메뉴 건너뛰기




Volumn 14, Issue 6, 2009, Pages 2130-2148

Na,K-ATPase and epithelial tight junctions

Author keywords

Fxyd; K ATpase; Na; Occludin; Polarity; Review; Signaling; Tight junction; subunit; subunit

Indexed keywords

DANIO RERIO; MAMMALIA;

EID: 63849192756     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3367     Document Type: Article
Times cited : (49)

References (221)
  • 4
    • 39849109700 scopus 로고    scopus 로고
    • Crosstalk of tight junction components with signaling pathways
    • DOI 10.1016/j.bbamem.2007.08.018, PII S0005273607003057
    • Gonzalez-Mariscal L., R. Tapia and D. Chamorro: Crosstalk of tight junction components with signaling pathways. Biochim Biophys Acta, 1778, 729-756 (2008). (Pubitemid 351317800)
    • (2008) Biochimica et Biophysica Acta - Biomembranes , vol.1778 , Issue.3 , pp. 729-756
    • Gonzalez-Mariscal, L.1    Tapia, R.2    Chamorro, D.3
  • 5
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • Van Itallie C. M. and J. M. Anderson: Claudins and epithelial paracellular transport. Annul Rev Physiol, 68, 403-429 (2006).
    • (2006) Annul Rev Physiol , vol.68 , pp. 403-429
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 6
    • 33645747414 scopus 로고    scopus 로고
    • Claudins in occluding junctions of humans and flies
    • Furuse M. and S. Tsukita: Claudins in occluding junctions of humans and flies. Trends Cell Biol, 16, 181-188 (2006).
    • (2006) Trends Cell Biol , vol.16 , pp. 181-188
    • Furuse, M.1    Tsukita, S.2
  • 7
    • 0141920729 scopus 로고    scopus 로고
    • The Claudin-like Megatrachea is essential in septate junctions for the epithelial barrier function in Drosophila
    • DOI 10.1016/S1534-5807(03)00275-2, PII S1534580703002752
    • Behr M., D. Riedel and R. Schuh: The claudin-like megatrachea is essential in septate junctions for the epithelial barrier function in Drosophila. Dev Cell, 5, 611-620 (2003). (Pubitemid 37243049)
    • (2003) Developmental Cell , vol.5 , Issue.4 , pp. 611-620
    • Behr, M.1    Riedel, D.2    Schuh, R.3
  • 8
    • 1642458089 scopus 로고    scopus 로고
    • Sinuous is a Drosophila claudin required for septate junction organization and epithelial tube size control
    • DOI 10.1083/jcb.200309134
    • Wu V. M., J. Schulte, A. Hirschi, U. Tepass and G. J. Beitel: Sinuous is a Drosophila claudin required for septate junction organization and epithelial tube size control. J Cell Biol, 164, 313-323 (2004). (Pubitemid 38133950)
    • (2004) Journal of Cell Biology , vol.164 , Issue.2 , pp. 313-323
    • Wu, V.M.1    Schulte, J.2    Hirschi, A.3    Tepass, U.4    Beitel, G.J.5
  • 9
    • 0037115724 scopus 로고    scopus 로고
    • Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells
    • DOI 10.1242/jcs.00165
    • Amasheh S., N. Meiri, A. H. Gitter, T. Schoneberg, J. Mankertz, J. D. Schulzke and M. Fromm: Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J Cell Sci, 115, 4969-4976 (2002). (Pubitemid 36061180)
    • (2002) Journal of Cell Science , vol.115 , Issue.24 , pp. 4969-4976
    • Amasheh, S.1    Meiri, N.2    Gitter, A.H.3    Schoneberg, T.4    Mankertz, J.5    Schulzke, J.D.6    Fromm, M.7
  • 10
    • 0038701734 scopus 로고    scopus 로고
    • Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture
    • Colegio O. R., C. Van Itallie, C. Rahner and J. M. Anderson: Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. Am J Physiol Cell Physiol, 284, C1346-1354 (2003). (Pubitemid 36583375)
