Na^＋/K^＋-ATPase α-subunit in swimming crab Portunus trituberculatus： molecular cloning, characterization, and expression under low salinity stress
Na^＋/K^＋-ATPases are membrane-associated enzymes responsible for the active transport of Na^＋ and K^＋ ions across cell membranes, generating chemical and electrical gradients. These enzymes＇ α-subunit provides catalytic function, binding and hydrolyzing ATP, and itself becoming phosphorylated during...
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| Published in | Chinese journal of oceanology and limnology Vol. 33; no. 4; pp. 828 - 837 |
|---|---|
| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
Heidelberg
Science Press
01.07.2015
Springer Nature B.V |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Na^＋/K^＋-ATPases are membrane-associated enzymes responsible for the active transport of Na^＋ and K^＋ ions across cell membranes, generating chemical and electrical gradients. These enzymes＇ α-subunit provides catalytic function, binding and hydrolyzing ATP, and itself becoming phosphorylated during the transport cycle. In this study, Na^＋/K^＋-ATPase α-subunit eDNA was cloned from gill tissue of the swimming crab Portunus trituberculatus by reverse-transcription polymerase chain reaction （RT-PCR） and rapid amplification of eDNA end methods. Analysis of the nucleotide sequence revealed that the eDNA had a full-length of 3 833 base pairs （bp）, with an open reading frame of 3 120 bp, 5＇ untranslated region （UTR） of 317 bp, and 3＇ UTR of 396 bp. The sequence encoded a 1 039 amino acid protein with a predicted molecular weight of 115.57 kDa and with estimated pI of 5.21. It was predicted here to possess all expected features of Na^＋/K^＋-ATPase members, including eight transmembrane domains, putative ATP-binding site, and phosphorylation site. Comparison of arnino acid sequences showed that the P. tritubereulatus α-subunit possessed an overall identity of 75%-99% to that of other organisms. Phylogenetic analysis revealed that this α-subunit was in the same category as those of crustaceans. Quantitative real-time RT-PCR analysis indicated that this α-subunit＇s transcript were most highly expressed in gill and lowest in muscle. RT-PCR analysis also revealed that α-subunit expression in crab gill decreased after 2 and 6 h, but increased after 12, 24, 48, and 72 h. In addition, α-subunit expression in hepatopancreas of crab decreased after 2-72 h. These facts indicated that the crab＇s Na^＋/K^＋-ATPase α-subunit was potentially involved in the observed acute response to low salinity stress. |
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| AbstractList | Na+/K+-ATPases are membrane-associated enzymes responsible for the active transport of Na+ and K+ ions across cell membranes, generating chemical and electrical gradients. These enzymes’ α-subunit provides catalytic function, binding and hydrolyzing ATP, and itself becoming phosphorylated during the transport cycle. In this study, Na+/K+-ATPase α-subunit cDNA was cloned from gill tissue of the swimming crab Portunus trituberculatus by reverse-transcription polymerase chain reaction (RT-PCR) and rapid amplification of cDNA end methods. Analysis of the nucleotide sequence revealed that the cDNA had a full-length of 3 833 base pairs (bp), with an open reading frame of 3 120 bp, 5′ untranslated region (UTR) of 317 bp, and 3′ UTR of 396 bp. The sequence encoded a 1 039 amino acid protein with a predicted molecular weight of 115.57 kDa and with estimated pI of 5.21. It was predicted here to possess all expected features of Na+/K+-ATPase members, including eight transmembrane domains, putative ATP-binding site, and phosphorylation site. Comparison of amino acid sequences showed that the P. trituberculatus α-subunit possessed an overall identity of 75%–99% to that of other organisms. Phylogenetic analysis revealed that this α-subunit was in the same category as those of crustaceans. Quantitative real-time RT-PCR analysis indicated that this α-subunit’s transcript were most highly expressed in gill and lowest in muscle. RT-PCR analysis also revealed that α-subunit expression in crab gill decreased after 2 and 6 h, but increased after 12, 24, 48, and 72 h. In addition, α-subunit expression in hepatopancreas of crab decreased after 2-72 h. These facts indicated that the crab’s Na+/K+-ATPase α-subunit was potentially involved in the observed acute response to low salinity stress. Na + /K + -ATPases are membrane-associated enzymes responsible for the active transport of Na + and K + ions