Identification and functional characterization of two executioner caspases in Crassostrea gigas.
Caspase-3 and caspase-7 are two key effector caspases that play important roles in apoptotic pathways that maintain normal tissue and organ development and homeostasis. However, little is known about the sequence, structure, activity, and function of effector caspases upon apoptosis in mollusks, esp...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3923871?pdf=render |
| _version_ | 1818153099156520960 |
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| author | Tao Qu Baoyu Huang Linlin Zhang Li Li Fei Xu Wen Huang Chunyan Li Yishuai Du Guofan Zhang |
| author_facet | Tao Qu Baoyu Huang Linlin Zhang Li Li Fei Xu Wen Huang Chunyan Li Yishuai Du Guofan Zhang |
| author_sort | Tao Qu |
| collection | DOAJ |
| description | Caspase-3 and caspase-7 are two key effector caspases that play important roles in apoptotic pathways that maintain normal tissue and organ development and homeostasis. However, little is known about the sequence, structure, activity, and function of effector caspases upon apoptosis in mollusks, especially marine bivalves. In this study, we investigated the possible roles of two executioner caspases in the regulation of apoptosis in the Pacific oyster Crassostrea gigas. A full-length caspase-3-like gene named Cgcaspase-3 was cloned from C.gigas cDNA, encoding a predicted protein containing caspase family p20 and p10 domain profiles and a conserved caspase active site motif. Phylogenetic analysis demonstrated that both Cgcaspase-3 and Cgcaspase-1 may function as effector caspases clustered in the invertebrate branch. Although the sequence identities between the two caspases was low, both enzymes possessed executioner caspase activity and were capable of inducing cell death. These results suggested that Cgcaspase-3 and Cgcaspase-1 were two effector caspases in C. gigas. We also observed that nucleus-localized Cgcaspase-3, may function as a caspase-3-like protein and cytoplasm-localized Cgcaspase-1 may function as a caspase-7-like protein. Both Cgcaspase-3 and Cgcaspase-1 mRNA expression increased after larvae settled on the substratum, suggesting that both caspases acted in several tissues or organs that degenerated after oyster larvae settlement. The highest caspase expression levels were observed in the gills indicating that both effector caspases were likely involved in immune or metabolic processes in C. gigas. |
| first_indexed | 2024-12-11T14:05:13Z |
| format | Article |
| id | doaj.art-db45caa4add546a69970c4df0aa75fc7 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T14:05:13Z |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-db45caa4add546a69970c4df0aa75fc72022-12-22T01:03:41ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0192e8904010.1371/journal.pone.0089040Identification and functional characterization of two executioner caspases in Crassostrea gigas.Tao QuBaoyu HuangLinlin ZhangLi LiFei XuWen HuangChunyan LiYishuai DuGuofan ZhangCaspase-3 and caspase-7 are two key effector caspases that play important roles in apoptotic pathways that maintain normal tissue and organ development and homeostasis. However, little is known about the sequence, structure, activity, and function of effector caspases upon apoptosis in mollusks, especially marine bivalves. In this study, we investigated the possible roles of two executioner caspases in the regulation of apoptosis in the Pacific oyster Crassostrea gigas. A full-length caspase-3-like gene named Cgcaspase-3 was cloned from C.gigas cDNA, encoding a predicted protein containing caspase family p20 and p10 domain profiles and a conserved caspase active site motif. Phylogenetic analysis demonstrated that both Cgcaspase-3 and Cgcaspase-1 may function as effector caspases clustered in the invertebrate branch. Although the sequence identities between the two caspases was low, both enzymes possessed executioner caspase activity and were capable of inducing cell death. These results suggested that Cgcaspase-3 and Cgcaspase-1 were two effector caspases in C. gigas. We also observed that nucleus-localized Cgcaspase-3, may function as a caspase-3-like protein and cytoplasm-localized Cgcaspase-1 may function as a caspase-7-like protein. Both Cgcaspase-3 and Cgcaspase-1 mRNA expression increased after larvae settled on the substratum, suggesting that both caspases acted in several tissues or organs that degenerated after oyster larvae settlement. The highest caspase expression levels were observed in the gills indicating that both effector caspases were likely involved in immune or metabolic processes in C. gigas.http://europepmc.org/articles/PMC3923871?pdf=render |
| spellingShingle | Tao Qu Baoyu Huang Linlin Zhang Li Li Fei Xu Wen Huang Chunyan Li Yishuai Du Guofan Zhang Identification and functional characterization of two executioner caspases in Crassostrea gigas. PLoS ONE |
| title | Identification and functional characterization of two executioner caspases in Crassostrea gigas. |
| title_full | Identification and functional characterization of two executioner caspases in Crassostrea gigas. |
| title_fullStr | Identification and functional characterization of two executioner caspases in Crassostrea gigas. |
| title_full_unstemmed | Identification and functional characterization of two executioner caspases in Crassostrea gigas. |
| title_short | Identification and functional characterization of two executioner caspases in Crassostrea gigas. |
| title_sort | identification and functional characterization of two executioner caspases in crassostrea gigas |
| url | http://europepmc.org/articles/PMC3923871?pdf=render |
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