    • (2003) American Journal of Physiology - Cell Physiology , vol.284 , Issue.6
    • Colegio, O.R.1    Van Itallie, C.2    Rahner, C.3    Anderson, J.M.4
  • 11
    • 0242665742 scopus 로고    scopus 로고
    • Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins
    • Van Itallie C. M., A. S. Fanning and J. M. Anderson: Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins. Am J Physiol Renal Physiol, 285, F1078-1084 (2003). (Pubitemid 37421043)
    • (2003) American Journal of Physiology - Renal Physiology , vol.285 , Issue.6
    • Van Itallie, C.M.1    Fanning, A.S.2    Anderson, J.M.3
  • 12
    • 0033552629 scopus 로고    scopus 로고
    • Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins
    • DOI 10.1083/jcb.147.6.1351
    • Itoh M., M. Furuse, K. Morita, K. Kubota, M. Saitou and S. Tsukita: Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J Cell Biol, 147, 1351-1363 (1999). (Pubitemid 30012818)
    • (1999) Journal of Cell Biology , vol.147 , Issue.6 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 13
    • 0037016668 scopus 로고    scopus 로고
    • Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule
    • DOI 10.1074/jbc.M109005200
    • Hamazaki Y., M. Itoh, H. Sasaki, M. Furuse and S. Tsukita: Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule. J Biol Chem, 277, 455-461 (2002). (Pubitemid 34952079)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.1 , pp. 455-461
    • Hamazaki, Y.1    Itoh, M.2    Sasaki, H.3    Furuse, M.4    Tsukita, S.5
  • 14
    • 1542778870 scopus 로고    scopus 로고
    • Claudin-8 interacts with multi-PDZ domain protein 1 (MUPP1) and reduces paracellular conductance in epithelial cells
    • Jeansonne B., Q. Lu, D. A. Goodenough and Y. H. Chen: Claudin-8 interacts with multi-PDZ domain protein 1 (MUPP1) and reduces paracellular conductance in epithelial cells. Cell Mol Biol, 49, 13-21 (2003).
    • (2003) Cell Mol Biol , vol.49 , pp. 13-21
    • Jeansonne, B.1    Lu, Q.2    Goodenough, D.A.3    Chen, Y.H.4
  • 15
    • 0037178864 scopus 로고    scopus 로고
    • The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions
    • DOI 10.1074/jbc.M201177200
    • Roh M. H., C. J. Liu, S. Laurinec and B. Margolis: The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions. J Biol Chem, 277, 27501-27509 (2002). (Pubitemid 34951771)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 27501-27509
    • Roh, M.H.1    Liu, C.-J.2    Laurinec, S.3    Margolis, B.4
  • 16
    • 22544434673 scopus 로고    scopus 로고
    • Phosphorylation of Claudin-3 at threonine 192 by cAMP-dependent protein kinase regulates tight junction barrier function in ovarian cancer cells
    • DOI 10.1074/jbc.M502003200
    • D'Souza T., R. Agarwal and P. J. Morin: Phosphorylation of claudin-3 at threonine 192 by cAMPdependent protein kinase regulates tight junction barrier function in ovarian cancer cells. J. Biol. Chem., 280, 26233-26240 (2005). (Pubitemid 41022220)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.28 , pp. 26233-26240
    • D'Souza, T.1    Agarwal, R.2    Morin, P.J.3
  • 17
    • 34548023972 scopus 로고    scopus 로고
    • Phosphorylation of claudin-4 by PKCε regulates tight junction barrier function in ovarian cancer cells
    • DOI 10.1016/j.yexcr.2007.06.026, PII S0014482707003163
    • D'Souza T., F. E. Indig and P. J. Morin: Phosphorylation of claudin-4 by PKC (epsilon) regulates tight junction barrier function in ovarian cancer cells. Exp Cell Res, 313, 3364-3375 (2007). (Pubitemid 47284066)
