TY - JOUR
T1 - A novel bio-functional material based on mammalian cell aggresomes
AU - Rodríguez-Carmona, Escarlata
AU - Mendoza, Rosa
AU - Ruiz-Cánovas, Eugènia
AU - Ferrer-Miralles, Neus
AU - Abasolo, Ibane
AU - Schwartz, Simó
AU - Villaverde, Antonio
AU - Corchero, José Luis
PY - 2015/9/18
Y1 - 2015/9/18
N2 - © 2015, Springer-Verlag Berlin Heidelberg. Aggresomes are protein aggregates found in mammalian cells when the intracellular protein degradation machinery is over-titered. Despite that they abound in cells producing recombinant proteins of biomedical and biotechnological interest, the physiological roles of these protein clusters and the functional status of the embedded proteins remain basically unexplored. In this work, we have determined for the first time that, like in bacterial inclusion bodies, deposition of recombinant proteins into aggresomes does not imply functional inactivation. As a model, human α-galactosidase A (GLA) has been expressed in mammalian cells as enzymatically active, mechanically stable aggresomes showing higher thermal stability than the soluble GLA version. Since aggresomes are easily produced and purified, we propose these particles as novel functional biomaterials with potential as carrier-free, self-immobilized catalyzers in biotechnology and biomedicine.
AB - © 2015, Springer-Verlag Berlin Heidelberg. Aggresomes are protein aggregates found in mammalian cells when the intracellular protein degradation machinery is over-titered. Despite that they abound in cells producing recombinant proteins of biomedical and biotechnological interest, the physiological roles of these protein clusters and the functional status of the embedded proteins remain basically unexplored. In this work, we have determined for the first time that, like in bacterial inclusion bodies, deposition of recombinant proteins into aggresomes does not imply functional inactivation. As a model, human α-galactosidase A (GLA) has been expressed in mammalian cells as enzymatically active, mechanically stable aggresomes showing higher thermal stability than the soluble GLA version. Since aggresomes are easily produced and purified, we propose these particles as novel functional biomaterials with potential as carrier-free, self-immobilized catalyzers in biotechnology and biomedicine.
KW - Aggresomes
KW - Immobilized catalyzer
KW - Protein nanoparticles
KW - Recombinant protein
U2 - https://doi.org/10.1007/s00253-015-6684-0
DO - https://doi.org/10.1007/s00253-015-6684-0
M3 - Article
SN - 0175-7598
VL - 99
SP - 7079
EP - 7088
JO - Applied Microbiology and Biotechnology
JF - Applied Microbiology and Biotechnology
ER -