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Human recombinant lysosomal enzymes produced in microorganisms.
Espejo-Mojica, Ángela J; Alméciga-Díaz, Carlos J; Rodríguez, Alexander; Mosquera, Ángela; Díaz, Dennis; Beltrán, Laura; Díaz, Sergio; Pimentel, Natalia; Moreno, Jefferson; Sánchez, Jhonnathan; Sánchez, Oscar F; Córdoba, Henry; Poutou-Piñales, Raúl A; Barrera, Luis A.
Afiliação
  • Espejo-Mojica ÁJ; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia.
  • Alméciga-Díaz CJ; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia. Electronic address: cjalmeciga@javeriana.edu.co.
  • Rodríguez A; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia; Chemical Department, School of Science, Pontificia Universidad Javeriana, Bogotá, Colombia.
  • Mosquera Á; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia.
  • Díaz D; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia.
  • Beltrán L; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia.
  • Díaz S; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia.
  • Pimentel N; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia.
  • Moreno J; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia.
  • Sánchez J; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia.
  • Sánchez OF; School of Chemical Engineering, Purdue University, West Lafayette, IN, USA.
  • Córdoba H; Chemical Department, School of Science, Pontificia Universidad Javeriana, Bogotá, Colombia.
  • Poutou-Piñales RA; Laboratorio de Biotecnología Molecular, Grupo de Biotecnología Ambiental e Industrial (GBAI), School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia.
  • Barrera LA; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá, Colombia.
Mol Genet Metab ; 116(1-2): 13-23, 2015.
Article em En | MEDLINE | ID: mdl-26071627
Lysosomal storage diseases (LSDs) are caused by accumulation of partially degraded substrates within the lysosome, as a result of a function loss of a lysosomal protein. Recombinant lysosomal proteins are usually produced in mammalian cells, based on their capacity to carry out post-translational modifications similar to those observed in human native proteins. However, during the last years, a growing number of studies have shown the possibility to produce active forms of lysosomal proteins in other expression systems, such as plants and microorganisms. In this paper, we review the production and characterization of human lysosomal proteins, deficient in several LSDs, which have been produced in microorganisms. For this purpose, Escherichia coli, Saccharomyces cerevisiae, Pichia pastoris, Yarrowia lipolytica, and Ogataea minuta have been used as expression systems. The recombinant lysosomal proteins expressed in these hosts have shown similar substrate specificities, and temperature and pH stability profiles to those produced in mammalian cells. In addition, pre-clinical results have shown that recombinant lysosomal enzymes produced in microorganisms can be taken-up by cells and reduce the substrate accumulated within the lysosome. Recently, metabolic engineering in yeasts has allowed the production of lysosomal enzymes with tailored N-glycosylations, while progresses in E. coli N-glycosylations offer a potential platform to improve the production of these recombinant lysosomal enzymes. In summary, microorganisms represent convenient platform for the production of recombinant lysosomal proteins for biochemical and physicochemical characterization, as well as for the development of ERT for LSD.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Recombinantes / Proteínas / Doenças por Armazenamento dos Lisossomos / Lisossomos Limite: Animals / Humans Idioma: En Revista: Mol Genet Metab Assunto da revista: BIOLOGIA MOLECULAR / BIOQUIMICA / METABOLISMO Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Colômbia País de publicação: Estados Unidos
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Recombinantes / Proteínas / Doenças por Armazenamento dos Lisossomos / Lisossomos Limite: Animals / Humans Idioma: En Revista: Mol Genet Metab Assunto da revista: BIOLOGIA MOLECULAR / BIOQUIMICA / METABOLISMO Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Colômbia País de publicação: Estados Unidos