



@article {2447,
	title = {Biological evaluation of calcium alginate microspheres as a vehicle for the localized delivery of a therapeutic enzyme},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {74},
	year = {2005},
	note = {Cited By (since 1996): 12Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.30348PubMed ID: 16028235Language of Original Document: EnglishCorrespondence Address: Barrias, C.C.; Instituto de Engenharia Biom{\'e}dica (INEB), Laborat{\'o}rio de Biomateriais, 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; calcium alginate, 9005-35-0; glucosylceramidase, 37228-64-1; iodine 125, 14158-31-7, 22822-81-7; Alginates; alginic acid, 9005-32-7; Drug Carriers; Enzymes, Immobilized; Glucosylceramidase, EC 3.2.1.45; Glucuronic Acid, 576-37-4; Hexuronic AcidsManufacturers: GenzymeReferences: Grabowski, G.A., Leslie, N., Wenstrup, R., Enzyme therapy for Gaucher disease: The first 5 years (1998) Blood Rev, 12, pp. 115-133;Zhao, H., Grabowski, G.A., Gaucher disease: Perspectives on a prototype lysosomal disease (2002) Cell Mol Life Sci, 59, pp. 694-707; 
Friedman, B., Vaddi, K., Preston, C., Mahon, E., Cataldo, J.R., McPherson, J.M., A comparison of the pharmacological properties of carbohydrate remodeled recombinant and placental-derived beta-glucocerebrosidase: Implications for clinical efficacy in treatment of Gaucher disease (1999) Blood, 93, pp. 2807-2816; 
Rasmussen, J., Barsomian, G., Bergh, M., Enzymatically active recombinant glucocerebrosidase. U.S. patent 6451600. 17 September 2002Elstein, D., Itzchaki, M., Mankin, H.J., Skeletal involvement in Gaucher{\textquoteright}s disease (1997) Baillieres Clin Haematol, 10, pp. 793-816; 
Wenstrup, R.J., Roca-Espiau, M., Weinreb, N.J., Bembi, B., Skeletal aspects of Gaucher disease: A review (2002) Br J Radiol, 75 (SUPPL. 1), pp. A2-A12; 
Mistry, P.K., Wraight, E.P., Cox, T.M., Therapeutic delivery of proteins to macrophages: Implications for treatment of Gaucher{\textquoteright}s disease (1996) Lancet, 348, pp. 1555-1559; 
Gregoriadis, G., Neerunjun, D., Meade, T.W., Goolamali, S.K., Weereratne, H., Bull, G., Experiences after long-term treatment of a type I Gaucher disease patient with liposome-entrapped glucocerebroside: Beta-glucosidase (1980) Birth Defects Orig Artic Ser, 16, pp. 383-392; 
Dale, G.L., Kuhl, W., Beutler, E., Incorporation of glucocerebrosidase into Gaucher{\textquoteright}s disease monocytes in vitro (1979) Proc Natl Acad Sci USA, 76, pp. 473-475; 
Beutler, E., Dale, G.L., Guinto, D.E., Kuhl, W., Enzyme replacement therapy in Gaucher{\textquoteright}s disease: Preliminary clinical trial of a new enzyme preparation (1977) Proc Natl Acad Sci USA, 74, pp. 4620-4623; 
Belchetz, P.E., Crawley, J.C., Braidman, I.P., Gregoriadis, G., Treatment of Gaucher{\textquoteright}s disease with liposome-entrapped glucocerebroside: Beta-glucosidase (1977) Lancet, 2, pp. 116-117; 
Korablyov, V., Zimran, A., Barenholz, Y., Cerebroside-beta-glucosidase encapsulation in liposomes for Gaucher{\textquoteright}s disease treatment revisited (1999) Pharm Res, 16, pp. 466-469; 
Busto, M.D., Ortega, N., Perez-Mateos, M., Effect of immobilization on the stability of bacterial and fungal beta-glucosidase (1997) Process Biochem, 32, pp. 441-449; 
Dashevsky, A., Protein loss by the microencapsulation of an enzyme (lactase) in alginate beads (1998) Int J Pharm, 161, pp. 1-5; 
Blandino, A., Macias, M., Cantero, D., Immobilization of glucose oxidase within calcium alginate gel capsules (2001) Process Biochem, 36, pp. 601-606; 
Kokufuta, E., Shimizu, N., Tanaka, H., Nakamura, I., Use of polyelectrolyte complex-stabilised calcium alginate gel for entrapment of beta-amylase (1988) Biotechnol Bioeng, 33, pp. 756-759; 
Edelman, E.R., Mathiowitz, E., Langer, R., Klagsbrun, M., Controlled and modulated release of basic fibroblast growth factor (1991) Biomaterials, 12, pp. 619-626; 
Peters, M.C., Isenberg, B.C., Rowley, J.A., Mooney, D.J., Release from alginate enhances the biological activity of vascular endothelial growth factor (1998) J Biomater Sci Polym Ed, 9, pp. 1267-1278; 
Alsberg, E., Anderson, K.W., Albeiruti, A., Franceschi, R.T., Mooney, D.J., Cell-interactive alginate hydrogels for bone tissue engineering (2001) J Dent Res, 80, pp. 2025-2029; 