across cell membranes, generating chemical and electrical gradients. These enzymes’ α-subunit provides catalytic function, binding and hydrolyzing ATP, and itself becoming phosphorylated during the transport cycle. In this study, Na + /K + -ATPase α-subunit cDNA was cloned from gill tissue of the swimming crab Portunus trituberculatus by reverse-transcription polymerase chain reaction (RT-PCR) and rapid amplification of cDNA end methods. Analysis of the nucleotide sequence revealed that the cDNA had a full-length of 3 833 base pairs (bp), with an open reading frame of 3 120 bp, 5′ untranslated region (UTR) of 317 bp, and 3′ UTR of 396 bp. The sequence encoded a 1 039 amino acid protein with a predicted molecular weight of 115.57 kDa and with estimated pI of 5.21. It was predicted here to possess all expected features of Na + /K + -ATPase members, including eight transmembrane domains, putative ATP-binding site, and phosphorylation site. Comparison of amino acid sequences showed that the P. trituberculatus α-subunit possessed an overall identity of 75%–99% to that of other organisms. Phylogenetic analysis revealed that this α-subunit was in the same category as those of crustaceans. Quantitative real-time RT-PCR analysis indicated that this α-subunit’s transcript were most highly expressed in gill and lowest in muscle. RT-PCR analysis also revealed that α-subunit expression in crab gill decreased after 2 and 6 h, but increased after 12, 24, 48, and 72 h. In addition, α-subunit expression in hepatopancreas of crab decreased after 2-72 h. These facts indicated that the crab’s Na + /K + -ATPase α-subunit was potentially involved in the observed acute response to low salinity stress. Na⁺/K⁺-ATPases are membrane-associated enzymes responsible for the active transport of Na⁺ and K⁺ ions across cell membranes, generating chemical and electrical gradients. These enzymes’ α-subunit provides catalytic function, binding and hydrolyzing ATP, and itself becoming phosphorylated during the transport cycle. In this study, Na⁺/K⁺-ATPase α-subunit cDNA was cloned from gill tissue of the swimming crab Portunus trituberculatus by reverse-transcription polymerase chain reaction (RT-PCR) and rapid amplification of cDNA end methods. Analysis of the nucleotide sequence revealed that the cDNA had a full-length of 3 833 base pairs (bp), with an open reading frame of 3 120 bp, 5′ untranslated region (UTR) of 317 bp, and 3′ UTR of 396 bp. The sequence encoded a 1 039 amino acid protein with a predicted molecular weight of 115.57 kDa and with estimated pI of 5.21. It was predicted here to possess all expected features of Na⁺/K⁺-ATPase members, including eight transmembrane domains, putative ATP-binding site, and phosphorylation site. Comparison of amino acid sequences showed that the P. trituberculatus α-subunit possessed an overall identity of 75%–99% to that of other organisms. Phylogenetic analysis revealed that this α-subunit was in the same category as those of crustaceans. Quantitative real-time RT-PCR analysis indicated that this α-subunit’s transcript were most highly expressed in gill and lowest in muscle. RT-PCR analysis also revealed that α-subunit expression in crab gill decreased after 2 and 6 h, but increased after 12, 24, 48, and 72 h. In addition, α-subunit expression in hepatopancreas of crab decreased after 2-72 h. These facts indicated that the crab’s Na⁺/K⁺-ATPase α-subunit was potentially involved in the observed acute response to low salinity stress. Na^＋/K^＋-ATPases are membrane-associated enzymes responsible for the active transport of Na^＋ and K^＋ ions across cell membranes, generating chemical and electrical gradients. These enzymes＇ α-subunit provides catalytic function, binding and hydrolyzing ATP, and itself becoming phosphorylated during the transport cycle. In this study, Na^＋/K^＋-ATPase α-subunit eDNA was cloned from gill tissue of the swimming crab Portunus trituberculatus by reverse-transcription polymerase chain reaction （RT-PCR） and rapid amplification of eDNA end methods. Analysis of the nucleotide sequence revealed that the eDNA had a full-length of 3 833 base pairs （bp）, with an open reading frame of 3 120 bp, 5＇ untranslated region （UTR） of 317 bp, and 3＇ UTR of 396 bp. The sequence encoded a 1 039 amino acid protein with a predicted molecular weight of 115.57 kDa and with estimated pI of 5.21. It was predicted here to possess all expected features of Na^＋/K^＋-ATPase members, including eight transmembrane domains, putative ATP-binding site, and phosphorylation