Google Scholar: cites
Characterization, Recombinant Production and Structure-Function Analysis of NvCI, A Picomolar Metallocarboxypeptidase Inhibitor from the Marine Snail Nerita versicolor
Covaleda Cortés, Giovanny (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Hernández, Martha (Universidad de Concepción (Xile). Centro de Biotecnología)
Trejo, Sebastián A. (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Mansur, Manuel (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Rodríguez Calado, Sergi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Garcia Pardo, Javier (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Lorenzo Rivera, Julia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Vendrell i Roca, Josep (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Chávez, María Ángeles (Universidad de la Habana. Centro de Estudio de Proteínas)
Alonso del Rivero, Maday (Universidad de la Habana. Centro de Estudio de Proteínas)
Avilés, Francesc X. (Francesc Xavier) (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular

Data: 2019
Resum: A very powerful proteinaceous inhibitor of metallocarboxypeptidases has been isolated from the marine snail Nerita versicolor and characterized in depth. The most abundant of four, very similar isoforms, NvCla, was taken as reference and N-terminally sequenced to obtain a 372-nucleotide band coding for the protein cDNA. The mature protein contains 53 residues and three disulphide bonds. NvCIa and the other isoforms show an exceptionally high inhibitory capacity of around 1. 8 pM for human Carboxypeptidase A1 (hCPA1) and for other A-like members of the M14 CPA subfamily, whereas a twofold decrease in inhibitory potency is observed for carboxypeptidase B-like members as hCPB and hTAFIa. A recombinant form, rNvCI, was produced in high yield and HPLC, mass spectrometry and spectroscopic analyses by CD and NMR indicated its homogeneous, compact and thermally resistant nature. Using antibodies raised with rNvCI and histochemical analyses, a preferential distribution of the inhibitor in the surface regions of the animal body was observed, particularly nearby the open entrance of the shell and gut, suggesting its involvement in biological defense mechanisms. The properties of this strong, small and stable inhibitor of metallocarboxypeptidases envisage potentialities for its direct applicability, as well as leading or minimized forms, in biotechnological/biomedical uses.
Nota: Número d'acord de subvenció MINECO/BIO2013-44973-R
Nota: Número d'acord de subvenció MINECO/BIO2016-78057-R
Nota: Número d'acord de subvenció AGAUR/2017/SGR-1584
Nota: Número d'acord de subvenció AGAUR/2014/SGR-1658
Drets: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original. Creative Commons
Llengua: Anglès.
Document: article ; recerca ; publishedVersion
Matèria: Nerita versicolor ; Proteinaceous inhibitor ; Recombinant production ; Carboxypeptidase ; Picomolar inhibition ; Biotechnological and biomedical applications
Publicat a: Marine Drugs, Vol. 17, Issue 9 (September 2019) , art. 511, ISSN 1660-3397

DOI: 10.3390/md17090511
PMID: 31470614


19 p, 4.1 MB

El registre apareix a les col·leccions:
Articles > Articles de recerca
Articles > Articles publicats

 Registre creat el 2019-10-03, darrera modificació el 2019-11-11



   Favorit i Compartir