Rowley, J.A., Madlambayan, G., Mooney, D.J., Alginate hydrogels as synthetic extracellular matrix materials (1999) Biomaterials, 20, pp. 45-53; 
Gagne, T.A., Chappell-Afonso, K., Johnson, J.L., McPherson, J.M., Oldham, C.A., Tubo, R.A., Vaccaro, C., Vasios, G.W., Enhanced proliferation and differentiation of human articular chondrocytes when seeded at low cell densities in alginate in vitro (2000) J Orthop Res, 18, pp. 882-890; 
(1993) Iodine-125. A Guide to Radioiodination Techniques: Amersham Life Science, , Amersham Place, Little Chalfont, Bucks: Amersham International pic; 64 pp; 
Sa Miranda, M.C., Aerts, J.M., Pinto, R., Fontes, A., De Lacerda, L.W., Van Weely, S., Barranger, J., Tager, J.M., Activity of glucocerebrosidase in extracts of different cell types from type 1 Gaucher disease patients (1990) Clin Genet, 38, pp. 218-227; 
Smith, P.K., Krohn, R.I., Hermanson, G.T., Mallia, A.K., Gartner, F.H., Provenzano, M.D., Fujimoto, E.K., Klenk, D.C., Measurement of protein using bicinchoninic acid (1985) Anal Biochem, 150, pp. 76-85; 
Sa Miranda, M.C., Aerts, J.M., Pinto, R.A., Magalhaes, J.A., Barranger, J.A., Tager, J.M., Schram, A.W., Heterogeneity in human acid beta-glucosidase revealed by cellulose-acetate electrophoresis (1988) Biochim Biophys Acta, 965, pp. 163-168; 
Smidsrod, O., Draget, K.I., Chemistry and physical properties of alginates (1996) Carbohyd Eur, 14, pp. 6-13; 
Gaserod, O., Sannes, A., Skjak-Braek, G., Microcapsules of alginate-chitosan. II. A study of capsule stability and permeability (1999) Biomaterials, 20, pp. 773-783; 
Aslani, P., Kennedy, R.A., Studies on diffusion in alginate gels. I. Effect of cross-linking with calcium or zinc ions on diffusion of acetaminophen (1996) J Control Release, 42, pp. 75-82
},
	month = {2005///},
	pages = {545 - 552},
	abstract = {Gaucher disease (GD) is caused by the decreased activity and/or stability of the lysosomal enzyme glucocerebrosidase (GCR). The available treatment consists in the intravenous administration of exogenous GCR, and is effective in reverting most of the symptoms. However, in terms of bone pathology, which is among the most disabling manifestations, a slow and incomplete response is observed, indicating that adjuvant therapies are necessary to consistently restore GCR activity in bone and accelerate regeneration. In this study, calcium alginate microspheres were analyzed as a vehicle for localized GCR delivery to bone. Results demonstrated that the entrapped enzyme retained full activity and exhibited a broader pH-dependent activity profile, compared to that of free-GCR, with improved stability at physiological pH. GCR release profile was established, and it was demonstrated that GCR could be released in a sustained manner. The biological behavior of the system was evaluated by analyzing the uptake of released GCR by GCR-deficient cells from GD patients, using different techniques: GCR activity measurements, radiolabeling, and cellulose acetate electrophoresis. Results demonstrated that GCR was internalized by cells significantly enhancing the residual enzymatic activity. To achieve an activity reconstitution level comparable to that obtained using free-GCR, only half of the dose was required with entrapped-GCR. {\textcopyright} 2005 Wiley Periodicals, Inc.},
	keywords = {Alginates, alginic acid, article, Bone, bone disease, Bone Regeneration, Calcium alginate, Calcium Compounds, catalysis, Cell culture, Cells, Cultured, controlled study, Drug Carriers, drug delivery system, enzyme activity, enzyme assay, enzyme replacement, Enzymes, Enzymes, Immobilized, fibroblast culture, Fibroblasts, Gaucher disease, Gaucher disease (GD), Glucocerebrosidase (GCR), Glucosylceramidase, Glucuronic Acid, Hexuronic Acids, human, human cell, Humans, iodine 125, Localized delivery, lysosome enzyme, lysosome storage disease, microsphere, Microspheres, Pathology, pH effects, physiology, recombinant enzyme, Therapeutic enzyme},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-24044465170\&partnerID=40\&md5=bbcee8568e0c0223975853a8177439c8},
	author = {Barrias, C.C. and Lamghari, M. and Granja, P.L. and S{\'a} Miranda, M.C. and Barbosa, M.A.}
}
