Institutional Repository of Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
Caspase-3 serves as an intracellular immune receptor specific for lipopolysaccharide in oyster Crassostrea gigas | |
Xu, Jiachao1,3; Jiang, Shuai1; Li, Yiqun1,3; Li, Meijia1,3; Cheng, Qi1,4; Zhao, Depeng1,4; Yang, Bin1,3; Jia, Zhihao1,3; Wang, Lingling1; Song, Linsheng2 | |
2016-08-01 | |
发表期刊 | DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY |
卷号 | 61页码:1-12 |
文章类型 | Article |
摘要 | Apoptosis is a form of programmed cell death process controlled by a family of cysteine proteases called caspases, which plays a crucial role in the immune system homeostasis. The apoptosis and the detailed regulation mechanism have been well studied in vertebrate, but the information in lower animals, especially invertebrates, is still very limited. In the present study, Caspase-3 in the Pacific oyster Crassostrea gigas (designated CgCaspase-3) was enriched by lipopolysaccharide (LPS) affinity chromatography and further identified by MALDI-TOF/TOF-mass spectrometry. The binding activity of CgCaspase-3 to LPS was confirmed by enzyme-linked immunosorbent assay, and surface plasmon resonance analysis revealed its high binding specificity and moderate binding affinity (K-D = 1.08 x 10(-6) M) to LPS. The recombinant CgCaspase-3 exhibited high proteolytic activity to substrate Ac-DEVD-pNA and relatively weak activity to substrate Ac-DMQD-pNA and Ac-VDQQD-pNA. The binding of CgCaspase-3 to LPS significantly inhibited its proteolytic activity toward AC-DEVD-pNA in vitro. The over-expression of CgCaspase-3 leaded to the phosphatidylserine exposure on the external plasma membrane and the cleavage of poly (ADP-ribose) polymerase, which reduced cell viability, and finally induced cell apoptosis. But the cell apoptosis mediated by CgCaspase-3 in vivo was significantly inhibited by the treatment of LPS. These results collectively indicated that CgCaspase-3 could serve as an intracellular LPS receptor, and the interaction of LPS with CgCaspase-3 specifically inhibited the cell apoptosis induced by CgCaspase-3. (C) 2016 Elsevier Ltd. All rights reserved. |
关键词 | Crassostrea Gigas Caspase-3 Intracellular Immune Receptor Lps Immune Response Apoptosis |
DOI | 10.1016/j.dci.2016.03.015 |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000376804300001 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://ir.qdio.ac.cn/handle/337002/126232 |
专题 | 实验海洋生物学重点实验室 |
作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China 2.Dalian Ocean Univ, Minist Agr, Key Lab Mariculture & Stock Enhancement North Chi, Dalian 116023, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 4.Dalian Polytech Univ, Dalian 116034, Peoples R China |
第一作者单位 | 实验海洋生物学重点实验室 |
推荐引用方式 GB/T 7714 | Xu, Jiachao,Jiang, Shuai,Li, Yiqun,et al. Caspase-3 serves as an intracellular immune receptor specific for lipopolysaccharide in oyster Crassostrea gigas[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2016,61:1-12. |
APA | Xu, Jiachao.,Jiang, Shuai.,Li, Yiqun.,Li, Meijia.,Cheng, Qi.,...&Song, Linsheng.(2016).Caspase-3 serves as an intracellular immune receptor specific for lipopolysaccharide in oyster Crassostrea gigas.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,61,1-12. |
MLA | Xu, Jiachao,et al."Caspase-3 serves as an intracellular immune receptor specific for lipopolysaccharide in oyster Crassostrea gigas".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 61(2016):1-12. |
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