site. Comparison of arnino acid sequences showed that the P. tritubereulatus α-subunit possessed an overall identity of 75%-99% to that of other organisms. Phylogenetic analysis revealed that this α-subunit was in the same category as those of crustaceans. Quantitative real-time RT-PCR analysis indicated that this α-subunit＇s transcript were most highly expressed in gill and lowest in muscle. RT-PCR analysis also revealed that α-subunit expression in crab gill decreased after 2 and 6 h, but increased after 12, 24, 48, and 72 h. In addition, α-subunit expression in hepatopancreas of crab decreased after 2-72 h. These facts indicated that the crab＇s Na^＋/K^＋-ATPase α-subunit was potentially involved in the observed acute response to low salinity stress. |
| Author | Duan, Yafei Xu, Wenfei Chen, Ping Wang, Haofeng Han, Xiaolin Gao, Baoquan Liu, Ping |
| AuthorAffiliation | Key Laboratory of Sustainable Development of Marine Fisheries, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China Dalian Ocean University, Dalian 116023, China |
| Author_xml | – sequence: 1 fullname: 韩晓琳 刘萍 高保全 王好锋 段亚飞 徐文斐 陈萍 |
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| CitedBy_id | crossref_primary_10_1016_j_cbd_2023_101166 crossref_primary_10_1071_ZO16048 crossref_primary_10_1007_s12192_016_0707_3 crossref_primary_10_1007_s11802_022_4880_y crossref_primary_10_1007_s13258_019_00828_4 crossref_primary_10_1016_j_ijbiomac_2019_02_098 crossref_primary_10_1016_j_aqrep_2024_102541 crossref_primary_10_1016_j_heliyon_2024_e25556 crossref_primary_10_7717_peerj_3623 |
| Cites_doi | 10.1016/j.fsi.2010.04.011 10.2108/zsj.13.833 10.1146/annurev.ph.53.030191.003025 10.1242/jeb.004309 10.1083/jcb.133.6.1193 10.1080/17451000.2010.538063 10.2108/zsj.25.205 10.1016/0014-5793(89)81816-2 10.3724/SP.J.1231.2012.27770 10.1016/j.molbiopara.2004.07.009 10.2144/05391RV01 10.1016/S1095-6433(03)00064-3 10.1007/s10126-002-0031-z 10.1016/S0005-2728(98)00041-3 10.1038/316691a0 10.1016/0300-9629(95)02076-4 10.2307/1549010 10.1002/jez.1402650408 10.1016/0305-0491(95)00037-9 10.1242/jeb.002873 10.1016/0145-305X(88)90071-7 10.1016/j.cbpb.2007.08.009 10.1093/molbev/msm092 10.1093/nar/22.22.4673 10.1016/S0022-0981(96)02778-5 10.1007/BF00175496 10.1016/j.aquaculture.2010.03.025 10.1093/emboj/16.14.4250 10.1007/BF01869450 10.1006/meth.2001.1262 10.1016/S0022-2836(05)80360-2 10.1016/j.bbrc.2005.04.038 10.1007/BF01870942 10.1007/PL00006286 10.1038/321429a0 10.1242/jeb.204.22.4005 10.1016/0304-4157(88)90017-2 10.1016/S0021-9258(17)32067-7 10.1093/icb/37.6.575 |
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| Keywords | salinity expression Na ATPase α-subunit K cloning |
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| Notes | HAN Xiaolin, LIU Ping , GAO Baoquan,WANG Haofeng , DUAN Yafei , XU Wenfei, CHEN Ping （1 Key Laboratory of Sustainable Development of Marine Fisheries, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China; 2 Dalian Ocean University, Dalian 116023, China） 37-1150/P cloning; expression; Na^＋/K^＋-ATPase; α-subunit; Portunus trituberculatus; salinity Na^＋/K^＋-ATPases are membrane-associated enzymes responsible for the active transport of Na^＋ and K^＋ ions across cell membranes, generating chemical and electrical gradients. These enzymes＇ α-subunit provides catalytic function, binding and hydrolyzing ATP, and itself becoming phosphorylated during the transport cycle. In this study, Na^＋/K^＋-ATPase α-subunit eDNA was cloned from gill tissue of the swimming crab Portunus trituberculatus by reverse-transcription polymerase chain reaction （RT-PCR） and rapid amplification of eDNA end methods. Analysis of the nucleotide sequence revealed that the eDNA had a full-length of 3 833 base pairs （bp）, with an open reading frame of 3 120 bp, 5＇ untranslated region （UTR） of 317 bp, and 3＇ UTR of 396 bp. The sequence encoded a 1 039 amino acid protein with a predicted molecular weight of 115.57 kDa and with estimated pI of 5.21. It was predicted here to possess all expected features of Na^＋/K^＋-ATPase members, including eight transmembrane domains, putative ATP-binding site, and phosphorylation site. Comparison of arnino acid sequences showed that the P. tritubereulatus α-subunit possessed an overall identity of 75%-99% to that of other organisms. Phylogenetic analysis revealed that this α-subunit was in the same category as those of crustaceans. Quantitative real-time RT-PCR analysis indicated that this α-subunit＇s transcript were most highly expressed in gill and lowest in muscle. RT-PCR analysis also revealed that α-subunit expression in crab gill decreased after 2 and 6 h, but increased after 12, 24, 48, and 72 h. In addition, α-subunit expression in hepatopancreas of crab decreased after 2-72 h. These facts indicated that the crab＇s Na^＋/K^＋-ATPase α-subunit was potentially involved in the observed acute response to low salinity stress. http://dx.doi.org/10.1007/s00343-015-4018-9 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
