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The ancient CgPEPCK-1, not CgPECK-2, evolved into a multifunctional molecule as an intracellular enzyme and extracellular PRR
Yin, Xiaoting1,2,3; Qiu, Limei1,2; Long, Dandan1,2; Lv, Zhao1,2; Liu, Qing1,2; Wang, Senyu1,4; Zhang, Weiqian1; Zhang, Kexin1,4; Xie, Mengxi1
2023-08-01
发表期刊DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
ISSN0145-305X
卷号145页码:13
通讯作者Qiu, Limei(qiulimei@qdio.ac.cn)
摘要Phosphoenolpyruvate carboxykinase (PEPCK) is a well-known lyase involved in gluconeogenesis, while their evolution and function differentiation have not been fully understood. In this study, by constructing a phylogenetic tree to examine PEPCKs throughout the evolution from poriferans to vertebrates, Mollusk was highlighted as the only phylum to exhibit two distinct lineages, Mollusca_PEPCK-1 and Mollusca_PEPCK-2. Further study of two representative members from Crassostrea gigas (CgPEPCK-1 and CgPEPCK-2) showed that they both shared conserved sequences and structural characteristics of the catalytic enzyme, while CgPEPCK-2 displayed a higher expression level than CgPEPCK-1 in all tested tissues, and CgPEPCK-1 was specifically implicated in the immune defense against LPS stimulation and Vibrio splendidus infection. Functional analysis revealed that CgPEPCK-2 had stronger enzymatic activity than CgPEPCK-1, while CgPEPCK-1 exhibited stronger binding activity with various PAMPs, and only the protein of CgPEPCK-1 increased significantly in hemolymph during immune stimulation. All results supported that distinct sequence and function differentiations of the PEPCK gene family should have occurred since Mollusk. The more advanced evolutionary branch Mollusca_PEPCK-2 should preserve its essential function as a catalytic enzyme to be more specialized and efficient, while the ancient branch Mollusca_PEPCK-1 probably contained some members, such as CgPEPCK-1, that should be integrated into the immune system as an extracellular immune recognition receptor.
关键词PEPCK Gene evolution and differentiation PRR Catalyzing enzyme
DOI10.1016/j.dci.2023.104722
收录类别SCI
语种英语
资助项目National Natural Science Foundation of China[32072999]
WOS研究方向Fisheries ; Immunology ; Veterinary Sciences ; Zoology
WOS类目Fisheries ; Immunology ; Veterinary Sciences ; Zoology
WOS记录号WOS:001000706600001
出版者ELSEVIER SCI LTD
WOS关键词C-TYPE LECTIN ; PHOSPHOENOLPYRUVATE CARBOXYKINASE PEPCK ; INFLAMMATORY CASPASES ; VIBRIO-SPLENDIDUS ; STRESS-RESPONSE ; PROTEIN ; GTP ; MITOCHONDRIAL ; EXPRESSION ; INTEGRIN
引用统计
文献类型期刊论文
条目标识符http://ir.qdio.ac.cn/handle/337002/183205
专题实验海洋生物学重点实验室
通讯作者Qiu, Limei
作者单位1.Chinese Acad Sci, Inst Oceanol, CAS Ctr Ocean Mega Sci, CAS & Shandong Prov Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
2.Pilot Natl Lab Marine Sci & Technol Qingdao, Lab Marine Biol & Biotechnol, Qingdao 266237, Peoples R China
3.Univ Chinese Acad Sci, Coll Earth & Planetary Sci, Beijing 100049, Peoples R China
4.Qingdao Agr Univ, Sch Marine Biol & Engn, Qingdao 266109, Peoples R China
第一作者单位中国科学院海洋研究所
通讯作者单位中国科学院海洋研究所
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Yin, Xiaoting,Qiu, Limei,Long, Dandan,et al. The ancient CgPEPCK-1, not CgPECK-2, evolved into a multifunctional molecule as an intracellular enzyme and extracellular PRR[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2023,145:13.
APA Yin, Xiaoting.,Qiu, Limei.,Long, Dandan.,Lv, Zhao.,Liu, Qing.,...&Xie, Mengxi.(2023).The ancient CgPEPCK-1, not CgPECK-2, evolved into a multifunctional molecule as an intracellular enzyme and extracellular PRR.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,145,13.
MLA Yin, Xiaoting,et al."The ancient CgPEPCK-1, not CgPECK-2, evolved into a multifunctional molecule as an intracellular enzyme and extracellular PRR".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 145(2023):13.
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