



@article {2207,
	title = {Methamphetamine mimics the neurochemical profile of aging in rats and impairs recognition memory},
	journal = {NeuroToxicologyNeuroToxicology},
	volume = {33},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusCODEN: NRTXDdoi: 10.1016/j.neuro.2012.03.002PubMed ID: 22433442Language of Original Document: EnglishCorrespondence Address: Melo, P.; Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal; email: pmelo@ibmc.up.ptChemicals/CAS: dopamine, 51-61-6, 62-31-7; methamphetamine, 28297-73-6, 51-57-0, 537-46-2, 7632-10-2; serotonin, 50-67-9; sodium chloride, 7647-14-5; Hydroxyindoleacetic Acid, 54-16-0; Methamphetamine, 537-46-2; Serotonin, 50-67-9References: Ali, S.F., David, S.N., Newport, G.D., Age-related susceptibility to MPTP-induced neurotoxicity in mice (1993) Neurotoxicology, 14, pp. 29-34;Alves, E., Binienda, Z., Carvalho, F., Alves, C.J., Fernandes, E., Bastos, M.D.L., Acetyl-l-carnitine provides effective in vivo neuroprotection over 3,4-methylenedioximethamphetamine-induced mitochondrial neurotoxicity in the adolescent rat brain (2009) Neuroscience, 158, pp. 514-523; 
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},
	month = {2012///},
	pages = {491 - 499},
	abstract = {Brain neurochemistry and cognition performance are thought to decline with age. Accumulating data indicate that similar events occur after prolonged methamphetamine (MA) exposure. Using the rat as a model, the present study was designed to uncover common alteration patterns in brain neurochemistry and memory performance between aging and prolonged MA exposure. To this end, animals were treated with a chronic binge MA administration paradigm (20. mg/kg/day from postnatal day 91 to 100). Three-age control groups received isovolumetric saline treatment and were tested at the MA age-matched period, and at 12 and 20 months. We observed that both MA and aged animals presented a long, but not short, time impairment in novelty preference and an increased anxiety-like behavior. Neurochemical analysis indicated similar MA- and age-related impairments in dopamine, serotonin and metabolites in the striatum, prefrontal cortex and hippocampus. Thus, the present data illustrate that MA may be used to mimic age-related effects on neurotransmitter systems and advocate MA treatment as a feasible animal model to study neuronal processes associated with aging. {\textcopyright} 2012 Elsevier Inc.},
	keywords = {Accelerated aging, Age Factors, aging, animal behavior, animal experiment, animal model, animal tissue, Animalia, Animals, anxiety, article, behavior change, Behavior, Animal, Brain, Brain Chemistry, controlled study, corpus striatum, dopamine, Exploratory Behavior, hippocampus, Hydroxyindoleacetic Acid, long term exposure, male, Memory Disorders, mental performance, Methamphetamine, Neurochemistry, neurotransmission, nonhuman, perinatal drug exposure, prefrontal cortex, priority journal, rat, Rats, Rats, Wistar, Rattus, recognition, Recognition (Psychology), Recognition memory, serotonin, sodium chloride, Time Factors},
	isbn = {0161813X (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84861188767\&partnerID=40\&md5=9c50ef658007fb37150c8b2d6d235d29},
	author = {Melo, P. and Magalh{\~a}es, A. and Alves, C.J. and Tavares, M.A. and De Sousa, L. and Summavielle, T. and Moradas-Ferreira, P.}
}
@article {2359,
	title = {Osteoblast adhesion and morphology on TiO                    2 depends on the competitive preadsorption of albumin and fibronectin
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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; 
Pettit, D.K., Horbett, T.A., Hoffman, A.S., Influence of the substrate binding characteristics of fibronectin on corneal epithelial cell outgrowth (1992) J Biomed Mater Res, 26, pp. 1259-1275; 
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 {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; 
Johnson, K.J., Sage, H., Briscoe, G., Erickson, H.P., (1999) J. Biol. Chem., 274, p. 15473; 
Bergkvist, M., Carlsson, J., Oscarsson, S., (2003) J. Biomed. Mater. Res. Part A., 64 A, p. 349; 
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Sukenik, C.N., Balachander, N., Culp, L.A., Lewandowska, K., Merritt, K., (1990) J. Biomed. Mater. Res., 24, p. 1307; 
Sousa, S.R., Moradas- Ferreira, P., Melo, L.V., Saramago, B., Barbosa, M.A., (2004) Langmuir, 20, p. 9745; 
Gehanno, V., Freitas, P.P., Ferreira, J., Almeida, B., Sousa, J.B., Kling, A., Soares, J.C., Silva, M.F., (1999) IEEE Trans. Magn., 35, p. 4361; 
(2003) Iodine-125, A Guide to Radioiodination Techniques - Amersham Life Science, p. 64. , Amersham International plc, Amersham Place, Little Chalfont, Bucks, HP7 9NA, England, 199; 
Lima, J., Sousa, S.R., Ferreira, A., Barbosa, M.A., (2001) J. Biomed. Mater. Res., 55, p. 45; 
Yu, X.J., Brash, J.L., (1993) Test Procedures for the Blood Compatibility of Biomaterials, Dordrecht, p. 287. , edited by S. Dawids (Kluwer Academic Publishers, Dordrecht); 
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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},
	note = {Cited By (since 1996): 58Export Date: 21 November 2012Source: ScopusCODEN: LANGDdoi: 10.1021/la049158dPubMed ID: 15491210Language of Original Document: EnglishCorrespondence Address: Sousa, S.R.; Inst. de Engenharia Biom{\'e}dica, Laborat{\'o}rio Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: ssousa@ibmc.up.ptChemicals/CAS: serum albumin, 9048-46-8; titanium dioxide, 1317-70-0, 1317-80-2, 13463-67-7, 51745-87-0; titanium, 7440-32-6; Serum Albumin; Solutions; titanium dioxide, 13463-67-7; Titanium, 7440-32-6References: Nakabayashi, N., Iwasaki, Y., (2000) European White Book on Fundamental Research in Materials Science, pp. pp70-71. , R{\"u}hle, M., Dosch, H., Mittemeijer, E. J.Van de Voorde, M. H., Eds.; Max Plank Institut fur Metallforschung: Stuttgart, Germany;Windler, M., Klabunde, R., (2001) Titanium in Medicine; Material Science, Surface Science, Engineering, Biological Responses and Medical Applications, pp. 703-746. , Brunette, D. M., Tengvall, P., Textor, M., Thomsen, P., Eds.; Springer-Verlag: Berlin, Germany; 
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},
	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.}
}