    • (2007) Experimental Cell Research , vol.313 , Issue.15 , pp. 3364-3375
    • D'Souza, T.1    Indig, F.E.2    Morin, P.J.3
  • 18
    • 1642543216 scopus 로고    scopus 로고
    • 203 of claudin-1, a putative phosphorylation site for MAP kinase, is required to promote the barrier function of tight junctions
    • DOI 10.1016/j.yexcr.2003.12.014, PII S0014482703006888
    • Fujibe M., H. Chiba, T. Kojima, T. Soma, T. Wada, T. Yamashita and N. Sawada: Thr203 of claudin-1, a putative phosphorylation site for MAP kinase, is required to promote the barrier function of tight junctions. Exp Cell Res, 295, 36-47 (2004). (Pubitemid 38407343)
    • (2004) Experimental Cell Research , vol.295 , Issue.1 , pp. 36-47
    • Fujibe, M.1    Chiba, H.2    Kojima, T.3    Soma, T.4    Wada, T.5    Yamashita, T.6    Sawada, N.7
  • 19
    • 20444481707 scopus 로고    scopus 로고
    • Interferon-γ induces internalization of epithelial tight junction proteins via a macropinocytosis-like process
    • DOI 10.1096/fj.04-3260com
    • Bruewer M., M. Utech, A. I. Ivanov, A. M. Hopkins, C. A. Parkos and A. Nusrat: Interferon-{gamma} induces internalization of epithelial tight junction proteins via a macropinocytosis-like process. FASEB J., 19, 923-933 (2005). (Pubitemid 40827713)
    • (2005) FASEB Journal , vol.19 , Issue.8 , pp. 923-933
    • Bruewer, M.1    Utech, M.2    Ivanov, A.I.3    Hopkins, A.M.4    Parkos, C.A.5    Nusrat, A.6
  • 20
    • 26244442836 scopus 로고    scopus 로고
    • Mechanism of IFN-γ-induced endocytosis of tight junction proteins: Myosin II-dependent vacuolarization of the apical plasma membrane
    • DOI 10.1091/mbc.E05-03-0193
    • Utech M., A. I. Ivanov, S. N. Samarin, M. Bruewer, J. R. Turner, R. J. Mrsny, C. A. Parkos and A. Nusrat: Mechanism of IFN-gamma-induced endocytosis of tight junction proteins: myosin II-dependent vacuolarization of the apical plasma membrane. Mol Biol Cell, 16, 5040-5052 (2005). (Pubitemid 41416480)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.10 , pp. 5040-5052
    • Utech, M.1    Ivanov, A.I.2    Samarin, S.N.3    Bruewer, M.4    Turner, J.R.5    Mrsny, R.J.6    Parkos, C.A.7    Nusrat, A.8
  • 21
    • 0942287209 scopus 로고    scopus 로고
    • Epidermal Growth Factor Receptor Activation Differentially Regulates Claudin Expression and Enhances Transepithelial Resistance in Madin-Darby Canine Kidney Cells
    • DOI 10.1074/jbc.M308682200
    • Singh A. B. and R. C. Harris: Epidermal growth factor receptor activation differentially regulates claudin expression and enhances transepithelial resistance in Madin-Darby canine kidney cells. J Biol Chem, 279, 3543-3552 (2004). (Pubitemid 38140594)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3543-3552
    • Singh, A.B.1    Harris, R.C.2
  • 22
    • 36049034205 scopus 로고    scopus 로고
    • Juxtacrine activation of EGFR regulates claudin expression and increases transepithelial resistance
    • DOI 10.1152/ajpcell.00274.2007
    • Singh A. B., K. Sugimoto, P. Dhawan and R. C. Harris: Juxtacrine activation of EGFR regulates claudin expression and increases transepithelial resistance. Am J Physiol Cell Physiol, 293, C1660-1668 (2007). (Pubitemid 350085633)
    • (2007) American Journal of Physiology - Cell Physiology , vol.293 , Issue.5
    • Singh, A.B.1    Sugimoto, K.2    Dhawan, P.3    Harris, R.C.4
  • 24
