The caspase-generated cleavage product of Ets-1 p51 and Ets-1 p27, Cp17, induces apoptosis
| Autor: | Marc Aumercier, David Tulasne, Souhaila Choul-Li |
|---|---|
| Přispěvatelé: | Facuté de Sciences, Université Chouaib Doukkali (UCD), Mécanismes de la Tumorigénèse et Thérapies Ciblées - UMR 8161 (M3T), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université de Lille, Institut Pasteur de Madagascar, Réseau International des Instituts Pasteur (RIIP), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS), Université de Lille, Sciences et Technologies, la Ligue contre le Cancer, Comite du Pas-de-Calais, Mécanismes de la Tumorigénèse et Thérapies Ciblées (M3T) - UMR 8161 (M3T), UMR1409, Unité de Glycobiologie Structurale et Fonctionnelle, Institut National de la Recherche Agronomique (INRA), Université de Lille-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Gene isoform Cleavage factor Programmed cell death [SDV]Life Sciences [q-bio] Biophysics Apoptosis Cp17 fragment Cleavage (embryo) Biochemistry Madin Darby Canine Kidney Cells Ets-1 Proto-Oncogene Protein c-ets-1 03 medical and health sciences Exon Dogs Animals Humans Protein Isoforms Molecular Biology Transcription factor Caspase biology Caspase 3 Cell Biology Exons Molecular biology Peptide Fragments Recombinant Proteins 030104 developmental biology HEK293 Cells Caspases biology.protein |
| Zdroj: | Biochemical and Biophysical Research Communications Biochemical and Biophysical Research Communications, Elsevier, 2016, 480 (1), pp.1-7. ⟨10.1016/j.bbrc.2016.10.020⟩ Biochemical and Biophysical Research Communications, 2016, 480 (1), pp.1-7. ⟨10.1016/j.bbrc.2016.10.020⟩ |
| ISSN: | 0006-291X 1090-2104 |
| Popis: | The transcription factor Ets-1 is involved in various physiological processes and invasive pathologies. Human Ets-1 exists under three isoforms: p51, the predominant full-length isoform, p42 and p27, shorter alternatively spliced isoforms. We have previously demonstrated that Ets-1 p51, but not the spliced variant Ets-1 p42, is processed by caspases in vitro and during apoptosis. However, the caspase cleavage of the second spliced variant Ets-1 p27 remains to investigate. In the present study, we demonstrate that Ets-1 p27 is a cleavage substrate of caspases. We show that Ets-1 p27 is processed in vitro by caspase-3, resulting in three C-terminal fragments Cp20, Cp17 and Cp14. Similarly, Ets-1 p27 was cleaved during apoptotic cell death induced by anisomycin, producing fragments consistent with those observed in in vitro cleavage assay. These fragments are generated by cleavage at three sites located in the exon VII-encoded region of Ets-1 p27. As a functional consequences, Cp17 fragment, the major cleavage product generated during apoptosis, induced itself apoptosis when transfected into cells. Our results show that Ets-1 p27 is cleaved in the same manner as Ets-1 p51 within the exon VII-encoded region, thus generating a stable C-terminal fragment that induces cell death by initiating apoptosis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect