七鳃鳗水通道蛋白3的克隆与生物学特性分析

doi:10.13560/j.cnki.biotech.bull.1985.2016.03.021

生物技术通报 ›› 2016, Vol. 32 ›› Issue (3): 129-136.doi: 10.13560/j.cnki.biotech.bull.1985.2016.03.021

七鳃鳗水通道蛋白3的克隆与生物学特性分析

赵春晖^1,2,史金杰¹,王浩²,刘欣²,李庆伟²

1.辽宁师范大学生命科学学院, 辽宁省生物技术与分子药物研发重点实验室大连 116081；2.辽宁师范大学七鳃鳗研究中心, 大连 116081

收稿日期:2015-06-23 出版日期:2016-03-24 发布日期:2016-03-25
作者简介:赵春晖, 女, 副教授, 硕士生导师, 研究方向：细胞生物学与蛋白质工程；E-mail：zch@lnnu.edu.cn
基金资助:
国家自然科学基金项目(31170353)

Cloning and Biological Characterization of Aquaporin 3 from Lampetra japonica

ZHAO Chun-hui^{1, 2}, SHI Jin-jie¹, WANG Hao², LIU Xin², LI Qing-wei²

1. Liaoning Provincial Key Laboratory of Biotechnology and Drug Discovery, College of Life Sciences, Liaoning Normal University, Dalian 116081；
2. Lamprey Research Center, Liaoning Normal University, Dalian 116081

Received:2015-06-23 Published:2016-03-24 Online:2016-03-25

摘要/Abstract

摘要： 水通道蛋白3(aquaporin 3, AQP3)属于水甘油通道蛋白家族, 参与水、尿素和甘油的转运和促进细胞增殖及迁移。从七鳃鳗中克隆得到了Aqp3(LjAqp3)cDNA(GenBank 序列号KR054618), 其开放阅读框为900 bp, 编码299个氨基酸, 含6个跨膜螺旋结构域, 有信号肽。序列分析结果表明, 七鳃鳗AQP3有2个高度保守的天冬酰胺-脯氨酸-丙氨酸(NPA)模体和1个芳香族/精氨酸(ar/R)结构。进行同源序列比对发现与其它物种具有较高的同源性。实时荧光定量PCR分析表明, LjAqp3在七鳃鳗中分布广泛, 在多种组织器官中表达。

关键词: 水通道蛋白3, 七鳃鳗, 天冬酰胺-脯氨酸-丙氨酸模体

Abstract: Aquaporin 3(AQP3)belongs to the family of aquaglyceroporin, and it involves in the transport of water, urea and glycerol and promotes cell proliferation and migration. In this study, the complete cDNA sequence of Aqp3(designated as LjAqp3)was cloned from Arctic lamprey Lampetra japonica(GenBank accession number KR054618). The open reading frame of LjAqp3 was 900 bp, encoding 299 amino acids, with a predicted 6 transmembrane helix domains and a putative signal peptide. There were 2 highly conserved asparagine-proline-alanine(NPA)motifs and the aromatic/arginine(ar/R)structure in LjAQP3. Additionally, LjAQP3 shared high sequence homology with AQP3 of other species. Real-time quantitative PCR revealed the constitutive expression of LjAqp3 in multiple tissues and organs.

Key words: aquaporin 3, Lampetra japonica, asparagine-proline-alanine motif

赵春晖,史金杰,王浩,刘欣,李庆伟. 七鳃鳗水通道蛋白3的克隆与生物学特性分析[J]. 生物技术通报, 2016, 32(3): 129-136.

ZHAO Chun-hui, SHI Jin-jie, WANG Hao, LIU Xin, LI Qing-wei. Cloning and Biological Characterization of Aquaporin 3 from Lampetra japonica[J]. Biotechnology Bulletin, 2016, 32(3): 129-136.

