Volume 14 Issue 4
Jul.  2018
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ZHAO Chaoping, GUO Huayang, ZHANG Jian, ZHU Kecheng, GUO Liang, ZHANG Nan, LIU Baosuo, YANG Jingwen, ZHANG Dianchang. Molecular characteristics and expression analysis of AQP1a from Trachinotus ovatus under acute salinity stress[J]. South China Fisheries Science, 2018, 14(4): 56-65. DOI: 10.3969/j.issn.2095-0780.2018.04.007
Citation: ZHAO Chaoping, GUO Huayang, ZHANG Jian, ZHU Kecheng, GUO Liang, ZHANG Nan, LIU Baosuo, YANG Jingwen, ZHANG Dianchang. Molecular characteristics and expression analysis of AQP1a from Trachinotus ovatus under acute salinity stress[J]. South China Fisheries Science, 2018, 14(4): 56-65. DOI: 10.3969/j.issn.2095-0780.2018.04.007
shu

Molecular characteristics and expression analysis of AQP1a from Trachinotus ovatus under acute salinity stress

  • 1.

    Key Laboratory of South China Sea Fishery Resources Exploitation & Utilization, Ministry of Agriculture; South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China

  • 2.

    College of Fisheries and Life Science, Shanghai Ocean University, Shanghai 200090, China

  • 3.

    Guangdong Provincial Engineer Technology Research Center of Marine Biological Seed Industry, Guangzhou 510300, China

  • 4.

