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RUAN Lingwei,XU Haipeng,LIN Wenyang,SHI Hong,CUI Zhizhong,XU Xun. 2017. A novel beta-galactose-specific lectin of the tubeworm, Ridgeia piscesae, from the hydrothermal vent. Acta Oceanologica Sinica, 36(6):61-67
A novel beta-galactose-specific lectin of the tubeworm, Ridgeia piscesae, from the hydrothermal vent
深海热液区管状蠕虫Ridgeia piscesae β型半乳糖凝集素的克隆与功能研究
Received:March 03, 2016  Revised:August 03, 2016
DOI:10.1007/s13131-017-1052-9
Key words:galectin  antitumor  apoptosis  tubeworm  Ridgeia piscesae
中文关键词:  galectin  antitumor  apoptosis  tubeworm  Ridgeia piscesae
基金项目:The Major State Basic Research Development Program of China (973 Program) under contract No. 2015CB755906; China Ocean Mineral Resources R&D Association under contract No. DYXM-115-02-2-16.
Author NameAffiliationE-mail
RUAN Lingwei State Key Laboratory Breeding Base of Marine Genetic Resources, Xiamen 361005, China
Key Laboratory of Marine Genetic Resources of State Oceanic Administration, Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, China
Fujian Key Laboratory of Marine Genetic Resources, Xiamen 361005, China 
ruanlingwei@aliyun.com 
XU Haipeng State Key Laboratory Breeding Base of Marine Genetic Resources, Xiamen 361005, China
Key Laboratory of Marine Genetic Resources of State Oceanic Administration, Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, China
Fujian Key Laboratory of Marine Genetic Resources, Xiamen 361005, China
Animal Science and Technology College, Shandong Agricultural University, Tai'an 271018, China 
 
LIN Wenyang State Key Laboratory Breeding Base of Marine Genetic Resources, Xiamen 361005, China
Key Laboratory of Marine Genetic Resources of State Oceanic Administration, Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, China
Fujian Key Laboratory of Marine Genetic Resources, Xiamen 361005, China 
 
SHI Hong State Key Laboratory Breeding Base of Marine Genetic Resources, Xiamen 361005, China
Key Laboratory of Marine Genetic Resources of State Oceanic Administration, Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, China
Fujian Key Laboratory of Marine Genetic Resources, Xiamen 361005, China 
 
CUI Zhizhong Animal Science and Technology College, Shandong Agricultural University, Tai'an 271018, China  
XU Xun State Key Laboratory Breeding Base of Marine Genetic Resources, Xiamen 361005, China
Key Laboratory of Marine Genetic Resources of State Oceanic Administration, Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, China
Fujian Key Laboratory of Marine Genetic Resources, Xiamen 361005, China 
 
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Abstract:
      Lectins are sugar-specific binding proteins or glycoproteins that play important physiological roles in cellular recognition and regulation. And they are also valuable in medicine and pharmacy. Tubeworm is the representative species around the hydrothermal vent in the deep sea. They have developed unique mechanisms to adapt to the harsh environment. In this study, a 1 092 bp cDNA, designed as rpgal, was first cloned and characterized from the tubeworm Ridgeia piscesae. Sequence analysis showed that RPGAL had low homology with the known galectin. And it had two homologous carbohydrate-recognition domains, which is the characteristic of the tandem-repeat type galectins. The RPGAL was successfully recombinant expressed in Escherichia col and purified. Analysis of biological activity revealed that RPGAL was metal ion independent and it could agglutinate all the vertebrate erythrocytes tested. It was stable at 10-50℃ and pH 5-10. And the hemagglutinating activity of RPGAL was strongly inhibited by D-Lactose and lipopolysaccharide. Although RPGAL had no effect on the microorganisms tested, it showed anti-tumor activity towards HeLa cells and HT1080 cells, which was accomplished by apoptosis. The study demonstrated that RPGAL was a novel galectin and provided a potential candidate for therapy of anti-tumor.
中文摘要:
      凝集素是一类能够特异性地识别糖苷结构并与之结合的蛋白质或糖蛋白,其不仅在细胞识别与调控中发挥着重要的生理功能,而且在医药等多个领域具有广泛的应用价值。管状蠕虫是深海热液区的典型生物,其独特的生理特征使其能够应对深海热液区的极端环境。本研究对管状蠕虫Ridgeia piscesae的半乳糖凝集素RPGAL进行了克隆与功能研究。RPGAL编码基因长1092 bp,与已知的半乳糖凝集素的同源性较低,具有串联重复型半乳糖凝集素的典型特征,含有两个同源的糖识别结构域。通过利用大肠杆菌原核表达系统,RPGAL成功地进行了重组表达与纯化。生物活性分析表明RPGAL对所测试的脊椎动物血细胞均具有凝集效应,并且为金属非依赖型,其在温度10-50℃,pH5-10范围内均比较稳定,而其对血细胞的凝集活性可以被D-乳糖和脂多糖强烈抑制。此外,RPGAL对所测试的微生物没有凝集效应,但具有抗肿瘤活性,可促进Hela和HT1080的细胞凋亡。本研究表明RPGAL是一种新的半乳糖凝集素,其在抗肿瘤方面具有潜在的应用价值
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