Inhibition of human initiator caspase 8 and effector caspase 3 by cross-class inhibitory bovSERPINA3-1 and A3-3
| Autor: | Miguel Angel Sentandreu, Gerald Coulis, Didier Delourme, Laure Bremaud, Ahmed Ouali, Abdelghani Boudjellal, Xavier Blanchet, Samira Becila, Patrick Pélissier, Carlos Hernan Herrera-Mendez |
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| Přispěvatelé: | Universidad de Guanajuato, Université des Frères Mentouri (Constantine 1), Unité de Génétique Moléculaire Animale (UMR GMA), Institut National de la Recherche Agronomique (INRA)-Université de Limoges (UNILIM), Qualité des Produits Animaux (QuaPA), Institut National de la Recherche Agronomique (INRA), Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), Institut de la Nutrition de l'Alimentation et des Technologies Agro-Alimentaire (INATAA) |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Proteases
Inhibitor Molecular Sequence Data Biophysics Caspase 3 bovSERPINA3 Caspase 8 Biochemistry Substrate Specificity 03 medical and health sciences Structural Biology Catalytic Domain Genetics medicine Animals Humans Protein Isoforms Amino Acid Sequence Molecular Biology Serpins Caspase 030304 developmental biology Serpin 0303 health sciences biology Effector 030302 biochemistry & molecular biology Mutagenesis Cell Biology Trypsin Caspase Inhibitors Molecular biology Bovine muscle Mutagenesis Site-Directed biology.protein Cattle [CHIM.OTHE]Chemical Sciences/Other Sequence Alignment medicine.drug Cysteine |
| Zdroj: | FEBS Letters FEBS Letters, Wiley, 2009, 583 (17), pp.2743-2748. ⟨10.1016/j.febslet.2009.07.055⟩ |
| ISSN: | 0014-5793 1873-3468 |
| DOI: | 10.1016/j.febslet.2009.07.055⟩ |
| Popis: | Serpins are a superfamily of structurally conserved proteins. Inhibitory serpins use a suicide substrate-like mechanism. Some are able to inhibit cysteine proteases in cross-class inhibition. Here, we demonstrate for the first time the strong inhibition of initiator and effector caspases 3 and 8 by two purified bovine SERPINA3s. SERPINA 3-1 (uniprotkb: Q9TTE1 ) binds tighly to human CASP3 (uniprotkb: P42574 ) and CASP8 (uniprotkb: Q14790 ) with kass of 4.2 × 105 and 1.4 × 106 M−1 s−1, respectively. A wholly similar inhibition of human CASP3 and CASP8 by SERPINA3-3 (uniprotkb: Q3ZEJ6 ) was also observed with kass of 1.5 × 105 and 2.7 × 106 M−1 s−1, respectively and form SDS-stable complexes with both caspases. By site-directed mutagenesis of bovSERPINA3-3, we identified Asp371 as the potential P1 residue for caspases. The ability of other members of this family to inhibit trypsin and caspases was analysed and discussed. Structured summary MINT- 7234656 : CASP8 (uniprotkb: Q14790 ) and SERPINA3-1 (uniprotkb: Q9TTE1 ) bind (MI: 0407 ) by biochemical (MI: 0401 ) MINT- 7234634 : SERPINA3-3 (uniprotkb: Q3ZEJ6 ) and CASP3 (uniprotkb: P42574 ) bind (MI: 0407 ) by biochemical (MI: 0401 ) MINT- 7234663 : CASP8 (uniprotkb: Q14790 ) and SERPINA3-3 (uniprotkb: Q3ZEJ6 ) bind (MI: 0407 ) by biochemical (MI: 0401 ) MINT- 7234625 : SERPINA3-1 (uniprotkb: Q9TTE1 ) and CASP3 (uniprotkb: P42574 ) bind (MI: 0407 ) by biochemical (MI: 0401 ) |
| Databáze: | OpenAIRE |
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