems comprising the primary tumor, lymph node and distant metastasis, bone marrow and blood and lymph circulation. Complexity is another characteristic, resulting from: heterogeneity of the cell populations; the numbers of promoter and suppressor genes, their levels of regulation, and the pleiotropic activities of their products; biological redundancy of the molecular mechanisms underpinning invasion-related activities. Clinical attention is paid to putative new targets, namely host cells, individual molecules and their signaling pathways, as well as the effects of current treatment on invasion and metastasis. {\textcopyright} 2009 Springer-Verlag.},
	keywords = {bone marrow, cancer cell, cancer invasion, carcinogenesis, cell activity, Circulation, ecosystem, epigenetics, extracellular matrix, gene control, host cell, human, Humans, lymph node metastasis, metastasis, Metastatic site, microarray analysis, Molecular biology, molecular imaging, Neoplasm Invasiveness, Neoplasm Metastasis, Neoplasms, nonhuman, pleiotropy, primary tumor, priority journal, Promoter and suppressor genes, promoter region, review, signal transduction, suppressor gene, Therapy guidance, Tumor-associated host cells},
	isbn = {09456317 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-67649116432\&partnerID=40\&md5=4c02a29f53858424b4c3191dcd86256c},
	author = {Mareel, M. and Oliveira, M.J. and Madani, I.}
}