    • 13544266585 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases 1/2 control claudin-2 expression in Madin-Darby canine kidney strain I and II cells
    • DOI 10.1074/jbc.M408122200
    • Lipschutz J. H., S. Li, A. Arisco and D. F. Balkovetz: Extracellular signal-regulated kinases 1/2 control claudin-2 expression in Madin-Darby canine kidney strain I and II cells. J. Biol. Chem., 280, 3780-3788 (2005). (Pubitemid 40223847)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3780-3788
    • Lipschutz, J.H.1    Li, S.2    Arisco, A.3    Balkovetz, D.F.4
  • 25
    • 2942571778 scopus 로고    scopus 로고
    • Hepatocyte growth factor disrupts tight junctions in human breast cancer cells
    • DOI 10.1016/j.cellbi.2004.03.003, PII S1065699504000587
    • Martin T. A., G. Watkins, R. E. Mansel and W. G. Jiang: Hepatocyte growth factor disrupts tight junctions in human breast cancer cells. Cell Biol Int, 28, 361-371 (2004). (Pubitemid 38748926)
    • (2004) Cell Biology International , vol.28 , Issue.5 , pp. 361-371
    • Martin, T.A.1    Watkins, G.2    Mansel, R.E.3    Jiang, W.G.4
  • 26
    • 1442300805 scopus 로고    scopus 로고
    • Hepatocyte growth factor induces MDCK cell morphogenesis without causing loss of tight junction functional integrity
    • Pollack A. L., G. Apodaca and K. E. Mostov: Hepatocyte growth factor induces MDCK cell morphogenesis without causing loss of tight junction functional integrity. Am J Physiol Cell Physiol, 286, C482-494 (2004). (Pubitemid 38292654)
    • (2004) American Journal of Physiology - Cell Physiology , vol.286 , Issue.3
    • Pollack, A.L.1    Apodaca, G.2    Mostov, K.E.3
  • 27
    • 0035047036 scopus 로고    scopus 로고
    • Transforming growth factor-β3 perturbs the inter-Sertoli tight junction permeability barrier in vitro possibly mediated via its effects on occludin, zonula occludens-1, and claudin-11
    • DOI 10.1210/en.142.5.1865
    • Lui W. Y., W. M. Lee and C. Y. Cheng: Transforming growth factor-beta3 perturbs the inter- Sertoli tight junction permeability barrier in vitro possibly mediated via its effects on occludin, zonula occludens-1, and claudin-11. Endocrinology, 142, 1865-1877 (2001). (Pubitemid 32405944)
    • (2001) Endocrinology , vol.142 , Issue.5 , pp. 1865-1877
    • Lui, W.-Y.1    Lee, W.M.2    Cheng, C.Y.3
  • 29
    • 0038106228 scopus 로고    scopus 로고
    • Regulation of tight junctions during the epithelium-mesenchyme transition: Direct repression of the gene expression of claudins/occludin by Snail
    • DOI 10.1242/jcs.00389
    • Ikenouchi J., M. Matsuda, M. Furuse and S. Tsukita: Regulation of tight junctions during the epithelium-mesenchyme transition: direct repression of the gene expression of claudins/occludin by Snail. J Cell Sci, 116, 1959-1967 (2003). (Pubitemid 36622294)
    • (2003) Journal of Cell Science , vol.116 , Issue.10 , pp. 1959-1967
    • Ikenouchi, J.1    Matsuda, M.2    Furuse, M.3    Tsukita, S.4
  • 30
    • 0942268163 scopus 로고    scopus 로고
    • Functional crosstalk between Wnt signaling and Cdx-related transcriptional activation in the regulation of the claudin-2 promoter activity
    • DOI 10.1016/j.bbrc.2003.12.185
    • Mankertz J., B. Hillenbrand, S. Tavalali, O. Huber, M. Fromm and J. D. Schulzke: Functional crosstalk between Wnt signaling and Cdx-related transcriptional activation in the regulation of the claudin-2 promoter activity. Biochem Biophys Res Commun, 314, 1001-1007 (2004). (Pubitemid 38142383)
