



@article {3278,
	title = {Dysregulation of T cell receptor N-glycosylation: A molecular mechanism involved in ulcerative colitis},
	journal = {Human Molecular Genetics},
	volume = {23},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {2416 - 2427},
	abstract = {The incidence of inflammatory bowel disease is increasing worldwide and the underlying molecular mechanisms are far from being fully elucidated. Herein, we evaluated the role of N-glycosylation dysregulation in T cells as a key mechanism in the ulcerative colitis (UC) pathogenesis. The evaluation of the branched N-glycosylation levelsandprofile of intestinalTcell receptor (TCR)wereassessedin colonic biopsies fromUCpatientsand healthy controls. Expression alterations of the glycosyltransferase gene MGAT5 were also evaluated. We demonstrated thatUCpatients exhibit a dysregulation ofTCRbranchedN-glycosylationonlamina propriaTlymphocytes. Patients with severe UC showed the most pronounced defect on N-glycan branching in T cells. Moreover, UC patients showed a significant reduction of MGAT5 gene transcription in T lymphocytes. In this study, we disclose for the first time that a deficiency in branched N-glycosylation on TCR due to a reduced MGAT5 gene expression is a new molecular mechanism underlying UC pathogenesis, being a potential novel biomarker with promising clinical and therapeutic applications. {\textcopyright} The Author 2013. Published by Oxford University Press. All rights reserved.},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84897565140\&partnerID=40\&md5=4ee6b5b3f85e16eba322ceb8e0d69dd3},
	author = {Dias, A.M. and Dourado, J. and Lago, P. and Cabral, J. and Marcos-Pinto, R. and Salgueiro, P. and Almeida, C.R. and Carvalho, S. and Fonseca, S. and Lima, M. and Vilanova, M. and Dinis-Ribeiro, M. and Reis, C.A. and Pinho, S.S.}
}
@article {2325,
	title = {Molecularly designed surfaces for blood deheparinization using an immobilized heparin-binding peptide},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {88},
	year = {2009},
	note = {Cited By (since 1996): 12Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.31849PubMed ID: 18286636Language of Original Document: EnglishCorrespondence Address: Martins, M. C. L.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomaterials, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180, Porto, Portugal; email: cmartins@ineb.up.ptChemicals/CAS: carbonyldiimidazole, 530-62-1; heparin, 37187-54-5, 8057-48-5, 8065-01-8, 9005-48-5; imidazole, 1467-16-9, 288-32-4; leucine, 61-90-5, 7005-03-0; lysine, 56-87-1, 6899-06-5, 70-54-2; tetraethylene glycol, 112-60-7; Ethylene Glycol, 107-21-1; Heparin, 9005-49-6; Leucine, 61-90-5; Lysine, 56-87-1; PeptidesReferences: Dailey J. Blood. Ipswich, MA, USA: Medical Consulting Group; 1998Section, V., Chronic intermittent haemodialysis and prevention of clotting in the extracorporal system (2002) Nephrol Dialysis Transplant, 17, pp. 63-71;Zhang, Y.H., Singh, V.K., Yang, V.C., Novel approach for optimizing the capacity and efficacy of a protamine filter for clinical extracorporeal heparin removal (1998) Asaio J, 44, pp. M368-M373; 
Tao, W., Deyo, D.J., Brunston, R.L., Vertrees, R.A., Zwischenberger, J.B., Extracorporeal heparin adsorption following cardiopulmonary bypass with a heparin removal device - An alternative to protamine (1998) Critical Care Med, 26, pp. 1096-1102; 
Ameer, G.A., Barabino, G., Sasisekharan, R., Harmon, W., Cooney, C.L., Langer, R., Ex vivo evaluation of a Taylor-Couette flow, immobilized heparinase I device for clinical application (1999) Proc Natl Acad Sci USA, 96, pp. 2350-2355; 
Ostuni, E., Yan, L., Whitesides, G.M., The interaction of proteins and cells with self-assembled monolayers of alkanethiolates on gold and silver (1999) Colloids Surf B-Biointerfaces, 15, pp. 3-30; 
Mrksich, M., Whitesides, G.M., Using self-assembled monolayers that present oligo(ethylene glycol) groups to control the interactions of proteins with surfaces. Poly(Ethylene Glycol) (1997) ACS Symposium Series, 680, pp. 361-373; 
Cardin, A.D., Weintraub, H.J.R., Molecular modeling of proteinglycosaminoglycan interactions (1989) Arteriosclerosis, 9, pp. 21-32; 
Kricheldorf, H.R., (1987) α-Amino Acid N-Carboxyanhydrides and Related Heterocycles, , New York: Springer Verlag;; 
Martins, M.C.L., Ratner, B.D., Barbosa, M.A., Protein adsorption on mixtures of hydroxyl- and methylterminated alkanethiols self-assembled monolayers (2003) J Biomed Mater Res A, 67, pp. 158-171; 