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| PublicationTitle | Chinese journal of oceanology and limnology |
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| References | Wong, Medrano (CR47) 2005; 39 Pan, Yue, Miao, Zhang, Li (CR31) 2010; 29 Péqueux (CR32) 1995; 15 Béguin, Wang, Firsov, Puoti, Claeys, Horisberger, Geering (CR5) 1997; 16 Jiang, Xu (CR19) 2011; 35 Semple, Green, Schulte (CR33) 2002; 4 Towle (CR43) 1993; 265 Serrano (CR34) 1988; 947 Deane, Woo (CR10) 2005; 331 Horisberger, Lemas, Kraehenbuhl, Rossier (CR16) 1991; 53 Geering (CR13) 1990; 115 Kinne, Kinne (CR21) 1971 Axelsen, Palmgren (CR2) 1998; 46 Thompson, Higgins, Gibson (CR40) 1994; 22 Sun, Zhang, Ren, Chen, Fan, Xia, Lin, Hu (CR37) 2011; 7 Nilsen, Ebbesson, Madsen, McCormick, Andersson, Björnsson, Prunet, Stefansson (CR29) 2007; 210 Lingrel, Kuntzweiler (CR22) 1994; 269 Mitsunaga-Nakatsubo, Yamazaki, Hatoh-Okazaki, Kawashita, Okamura, Akasaka, Shimada, Yasumasu (CR28) 1996; 13 Altschul, Gish, Miller, Myers, Lipman (CR1) 1990; 215 Corotto, Holliday (CR8) 1996; 113A Huong, Jasmani, Jayasankar, Wilder (CR17) 2010; 304 Liu, Liu (CR23) 2008 Lu, Wang, Zhao, Dong, Ma (CR25) 2012; 19 Towle, Kinne (CR42) 1990 Shull, Lane, Lingrel (CR35) 1986; 321 Fagan, Saier (CR11) 1994; 38 Tamura, Dudley, Nei, Kumar (CR38) 2007; 24 Jørgensen, Andersen (CR20) 1988; 103 Towle (CR41) 1981; 2 Baxter-Lowe, Guo, Bergstrom, Hokin (CR4) 1989; 257 Choi, An (CR6) 2008; 149 Livak, Schmittgen (CR24) 2001; 25 Willms, Shoemaker, Skelly, Landa (CR46) 2004; 138 Towle, Paulsen, Weihrauch, Kordylewski, Salvador, Lignot, Spanings-Pierrot (CR45) 2001; 204 Shull, Schwartz, Lingrel (CR36) 1985; 316 Geering, Beggah, Good, Girardet, Roy, Schaer, Jaunin (CR14) 1996; 133 Towle (CR44) 1997; 37 Cutler, Sanders, Hazon, Cramb (CR9) 1995; 111 Mercer (CR27) 1993; 137C Palmgren, Axelsen (CR30) 1998; 1365 Lucu, Towle (CR26) 2003; 135 Bachère, Chagot, Grizel (CR3) 1988; 12 Harasywych, Adamkewicz, Blake, Suadek, Spriggs, Bolt (CR15) 1997; 6 Tang, Chang, Chen, Lee, Hwang (CR39) 2008; 25 Feng, Zhao, Zhuang, Zhang (CR12) 2012; 36 Cooper, Morris (CR7) 1997; 214 Jayasundara, Towle, Weihrauch, Spanings-Pierrot (CR18) 2007; 210 F S Corotto (4018_CR8) 1996; 113A K J Livak (4018_CR24) 2001; 25 Z S Liu (4018_CR23) 2008 R Serrano (4018_CR34) 1988; 947 D W Towle (4018_CR42) 1990 K Geering (4018_CR14) 1996; 133 K Willms (4018_CR46) 2004; 138 E E Deane (4018_CR10) 2005; 331 J D Horisberger (4018_CR16) 1991; 53 K Mitsunaga-Nakatsubo (4018_CR28) 1996; 13 S F Altschul (4018_CR1) 1990; 215 J D Thompson (4018_CR40) 1994; 22 R W Mercer (4018_CR27) 1993; 137C D W Towle (4018_CR43) 1993; 265 C Y Choi (4018_CR6) 2008; 149 N Jayasundara (4018_CR18) 2007; 210 G E Shull (4018_CR36) 1985; 316 P Béguin (4018_CR5) 1997; 16 J B Lingrel (4018_CR22) 1994; 269 O Kinne (4018_CR21) 1971 K B Axelsen (4018_CR2) 1998; 46 K Geering (4018_CR13) 1990; 115 D T T Huong (4018_CR17) 2010; 304 T O Nilsen (4018_CR29) 2007; 210 L A Baxter-Lowe (4018_CR4) 1989; 257 M G Harasywych (4018_CR15) 1997; 6 D W Towle (4018_CR41) 1981; 2 A R Cooper (4018_CR7) 1997; 214 D W Towle (4018_CR44) 1997; 37 C P Cutler (4018_CR9) 1995; 111 L Q Pan (4018_CR31) 2010; 29 A Péqueux (4018_CR32) 1995; 15 G E Shull (4018_CR35) 1986; 321 Y L Lu (4018_CR25) 2012; 19 D W Towle (4018_CR45) 2001; 204 M J Fagan (4018_CR11) 1994; 38 P L Jørgensen (4018_CR20) 1988; 103 M G Palmgren (4018_CR30) 1998; 1365 K Tamura (4018_CR38) 2007; 24 Lucu (4018_CR26) 2003; 135 C H Tang (4018_CR39) 2008; 25 J W Semple (4018_CR33) 2002; 4 S Y Feng (4018_CR12) 2012; 36 S Jiang (4018_CR19) 2011; 35 M Wong (4018_CR47) 2005; 39 E Bachère (4018_CR3) 1988; 12 H Y Sun (4018_CR37) 2011; 7 |