参考文献

[1]Fujiyoshi Y, Mitsuoka K, de Groot BL, et al. Structure and function of water channels[J]. Curr Opin Struct Biol, 2002, 12(4)：509-515.
[2]Chauvigné F, Lubzens E, Cerdà J. Design and characterization of genetically engineered zebrafish aquaporin-3 mutants highly permeable to the cryoprotectant ethylene glycol[J]. BMC Biotechnol, 2011, 11：34.
[3]Abascal F, Irisarri I, Zardoya R. Diversity and evolution of membrane intrinsic proteins[J]. Biochim Biophys Acta, 2014, 1840(5)：1468-1481.
[4]王芳, 董乐, 戴聪杰, 等. 甘草质膜水通道蛋白GuPIPl对甘油的转运[J]. 生物技术通报, 2011(5)：172-177.
[5]Zhu C, Jiang Z, Bazer FW, et al. Aquaporins in the female reproductive system of mammals[J]. Front Biosci(Landmark Ed), 2015, 20：838-871.
[6]Cutler CP, Martinez AS, Cramb G. The role of aquaporin 3 in teleost fish[J]. Comp Biochem Physiol A Mol Integr Physiol, 2007, 148(1)：82-91.
[7]苏维恒. 水通道蛋白的结构与功能研究[D]. 长春：东北师范大学, 2013：1-8.
[8]Tingaud-Sequeira A, Calusinska M, Finn RN, et al. The zebrafish genome encodes the largest vertebrate repertoire of functional aquaporins with dual paralogy and substrate specificities similar to mammals[J]. BMC Evol Biol, 2010, 10：38.
[9]陈利琼, 朱雪琼. 水通道蛋白3的研究进展[J]. 医学研究杂志, 2012, 41(6)：8-10.
[10] 熊正方, 刘慧妹. 水通道蛋白3功能的研究动态[J]. 中华生物医学工程杂志, 2008, 14(5)：391-393.
[11]Guo L, Chen H, Li Y, et al. An aquaporin 3-notch1 axis in keratinocyte differentiation and inflammation[J]. PLoS One, 2013, 8(11)：e80179.
[12]Chen J, Wang Z, Xu D, et al. Aquaporin 3 promotes prostate cancer cell motility and invasion via extracellular signal-regulated kinase 1/2-mediated matrix metalloproteinase-3 secretion[J]. Mol Med Rep, 2015, 11(4)：2882-2888.
[13]Jung D, Adamo MA, Lehman RM, et al. A novel variant of aquaporin 3 is expressed in killifish(Fundulus heteroclitus)intestine[J]. Comp Biochem Physiol C Toxicol Pharmacol, 2015, 171：1-7.
[14]Hirata T, Kaneko T, Ono T, et al. Mechanism of acid adaptation of a fish living in a pH 3. 5 lake[J]. Am J Physiol Regul Integr Comp Physiol, 2003, 284(5)：R1199-R2212.
[15]Cutler CP, Cramb G. Branchial expression of an aquaporin 3(AQP-3)homologue is downregulated in the European eel Anguilla anguilla following seawater acclimation[J]. J Exp Biol, 2002, 205(Pt 17)：2643-2651.
[16]Watanabe S, Kaneko T, Aida K. Aquaporin-3 expressed in the basolateral membrane of gill chloride cells in Mozambique tilapia Oreochromis mossambicus adapted to freshwater and seawater[J]. J Exp Biol, 2005, 208(Pt 14)：2673-2682.
[17]甘远迪, 赵金良, Jeerawat Thammaratsuntorn, 等. 萨罗罗非鱼AQP3 cDNA序列克隆及盐度胁迫下组织表达特征[J]. 动物学杂志, 2014, 49(4)：560-569.
[18]Amemiya CT, Saha NR, Zapata A. Evolution and development of immunological structures in the lamprey[J]. Curr Opin Immunol, 2007, 19(5)：535-541.
[19]Wu F, Zhao J, Chen L, et al. A novel BTK-like protein involved in immune response in Lethenteron japonicum[J]. Immunol Lett, 2012, 146(1-2)：57-63.
[20]Arocho A, Chen B, Ladanyi M, et al. Validation of the 2- DeltaDeltaCt calculation as an alternate method of data analysis for quantitative PCR of BCR-ABL P210 transcripts[J]. Diagn Mol Pathol, 2006, 15(1)：56-61.
[21]Pancer Z, Amemiya CT, Ehrhardt GR, et al. Somatic diversi-fication of variable lymphocyte receptors in the agnathan sea lamprey[J]. Nature, 2004, 430(6996)：174-180.
[22]Ishibashi K. Aquaporin subfamily with unusual NPA boxes[J]. Biochim Biophys Acta, 2006, 1758(8)：989-993.
[23]Verma RK, Prabh ND, Sankararamakrishnan R. Intra-helical salt-bridge and helix destabilizing residues within the same helical turn：Role of functionally important loop E half-helix in channel regulation of major intrinsic proteins[J]. Biochim Biophys Acta, 2015, 1848(6)：1436-1449.

七鳃鳗水通道蛋白3的克隆与生物学特性分析

Cloning and Biological Characterization of Aquaporin 3 from Lampetra japonica

PDF (PC)

可视化

摘要/Abstract

引用本文

使用本文

参考文献

相关文章 0

编辑推荐

Metrics

本文评价