Lee, H.J., Nedelkov, D., Corn, R.M., Surface plasmon resonance imaging measurements of antibody arrays for the multiplexed detection of low molecular weight protein biomarkers (2006) Anal Chem, 78, pp. 6504-6510; 
Roeges, N.P.G., (1994) A Guide to the Complete Interpretation of Infrared Spectra of Organic Structures, , England: Wiley;; 
Li, L.Y., Chen, S.F., Zheng, J., Ratner, B.D., Jiang, S.Y., Protein adsorption on oligo(ethylene glycol)-terminated alkanethiolate self-assembled monolayers: The molecular basis for non-fouling behavior (2005) J Phys Chem B, 109, pp. 2934-2941; 
Beamson, G., High, B.D., (1992) Resolution XPS of Organic Polymers, , Chichester: Wiley;; 
Sousa, S.R., Moradas, F.P., Saramago, B., Viseu, M.L., Barbosa, M.A., Human serum albumin adsorption on TiO2 from single protein solutions and from plasma (2004) Langmuir, 20, pp. 9745-9754; 
Socrates, G., (2001) Infrared and Raman Characteristic Group Frequencies: Tables and Charts, , Chichester: Wiley;; 
Capila, I., Linhardt, R.J., Heparin - Protein interactions (2002) Angewandte Chemie-Int Ed, 41, pp. 391-112; 
Snell, C.R.F.G., Kinetics and thermodynamics of the alpha Helix - β Transconformation of poly(L-lysine) and L-leucine copolymers. A compensation phenomenon (1973) Biochemistry, 12, pp. 1017-1025; 
Hearn, M.T.W., 1,1'-Carbonyldiimidazole-mediated immobilization of enzymes and affinity ligands (1987) Methods Enzymol, 135, pp. 102-117; 
Stollner, D., Scheller, F.W., Warsinke, A., Activation of cellulose membranes with 1,1'-carbonyldiimidazole or 1-cyano-4-dimethylaminopyridinium tetrafluoroborate as a basis for the development of immunosensors (2002) Anal Biochem, 304, pp. 157-165
},
	month = {2009///},
	pages = {162 - 173},
	abstract = {Systemic heparinization, used during haemodialysis to prevent blood clotting on the extracorporeal circuit, leads to a high incidence of hemorrhagic complications. The adverse reactions associated with heparin neutralization using protamine sulphate justify the development of an alternative system for blood deheparinization. The main objective of this work is to design nanostructured surfaces with the capacity to bind heparin from blood in a selective way. A heparin-binding polypeptide, composed of L-lysine and L-leucine (pKL), was synthesized and immobilized, in different concentrations, onto self-assembled monolayers (SAMs) terminated with tetra(ethylene-glycol) (EG4 SAMs). Immobilization was performed using a fixed concentration of pKL after surface activation to different degrees using a range of CDI (N,N'-carbonyldiimidazole) concentrations. Results demonstrated that the presence of pKL increases heparin adsorption to EG4-SAMs, independently of the pKL concentration and the way of immobilization (adsorption or covalent bound). Selectivity towards heparin was successfully achieved on SAMs with low concentrations of immobilized pKL (9-17\% of pKL). Surfaces were characterized using ellipsometry, contact angle measurements, Fourier transform infrared reflection absorption spectroscopy (IRAS), atomic force microscopy, and X-ray photoelectron spectroscopy. Heparin adsorption was assessed using IRAS and N-sulphonate-                        35S-heparin. Therefore, this study could give a good contribution for the design of blood deheparinization devices. {\textcopyright} 2008 Wiley Periodicals, Inc.
},
	keywords = {Absorption spectroscopy, Adsorption, Alternative systems, Amines, Amino acids, Angle measurement, article, Atomic force microscopy, Atomic forces, Atomic spectroscopy, Binding peptides, Blood, Blood clotting, Carbonyl diimidazole, Carbonyldiimidazole, Contact angle, deheparinization, device, Dialysis, Electron energy levels, ellipsometry, Ethylene, Ethylene Glycol, Fourier Transform Infrared, Fourier transforms, Glycols, Haemodialysis, heparin, heparin binding protein, Heparinization, High incidences, Humans, imidazole, immobilization, infrared spectroscopy, leucine, Low concentrations, lysine, Methods, Missile bases, Monolayers, nanomaterial, Nanostructured surfaces, Nanostructures, Peptide immobilization, Peptides, Photoelectron spectroscopy, Polysaccharides, Protein adsorption, protein binding, Renal Dialysis, Self assembled monolayers, Self-assembled monolayers, Sulphate, Surface activations, Surface functionalization, Surface Properties, surface property, tetraethylene glycol, unclassified drug, X ray photoelectron spectroscopy, X-ray photoelectron spectroscopies},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-57449118932\&partnerID=40\&md5=8f442ccbde0273f4ed4e04024a75fd37},
	author = {Martins, M.C.L. and Curtin, S.A. and Freitas, S.C. and Salgueiro, P. and Ratner, B.D. and Barbosa, M.A.}
}