| References_xml | – volume: 29 start-page: 286 issue: 2 year: 2010 end-page: 292 ident: CR31 article-title: Molecular cloning and characterization of a novel c-type lysozyme gene in swimming crab publication-title: Fish. Shellfish Immunol. doi: 10.1016/j.fsi.2010.04.011 – volume: 13 start-page: 833 issue: 6 year: 1996 end-page: 841 ident: CR28 article-title: cDNA cloning of NA , K -ATPase α-subunit from embryos of the sea urchin, publication-title: Zool Sci. doi: 10.2108/zsj.13.833 – volume: 53 start-page: 565 issue: 1 year: 1991 end-page: 584 ident: CR16 article-title: Structure-function relationship of Na, K-ATPase publication-title: Annu. Rev. Physiol. doi: 10.1146/annurev.ph.53.030191.003025 – volume: 210 start-page: 2 070 issue: Pt12 year: 2007 end-page: 2 081 ident: CR18 article-title: Gill-specific transcriptional regulation of Na /K -ATPase α-subunit in the euryhaline shore crab : sequence variants and promoter structure publication-title: J. Exp. Biol. doi: 10.1242/jeb.004309 – volume: 133 start-page: 1 193 issue: 6 year: 1996 end-page: 1 204 ident: CR14 article-title: Oligomerization and maturation of Na, K-ATPase: functional interaction of the cytoplasmic NH 2 terminus of the beta subunit with the alpha subunit publication-title: J. Cell Biol. doi: 10.1083/jcb.133.6.1193 – volume: 7 start-page: 623 issue: 6 year: 2011 end-page: 628 ident: CR37 article-title: The expression of Na, K-ATPase in under salinity stress publication-title: Mar. Biol. Res. doi: 10.1080/17451000.2010.538063 – start-page: 241 year: 1990 end-page: 263 ident: CR42 article-title: Sodium transport systems in gills. In publication-title: Comparative Aspects of Sodium Cotransport Systems – volume: 25 start-page: 205 issue: 2 year: 2008 end-page: 211 ident: CR39 article-title: Phenotypic changes in mitochondrion-rich cells and responses of Na /K -ATPase in gills of tilapia exposed to deionized water publication-title: Zool Sci. doi: 10.2108/zsj.25.205 – volume: 257 start-page: 181 issue: 1 year: 1989 end-page: 187 ident: CR4 article-title: Molecular cloning of the Na, K-ATPase α-subunit in developing brine shrimp and sequence comparison with higher organisms publication-title: FEBS Lett. doi: 10.1016/0014-5793(89)81816-2 – volume: 36 start-page: 1 386 issue: 9 year: 2012 end-page: 1 391 ident: CR12 article-title: Preliminary studies on molecular mechanism of salinity regulation of Na , K -ATPase α-subunit in gills of juvenile Chinese sturgeon ( ) publication-title: J. Fish. Chin. doi: 10.3724/SP.J.1231.2012.27770 – volume: 6 start-page: 1 issue: 1 year: 1997 end-page: 20 ident: CR15 article-title: Phylogeny and relationships of pleurotomariid gastropods (Mollusca: Gastropoda): an assessment based on partial 18S rDNA and cytochrome oxidase I sequences publication-title: Mol. Mar. Biol. Biotechnol. – volume: 138 start-page: 79 issue: 1 year: 2004 end-page: 82 ident: CR46 article-title: Cloning and expression of a Na , K -ATPase α-subunit from (TNaK1α) publication-title: Mol. Biochem. Parasitol. doi: 10.1016/j.molbiopara.2004.07.009 – volume: 204 start-page: 4 005 year: 2001 end-page: 4 012 ident: CR45 article-title: Na +K -ATPase in gills of the blue crab : cDNA sequencing and salinity-related expression of α-subunit mRNA and protein publication-title: J. Exp. Biol. – volume: 39 start-page: 75 issue: 1 year: 2005 end-page: 85 ident: CR47 article-title: Real-time PCR for mRNA quantitation publication-title: Biotechniques doi: 10.2144/05391RV01 – volume: 135 start-page: 195 issue: 2 year: 2003 end-page: 214 ident: CR26 article-title: Na +K -ATPase in gills of aquatic crustacean publication-title: Comp. Biochem. Physiol. A: Mol. Integr. Physiol. doi: 10.1016/S1095-6433(03)00064-3 – volume: 4 start-page: 512 issue: 5 year: 2002 end-page: 519 ident: CR33 article-title: Molecular cloning and characterization of two Na/K-ATPase isoforms in publication-title: Marine Biotechnology doi: 10.1007/s10126-002-0031-z – volume: 1365 start-page: 37 issue: 1–2 year: 1998 end-page: 45 ident: CR30 article-title: Evolution of P-type ATPases publication-title: Biochim. Biophys. Acta doi: 10.1016/S0005-2728(98)00041-3 – volume: 316 start-page: 691 issue: 6030 year: 1985 end-page: 695 ident: CR36 article-title: Amino-acid sequence of the catalytic subunit of the (Na +K )ATPase deduced from a complementary DNA publication-title: Nature doi: 10.1038/316691a0 – volume: 113A start-page: 361 issue: 4 year: 1996 end-page: 368 ident: CR8 article-title: Branchial Na, K-ATPase and osmoregulation in the purple shore crab (Dana) publication-title: Comp. Biochem. Physiol. doi: 10.1016/0300-9629(95)02076-4 – volume: 15 start-page: 1 issue: 1 year: 1995 end-page: 60 ident: CR32 article-title: Osmotic regulation in crustaceans publication-title: J. Crust. Biol. doi: 10.2307/1549010 – volume: 2 start-page: 107 year: 1981 end-page: 122 ident: CR41 article-title: Role of Na -K -ATPase in ionic regulation by marine and estuarine animals publication-title: Mar. Biol. Lett. – volume: 265 start-page: 