Enregistré dans:
| Auteurs principaux: | , , , , , , , |
|---|---|
| Format: | Artículo científico |
| Langue: | en |
| Publié: |
Fish & shellfish immunology
2025
|
| Sujets: | |
| Accès en ligne: | https://pubmed.ncbi.nlm.nih.gov/40848963/ |
| Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
| _version_ | 1868266162714836994 |
|---|---|
| author | Yang, Chuanyan Xu, Jiachao Tong, Ziling Wang, Xiudan Jiang, Shuai Yang, Bin Wang, Lingling Song, Linsheng |
| author_facet | Yang, Chuanyan Xu, Jiachao Tong, Ziling Wang, Xiudan Jiang, Shuai Yang, Bin Wang, Lingling Song, Linsheng Yang, Chuanyan Xu, Jiachao Tong, Ziling Wang, Xiudan Jiang, Shuai Yang, Bin Wang, Lingling Song, Linsheng |
| collection | PubMed - marine biology |
| contents | The involvement of caspase-8-3 in cleavaging caspase-3 and immune response of oyster Crassostrea gigas. Yang, Chuanyan Xu, Jiachao Tong, Ziling Wang, Xiudan Jiang, Shuai Yang, Bin Wang, Lingling Song, Linsheng Animals Crassostrea Caspase 8 Phylogeny Caspase 3 Immunity, Innate Amino Acid Sequence Sequence Alignment Vibrio Gene Expression Regulation Gene Expression Profiling The caspase family play a crucial role in both apoptosis signaling and immune response. In the present study, a caspase-8 was identified from Crassostrea gigas (designed as CgCaspase-8-3), which contained two tandem death effector domains (DEDs) and a CASc domain, as well as conserved cysteine active site motif "QACQG". CgCaspase-8-3 was initially clustered with molluscan Caspase-8 homologs, and subsequently grouped with vertebrate sequences, while maintaining a relatively distant phylogenetic relationship from the mammalian clade. It was widely expressed in various tissues with the highest expression level in mantle, as well as in different development stages with the highest expression level in two-cell embryos. CgCaspase-8-3 was localized in the cytoplasm and co-localized with CgCaspase-3 in haemocytes. Although the full-length recombinant CgCaspase-8-3 showed weak proteolytic activity toward Ac-IETD-pNA, its C-terminal truncated form (rCgCaspase-8-3(CT)) displayed enhanced enzymatic activity and efficiently cleaved the downstream effector rCgCaspase-3 in vitro, indicating a direct role in the caspase activation cascade. This activity was significantly inhibited by the caspase-8-specific inhibitor Z-IETD-FMK. In addition, CgCaspase-8-3 mRNA expression in haemocytes significantly upregulated post LPS, PGN and Vibrio splendidus stimulation. All these results collectively indicate that CgCaspase-8-3 is involved in apoptosis and immune response in oyster. |
| format | Artículo científico |
| id | pubmed_40848963 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Fish & shellfish immunology |
| record_format | pubmed |
| spellingShingle | The involvement of caspase-8-3 in cleavaging caspase-3 and immune response of oyster Crassostrea gigas. Yang, Chuanyan Xu, Jiachao Tong, Ziling Wang, Xiudan Jiang, Shuai Yang, Bin Wang, Lingling Song, Linsheng Animals Crassostrea Caspase 8 Phylogeny Caspase 3 Immunity, Innate Amino Acid Sequence Sequence Alignment Vibrio Gene Expression Regulation Gene Expression Profiling The involvement of caspase-8-3 in cleavaging caspase-3 and immune response of oyster Crassostrea gigas. Yang, Chuanyan Xu, Jiachao Tong, Ziling Wang, Xiudan Jiang, Shuai Yang, Bin Wang, Lingling Song, Linsheng Animals Crassostrea Caspase 8 Phylogeny Caspase 3 Immunity, Innate Amino Acid Sequence Sequence Alignment Vibrio Gene Expression Regulation Gene Expression Profiling The caspase family play a crucial role in both apoptosis signaling and immune response. In the present study, a caspase-8 was identified from Crassostrea gigas (designed as CgCaspase-8-3), which contained two tandem death effector domains (DEDs) and a CASc domain, as well as conserved cysteine active site motif "QACQG". CgCaspase-8-3 was initially clustered with molluscan Caspase-8 homologs, and subsequently grouped with vertebrate sequences, while maintaining a relatively distant phylogenetic relationship from the mammalian clade. It was widely expressed in various tissues with the highest expression level in mantle, as well as in different development stages with the highest expression level in two-cell embryos. CgCaspase-8-3 was localized in the cytoplasm and co-localized with CgCaspase-3 in haemocytes. Although the full-length recombinant CgCaspase-8-3 showed weak proteolytic activity toward Ac-IETD-pNA, its C-terminal truncated form (rCgCaspase-8-3(CT)) displayed enhanced enzymatic activity and efficiently cleaved the downstream effector rCgCaspase-3 in vitro, indicating a direct role in the caspase activation cascade. This activity was significantly inhibited by the caspase-8-specific inhibitor Z-IETD-FMK. In addition, CgCaspase-8-3 mRNA expression in haemocytes significantly upregulated post LPS, PGN and Vibrio splendidus stimulation. All these results collectively indicate that CgCaspase-8-3 is involved in apoptosis and immune response in oyster. |
| title | The involvement of caspase-8-3 in cleavaging caspase-3 and immune response of oyster Crassostrea gigas. |
| topic | Animals Crassostrea Caspase 8 Phylogeny Caspase 3 Immunity, Innate Amino Acid Sequence Sequence Alignment Vibrio Gene Expression Regulation Gene Expression Profiling |
| url | https://pubmed.ncbi.nlm.nih.gov/40848963/ |