    Guangdong Haid Group Co., Ltd., Guangzhou 511140, China

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  • Received Date: March 04, 2018
  • Revised Date: March 28, 2018
  • Available Online: December 04, 2018
    Graphical Abstract
    • Abstract
  • Aquaporin, a superfamily of internal membrane proteins that mediate transmembrane transport of water molecules, plays an important role in osmotic adjustment. AQP1a gene was obtained in order to study the role of AQP1a in osmoregulation of Trachinotus ovatus under acute salinity stress. The sequence of AQP1a gene was 1 078 bp with an open reading frame of 786 bp encoding 261 amino acids. The structural analysis shows that it has the structural characteristics of MIP family-specific sequence (HINPAVTLG) and two asparagine-proline-alanine (NPA) motifs. The qRT-PCR results show that AQP1a was distributed in the 11 tested tissues, highest in gonads and then in gill, intestine and liver, lowest in muscle. Under acute salinity stress, after being transfered to fresh water, the expression of AQP1a in gill increased at 4th hour, while there was no significant change in the expression in kidney and intestine. After being transfered to 10‰ and 20‰ salinity seawater, the expression of AQP1a in gill increased significantly at 2nd and 4th hour, and then decreased gradually. When being transferred to 10‰ salinity seawater, the expression of AQP1a in intestine increased. In kidney, the expression of AQP1a first increased and then decreased. When being transferred to 20‰ salinity seawater, the expression of AQP1a in intestine only increased significantly at 4th, 8th and 48th hour. In kidney, the expression of AQP1a reached the maximum at 12th hour. In 40‰ salinity seawater, the expression of AQP1a in gill decreased significantly. On the contrary, the expression of AQP1a in kidney and intestine were significantly up-regulated. The results reveal that the specificity of AQP1a functions in different tissues and plays an important role in T.ovatus salinity adaptation.
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    • References (31)
  • [1]
    AN K W, KIM N N, CHOI C Y. Cloning and expression of aquaporin 1 and arginine vasotocin receptor mRNA from the black porgy, Acanthopagrus schlegeli: effect of freshwater acclimation[J]. Fish Physiol Biochem, 2008, 34(2): 185-194.
    [2]
    CHNG Y R, ONG J L, CHING B, et al. Molecular characterization of aquaporin 1 and aquaporin 3 from the gills of the African lungfish, Protopterus annectens, and changes in their branchial mRNA expression levels and protein abundance during three phases of aestivation[J]. Front Physiol, 2016, 7: 532.
    [3]
    ABASCAL F, IRISARRI I, ZARDOYA R. Diversity and evolution of membrane intrinsic proteins[J]. Biochim Biophys Acta, 2014, 1840(5): 1468-1481.
    [4]
    FINN R N, CERDÀ J. Evolution and functional diversity of aquaporins[J]. Biol Bull, 2015, 229(1): 6-23.
    [5]
    AGRE P, SASAKI S, CHRISPEELS M J. Aquaporins: a family of water channel proteins[J]. Am J Physiol, 1993, 265(3 Pt 2): F461.
    [6]
    TINGAUD-SEQUEIRA A, CHAUVIGNÉ F, FABRA M, et al. Structural and functional divergence of two fish aquaporin-1 water channels following teleost-specific gene duplication[J]. BMC Evol Biol, 2008, 8(1): 259.
    [7]
    CHEN L M, ZHAO J, MUSA-AZIZ R, et al. Cloning and characterization of a zebrafish homologue of human AQP1: a bifunctional water and gas channel[J]. Am J Physiol Regul Integr Comp Physiol, 2010, 299(5): R1163-R1174.
    [8]
    DEANE E E, LUK J C Y, WOO N Y S. Aquaporin 1a expression in gill, intestine, and kidney of the euryhaline silver sea bream[J]. Front Physiol, 2011, 2: 39.
    [9]
    GUO H, WEI M, LIU Y, et al. Molecular cloning and expression analysis of the aqp1aa gene in half-smooth tongue sole (Cynoglossus semilaevis)[J]. PLoS One, 2017, 12(4): e175033.
    [10]
    TIPSMARK C K, SØRENSEN K J, MADSEN S S. Aquaporin expression dynamics in osmoregulatory tissues of Atlantic salmon during smoltification and seawater acclimation[J]. J Exp Biol, 2010, 213(3): 368-379.
    [11]
    MARTINEZ A S, CUTLER C P, WILSON G D, et al. Regulation of expression of two aquaporin homologs in the intestine of the European eel: effects of seawater acclimation and cortisol treatment[J]. Am J Physiol Regul Integr Comp Physiol, 2005, 288(6): R1733-R1743.
    [12]
    JEONG S Y, KIM J H, LEE W O, et al. Salinity changes in the anadromous river pufferfish, Takifugu obscurus, mediate gene regulation[J]. Fish Physiol Biochem, 2014, 40(1): 205-219.
    [13]
    KIM Y K, LEE S Y, KIM B S, et al. Isolation and mRNA expression analysis of aquaporin isoforms in marine medaka Oryzias dancena, a euryhaline teleost[J]. Comp Biochem Physiol A, 2014, 171(5): 1-8.
    [14]
    IP Y K, SOH M M, CHEN X L, et al. Molecular characterization of branchial aquaporin 1aa and effects of seawater acclimation, emersion or ammonia exposure on its mRNA expression in the gills, gut, kidney and skin of the freshwater climbing perch, Anabas testudineus[J]. PLoS One, 2013, 8(4): e61163.
    [15]
    GIFFARD-MENA I, BOULO V, AUJOULAT F, et al. Aquaporin molecular characterization in the sea-bass (Dicentrarchus labrax): the effect of salinity on AQP1 and AQP3 expression[J]. Comp Biochem Physiol A, 2007, 148(2): 430-444.
    [16]
    于文博, 朱克诚, 郭华阳, 等. 卵形鲳鲹MHCⅡβ基因的克隆与表达分析[J]. 南方水产科学, 2017, 13(4): 69-79.
    [17]
    GEYER R R, MUSA-AZIZ R, QIN X, et al. Relative CO(2)/NH(3) selectivity's of mammalian aquaporins 0-9[J]. Am J Physiol Cell Physiol, 2013, 304(10): C985-C994.
    [18]
    FINN R N, CHAUVIGNÉ F, HLIDBERG J B, et al. The lineage-specific evolution of aquaporin gene clusters facilitated tetrapod terrestrial adaptation[J]. PLoS One, 2014, 9(11): e113686.
    [19]
    KONG Y, MA J. Dynamic mechanisms of the membrane water channel aquaporin-1(AQP1)[J]. Proc Natl Acad Sci USA, 2001, 98(25): 14345-14349.
    [20]
    FUJIYOSHI Y, MITSUOKA K, de GROOT B L, et al. Structure and function of water channels[J]. Curr Opin Struct Biol, 2002, 12(4): 509-515.
    [21]
    De GROOT B L, GRUBMÜLLER H. Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF[J]. Science, 2001, 294(5550): 2353-2357.
    [22]
    BEITZ E, WU B, HOLM L M, et al. Point mutations in the aromatic/arginine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons[J]. Proc Natl Acad Sci USA, 2006, 103(2): 269-274.
    [23]
    姜勇, 麻彤辉. NPA motif在水通道蛋白AQP1表达和转水功能中的重要性[J]. 科学通报, 2007, 52(4): 426-431.
    [24]
    WALZ T, HIRAI T, MURATA K, et al. The three-dimensional structure of aquaporin-1[J]. Nature, 1997, 387(6633): 624-627.
    [25]
    丁炜东. 黄鳝性别分化相关候选基因的筛选及相关功能研究[D]. 南京: 南京农业大学, 2016: 76-83
    [26]
    姚小皓, 李学军. 水孔蛋白1的结构与功能[J]. 生理科学进展, 2000, 31(4): 345-348.
    [27]
    BOJ M, CHAUVIGNÃ F, ZAPATER C, et al. Gonadotropin-activated androgen-dependent and independent pathways regulate aquaporin expression during teleost (Sparus aurata) spermatogenesis[J]. PLoS One, 2015, 10(11): e0142512.
    [28]
    AOKI M, KANEKO T, KATOH F, et al. Intestinal water absorption through aquaporin 1 expressed in the apical membrane of mucosal epithelial cells in seawater-adapted Japanese eel[J]. J Exp Biol, 2003, 206(19): 3495-3505.
    [29]
    丁炜东, 曹丽萍, 曹哲明, 等. 黄鳝AQP1 cDNA的克隆与表达分析[J]. 华北农学报, 2012, 27(S1): 6-11.
    [30]
    SANG Y L, NAM Y K, YI K K. Characterization and expression profiles of aquaporins (AQPs) 1a and 3a in mud loach Misgurnus mizolepis after experimental challenges[J]. Fish Aquat Sci, 2017, 20(1): 23.
    [31]
    王美垚, 杨健, 徐跑, 等. 刀鲚水通道蛋白1的分子克隆及高盐作用下的表达分析[J]. 中国水产科学, 2017, 24(3): 449-458.
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