387 issue: 4 year: 1993 end-page: 396 ident: CR43 article-title: Ion transport systems in membrane vesicles isolated from crustacean tissues publication-title: J. Exp. Zool. doi: 10.1002/jez.1402650408 – volume: 111 start-page: 567 issue: 4 year: 1995 end-page: 573 ident: CR9 article-title: Primary sequence, tissue specificity and expression of the Na , K -ATPase α 1 subunit in the European eel ( ) publication-title: Comp. Biochem. Physiol. B: Biochem. Mol. Biol. doi: 10.1016/0305-0491(95)00037-9 – volume: 210 start-page: 2 885 issue: 16 year: 2007 end-page: 2 896 ident: CR29 article-title: Differential expression of gill Na , K -ATPase α- and β-subunits, Na , K , 2Cl cotransporter and CFTR anion channel in juvenile anadromous and landlocked Atlantic salmon publication-title: J. Exp. Biol. doi: 10.1242/jeb.002873 – volume: 12 start-page: 549 issue: 3 year: 1988 end-page: 559 ident: CR3 article-title: Separation of hemocytes by density gradient centrifugation and counterflow centrifugal elutriation publication-title: Dev. Comp. Immunol. doi: 10.1016/0145-305X(88)90071-7 – volume: 149 start-page: 91 issue: 1 year: 2008 end-page: 100 ident: CR6 article-title: Cloning and expression of Na /K -ATPase and osmotic stress transcription factor 1 mRNA in black porgy, during osmotic stress publication-title: Comp. Biochem. Physiol. Part B: Biochem. Mol. Biol. doi: 10.1016/j.cbpb.2007.08.009 – start-page: 821 year: 1971 end-page: 995 ident: CR21 article-title: Salinity: Animal invertebrates publication-title: Marine Ecology Vol. 1: Environmental Factors – volume: 24 start-page: 1 596 issue: 8 year: 2007 end-page: 1 599 ident: CR38 article-title: MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0 publication-title: Mol. Biol. Evol. doi: 10.1093/molbev/msm092 – volume: 22 start-page: 4 673 issue: 22 year: 1994 end-page: 4 680 ident: CR40 article-title: CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice publication-title: Nucl. Acids Res. doi: 10.1093/nar/22.22.4673 – volume: 214 start-page: 263 issue: 1–2 year: 1997 end-page: 282 ident: CR7 article-title: Osmotic and ionic regulation by during hyposaline exposure and in response to emersion publication-title: J. Exp. Mar. Biol. Ecol. doi: 10.1016/S0022-0981(96)02778-5 – volume: 38 start-page: 57 issue: 1 year: 1994 end-page: 99 ident: CR11 article-title: P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees publication-title: J. Mol. Evol. doi: 10.1007/BF00175496 – volume: 304 start-page: 88 issue: 1–4 year: 2010 end-page: 94 ident: CR17 article-title: Na/KATPase activity and osmo-ionic regulation in adult whiteleg shrimp exposed to low salinities publication-title: Aquaculture doi: 10.1016/j.aquaculture.2010.03.025 – volume: 16 start-page: 4 250 issue: 14 year: 1997 end-page: 4 260 ident: CR5 article-title: The γ subunit is a specific component of the Na, K-ATPase and modulates its transport function publication-title: Embo J. doi: 10.1093/emboj/16.14.4250 – volume: 115 start-page: 109 issue: 2 year: 1990 end-page: 121 ident: CR13 article-title: Subunit assembly and functional maturation of Na, K-ATPase publication-title: J. Membr. Biol. doi: 10.1007/BF01869450 – volume: 269 start-page: 19 659 issue: 31 year: 1994 end-page: 19 662 ident: CR22 article-title: Na /K -ATPase publication-title: J. Biol. Chem. – volume: 25 start-page: 402 issue: 4 year: 2001 end-page: 408 ident: CR24 article-title: Analysis of relative gene expression data using real-time quantitative PCR and the 2 method publication-title: Methods doi: 10.1006/meth.2001.1262 – volume: 137C start-page: 139 year: 1993 end-page: 168 ident: CR27 article-title: Structure of the Na, K-ATPase publication-title: Int. Rev. Cytol. – volume: 215 start-page: 403 issue: 3 year: 1990 end-page: 410 ident: CR1 article-title: Basic local alignment search tool publication-title: J. Mol. Biol. doi: 10.1016/S0022-2836(05)80360-2 – volume: 331 start-page: 1 229 issue: 4 year: 2005 end-page: 1 238 ident: CR10 article-title: Cloning and characterization of sea bream Na -K -ATPase α and β subunit genes: in vitro effects of hormones on transcriptional and translational expression publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2005.04.038 – volume: 35 start-page: 1 475 issue: 10 year: 2011 end-page: 1 480 ident: CR19 article-title: Influence of salinity stress on the activity of gill Na /K -ATPase in swimming crab ( ) publication-title: J. Fish. Chin. – year: 2008 ident: CR23 publication-title: China Fisheries Yearbook 2008 – volume: 103 start-page: 95 issue: 2 year: 1988 