| Revista: | Biotecnología aplicada |
| Base de datos: | PERIÓDICA |
| Número de sistema: | 000353534 |
| ISSN: | 0864-4551 |
| Autores: | González González, Yamile1 Gil, Dayrom1 Alonso del Rivero, Maday1 Besada, Vladimir2 Gil, Jeovanis2 Araujo, Mariana S3 Tanaka, Aparecida S3 Pons, Tirso1 Chávez, María de los Angeles1 |
| Instituciones: | 1Universidad de La Habana, Facultad de Biología, La Habana. Cuba 2Centro de Ingeniería Genética y Biotecnología, División de Química-Física, La Habana. Cuba 3Universidade Federal de Sao Paulo, Instituto de Farmacologia e Biologia Molecular, Sao Paulo. Brasil |
| Año: | 2010 |
| Volumen: | 27 |
| Número: | 4 |
| Paginación: | 311-313 |
| País: | Cuba |
| Idioma: | Inglés |
| Tipo de documento: | Artículo |
| Enfoque: | Experimental, aplicado |
| Resumen en inglés | Two new protease inhibitors (PIs), CmPI-II and AdKI were purified and characterized from mollusks Cenchritis muricatus and Aplysia dactylomela, respectively. They showed different specificities, CmPI-II for human neutrophil elastase (HNE) and AdKI for human plasma kallikrein (HPK). Purification procedures were established, rendering good yields and high purification degree. CmPI-II (UNIPROT: P84755) is a 5480 Da polypeptide of three disulphide bridges belong to the “non-classical” Kazal-type inhibitors. A new group was proposed according to the location of the CysI-CysV disulfide bridge. The presence of a basic residue at the inhibitor active site changed the pre-established requirement of a hydrophobic residue for elastase inhibition. The three-dimensional CmPI-II/HNE complex model contributes to explain the CmPI-II specificity for the enzyme. This is the first PI molecule isolated from C. muricatus. On the other hand, AdKI (2.9 kDa polypeptide) is an exception among invertebrate inhibitors in terms of inhibitory strength and selectivity against HPK. A new serine protease, AdSP, was also purified and characterized from the same extract, which could be the target for AdKI. CmPI-II and AdKI are the first inhibitors isolated from the phyllum Mollusca against ENH and HPK, respectively |
| Disciplinas: | Medicina |
| Palabras clave: | Farmacología, Bioquímica, Proteasas, Inhibidores enzimáticos, Elastasa, Calicreína |
| Keyword: | Medicine, Pharmacology, Biochemistry, Proteases, Enzymatic inhibitors, Elastase, Kallikrein |
| Texto completo: | Texto completo (Ver PDF) |