end-page: 120 ident: CR20 article-title: Structural basis for E -E conformational transitions in Na, K-pump and Ca-pump proteins publication-title: J. Membr. Biol. doi: 10.1007/BF01870942 – volume: 46 start-page: 84 issue: 1 year: 1998 end-page: 101 ident: CR2 article-title: Evolution of substrate specificities in the P-type ATPase superfamily publication-title: J. Mol. Evol. doi: 10.1007/PL00006286 – volume: 19 start-page: 237 issue: 2 year: 2012 end-page: 245 ident: CR25 article-title: Effects of salinity on growth, molt and energy utilization of juvenile swimming crab publication-title: J. Fish. Sci. Chin. – volume: 947 start-page: l issue: 1 year: 1988 end-page: 28 ident: CR34 article-title: Structure and function of proton translocating ATPase in plasma membranes of plants and fungi publication-title: Biochim. Biophys. Acta – volume: 37 start-page: 575 issue: 6 year: 1997 end-page: 584 ident: CR44 article-title: Molecular approaches to understanding salinity adaptation of estuarine animals publication-title: Am. Zool. – volume: 321 start-page: 429 issue: 6068 year: 1986 end-page: 431 ident: CR35 article-title: Amino-acid sequence of the -subunit of the (Na +K )ATPase deduced from a cDNA publication-title: Nature doi: 10.1038/321429a0 – volume: 15 start-page: 1 issue: 1 year: 1995 ident: 4018_CR32 publication-title: J. Crust. Biol. doi: 10.2307/1549010 – volume: 204 start-page: 4 005 year: 2001 ident: 4018_CR45 publication-title: J. Exp. Biol. doi: 10.1242/jeb.204.22.4005 – volume: 1365 start-page: 37 issue: 1–2 year: 1998 ident: 4018_CR30 publication-title: Biochim. Biophys. Acta doi: 10.1016/S0005-2728(98)00041-3 – volume: 947 start-page: l issue: 1 year: 1988 ident: 4018_CR34 publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4157(88)90017-2 – volume: 214 start-page: 263 issue: 1–2 year: 1997 ident: 4018_CR7 publication-title: J. Exp. Mar. Biol. Ecol. doi: 10.1016/S0022-0981(96)02778-5 – volume: 133 start-page: 1 193 issue: 6 year: 1996 ident: 4018_CR14 publication-title: J. Cell Biol. doi: 10.1083/jcb.133.6.1193 – volume: 135 start-page: 195 issue: 2 year: 2003 ident: 4018_CR26 publication-title: Comp. Biochem. Physiol. A: Mol. Integr. Physiol. doi: 10.1016/S1095-6433(03)00064-3 – volume: 103 start-page: 95 issue: 2 year: 1988 ident: 4018_CR20 publication-title: J. Membr. Biol. doi: 10.1007/BF01870942 – volume: 210 start-page: 2 885 issue: 16 year: 2007 ident: 4018_CR29 publication-title: J. Exp. Biol. doi: 10.1242/jeb.002873 – volume: 24 start-page: 1 596 issue: 8 year: 2007 ident: 4018_CR38 publication-title: Mol. Biol. Evol. doi: 10.1093/molbev/msm092 – volume: 25 start-page: 402 issue: 4 year: 2001 ident: 4018_CR24 publication-title: Methods doi: 10.1006/meth.2001.1262 – volume: 19 start-page: 237 issue: 2 year: 2012 ident: 4018_CR25 publication-title: J. Fish. Sci. Chin. – volume: 39 start-page: 75 issue: 1 year: 2005 ident: 4018_CR47 publication-title: Biotechniques doi: 10.2144/05391RV01 – volume: 137C start-page: 139 year: 1993 ident: 4018_CR27 publication-title: Int. Rev. Cytol. – volume: 13 start-page: 833 issue: 6 year: 1996 ident: 4018_CR28 publication-title: Zool Sci. doi: 10.2108/zsj.13.833 – volume: 36 start-page: 1 386 issue: 9 year: 2012 ident: 4018_CR12 publication-title: J. Fish. Chin. doi: 10.3724/SP.J.1231.2012.27770 – volume: 4 start-page: 512 issue: 5 year: 2002 ident: 4018_CR33 publication-title: Marine Biotechnology doi: 10.1007/s10126-002-0031-z – volume: 7 start-page: 623 issue: 6 year: 2011 ident: 4018_CR37 publication-title: Mar. Biol. Res. doi: 10.1080/17451000.2010.538063 – volume: 111 start-page: 567 issue: 4 year: 1995 ident: 4018_CR9 publication-title: Comp. Biochem. Physiol. B: Biochem. Mol. Biol. doi: 10.1016/0305-0491(95)00037-9 – volume: 149 start-page: 91 issue: 1 year: 2008 ident: 4018_CR6 publication-title: Comp. Biochem. Physiol. Part B: Biochem. Mol. Biol. doi: 10.1016/j.cbpb.2007.08.009 – volume: 331 start-page: 1 229 issue: 4 year: 2005 ident: 4018_CR10 publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2005.04.038 – volume: 53 start-page: 565 issue: 1 year: 1991 ident: 4018_CR16 publication-title: Annu. Rev. Physiol. doi: 10.1146/annurev.ph.53.030191.003025 – volume: 269 start-page: 19 659 issue: 31 year: 1994 ident: 4018_CR22 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)32067-7 – volume: 265 start-page: 387 issue: 4 year: 1993 ident: 4018_CR43 publication-title: J. Exp. Zool. doi: 10.1002/jez.1402650408 – start-page: 821 volume-title: Marine Ecology Vol. 1: Environmental Factors year: 1971 ident: 4018_CR21 – volume: 25 start-page: 205 issue: 2 year: 2008 ident: 4018_CR39 publication-title: Zool Sci. doi: 10.2108/zsj.25.205 – volume: 46 start-page: 84 issue: 1 year: 1998 ident: 4018_CR2 publication-title: J. Mol. Evol. doi: 10.1007/PL00006286 – volume: 304 start-page: 88 issue: 1–4 year: 2010 ident: 4018_CR17 publication-title: Aquaculture doi: 10.1016/j.aquaculture.2010.03.025 – volume: 115 start-page: 109 issue: 2 year: 1990 ident: 4018_CR13 publication-title: J. Membr. Biol. doi: 10.1007/BF01869450 – volume: 38 start-page: 57 issue: 1 year: 1994 ident: 4018_CR11 publication-title: J. Mol. Evol. doi: 10.1007/BF00175496 – volume: 321 start-page: 429 issue: 6068 year: 1986 ident: 4018_CR35 publication-title: Nature doi: 10.1038/321429a0 – volume: 138 start-page: 79 issue: 1 year: 2004 ident: 4018_CR46 publication-title: Mol. Biochem. Parasitol. doi: 10.1016/j.molbiopara.2004.07.009 – volume: 12 start-page: 549 issue: 3 year: 1988 ident: 4018_CR3 publication-title: Dev. Comp. Immunol. doi: 10.1016/0145-305X(88)90071-7 – volume: 22 start-page: 4 673 issue: 22 year: 1994 ident: 4018_CR40 publication-title: Nucl. Acids Res. doi: 10.1093/nar/22.22.4673 – volume: 316 start-page: 691 issue: 6030 year: 1985 ident: 4018_CR36 publication-title: Nature doi: 10.1038/316691a0 – volume: 210 start-page: 2 070 issue: Pt12 year: 2007 ident: 4018_CR18 publication-title: J. Exp. Biol. doi: 10.1242/jeb.004309 – volume: 215 start-page: 403 issue: 3 year: 1990 ident: 4018_CR1 publication-title: J. Mol. Biol. doi: 10.1016/S0022-2836(05)80360-2 – volume: 6 start-page: 1 issue: 1 year: 1997 ident: 4018_CR15 publication-title: Mol. Mar. Biol. Biotechnol. – volume: 113A start-page: 361 issue: 4 year: 1996 ident: 4018_CR8 publication-title: Comp. Biochem. Physiol. doi: 10.1016/0300-9629(95)02076-4 – volume: 35 start-page: 1 475 issue: 10 year: 2011 ident: 4018_CR19 publication-title: J. Fish. Chin. – volume: 257 start-page: 181 issue: 1 year: 1989 ident: 4018_CR4 publication-title: FEBS Lett. doi: 10.1016/0014-5793(89)81816-2 – volume: 2 start-page: 107 year: 1981 ident: 4018_CR41 publication-title: Mar. Biol. Lett. – start-page: 241 volume-title: Comparative Aspects of Sodium Cotransport Systems year: 1990 ident: 4018_CR42 – volume: 29 start-page: 286 issue: 2 year: 2010 ident: 4018_CR31 publication-title: Fish. Shellfish Immunol. doi: 10.1016/j.fsi.2010.04.011 – volume: 37 start-page: 575 issue: 6 year: 1997 ident: 4018_CR44 publication-title: Am. Zool. doi: 10.1093/icb/37.6.575 – volume: 16 start-page: 4 250 issue: 14 year: 1997 ident: 4018_CR5 publication-title: Embo J. doi: 10.1093/emboj/16.14.4250 – volume-title: China Fisheries Yearbook 2008 year: 2008 ident: 4018_CR23 |
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| Snippet | Na^＋/K^＋-ATPases are membrane-associated enzymes responsible for the active transport of Na^＋ and K^＋ ions across cell membranes, generating chemical and... Na⁺/K⁺-ATPases are membrane-associated enzymes responsible for the active transport of Na⁺ and K⁺ ions across cell membranes, generating chemical and... Na + /K + -ATPases are membrane-associated enzymes responsible for the active transport of Na + and K + ions across cell membranes, generating chemical and... Na+/K+-ATPases are membrane-associated enzymes responsible for the active transport of Na+ and K+ ions across cell membranes, generating chemical and... |
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| SubjectTerms | 3' Untranslated regions 5' Untranslated Regions Active transport Adenosine triphosphate Amino acid sequence Amino acid sequences Amino acids Analysis Aquatic crustaceans ATP ATP酶 Binding sites Biology Cell membranes Cladistics Cloning Complementary DNA Crabs Crustaceans Earth and Environmental Science Earth Sciences Enzymes Hepatopancreas ions Marine biology Marine crustaceans Membranes molecular cloning Molecular weight muscles Na+/K+-exchanging ATPase Nucleotide sequence Nucleotides Oceanography open reading frames PCR Phosphorylation Phylogeny Polymerase chain reaction Portunus trituberculatus potassium rapid amplification of cDNA ends reverse transcriptase polymerase chain reaction RT-PCR分析 Salinity Salinity effects salt stress Sequencing sodium Swimming Transcription Transmembrane domains 三疣梭子蟹 亚单位 分子克隆 核苷酸序列分析 盐胁迫 逆转录聚合酶链反应 |
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| Title | Na^＋/K^＋-ATPase α-subunit in swimming crab Portunus trituberculatus： molecular cloning, characterization, and expression under low salinity stress |
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