    • (2004) Biochemical and Biophysical Research Communications , vol.314 , Issue.4 , pp. 1001-1007
    • Mankertz, J.1    Hillenbrand, B.2    Tavalali, S.3    Huber, O.4    Fromm, M.5    Schulzke, J.-D.6
  • 31
    • 0034584636 scopus 로고    scopus 로고
    • Involvement of claudin-1 in the β-catenin/Tcf signaling pathway and its frequent upregulation in human colorectal cancers
    • Miwa N., M. Furuse, S. Tsukita, N. Niikawa, Y. Nakamura and Y. Furukawa: Involvement of claudin-1 in the beta-catenin/Tcf signaling pathway and its frequent upregulation in human colorectal cancers. Oncol Res, 12, 469-476 (2001). (Pubitemid 33791807)
    • (2000) Oncology Research , vol.12 , Issue.11-12 , pp. 469-476
    • Miwa, N.1    Furuse, M.2    Tsukita, S.3    Niikawa, N.4    Nakamura, Y.5    Furukawa, Y.6
  • 32
    • 0037077248 scopus 로고    scopus 로고
    • Cloning of the human claudin-2 5'-flanking region revealed a TATA-less promoter with conserved binding sites in mouse and human for caudal-related homeodomain proteins and hepatocyte nuclear factor-1α
    • DOI 10.1074/jbc.M110261200
    • Sakaguchi T., X. Gu, H. M. Golden, E. Suh, D. B. Rhoads and H. C. Reinecker: Cloning of the human claudin-2 5'-flanking region revealed a TATA-less promoter with conserved binding sites in mouse and human for caudal-related homeodomain proteins and hepatocyte nuclear factor-1alpha. J Biol Chem, 277, 21361-21370 (2002). (Pubitemid 34952276)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21361-21370
    • Sakaguchi, T.1    Gu, X.2    Golden, H.M.3    Suh, E.4    Rhoads, D.B.5    Reinecker, H.-C.6
  • 34
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda M. S., J. A. Whitney, C. Flores, S. Gonzalez, M. Cereijido and K. Matter: Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J Cell Biol, 134, 1031-1049 (1996). (Pubitemid 26278226)
    • (1996) Journal of Cell Biology , vol.134 , Issue.4 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3    Gonzalez, S.4    Cereijido, M.5    Matter, K.6
  • 36
    • 0032550221 scopus 로고    scopus 로고
    • Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions
    • DOI 10.1083/jcb.141.2.397
    • Saitou M., K. Fujimoto, Y. Doi, M. Itoh, T. Fujimoto, M. Furuse, H. Takano, T. Noda and S. Tsukita: Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions. J Cell Biol, 141, 397-408 (1998). (Pubitemid 28237088)
    • (1998) Journal of Cell Biology , vol.141 , Issue.2 , pp. 397-408
    • Saitou, M.1    Fujimoto, K.2    Doi, Y.3    Itoh, M.4    Fujimoto, T.5    Furuse, M.6    Takano, H.7    Noda, T.8    Tsukita, S.9
  • 38
    • 0034703027 scopus 로고    scopus 로고
    • The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction
    • DOI 10.1074/jbc.M002450200
    • Nusrat A., J. A. Chen, C. S. Foley, T. W. Liang, J. Tom, M. Cromwell, C. Quan and R. J. Mrsny: The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction. J Biol Chem, 275, 29816-29822 (2000). (Pubitemid 32043866)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.38 , pp. 29816-29822
    • Nusrat, A.1    Chen, J.A.2    Foley, C.S.3    Liang, T.W.4    Tom, J.5    Cromwell, M.6    Quan, C.7    Mrsny, R.J.8
  • 39
    • 0038201989 scopus 로고    scopus 로고
    • Occludin phosphorylation: Identification of an occludin kinase in brain and cell extracts as CK2
    • DOI 10.1016/S0014-5793(03)00525-8
    • Smales C., M. Ellis, R. Baumber, N. Hussain, H. Desmond and J. M. Staddon: Occludin phosphorylation: identification of an occludin kinase in brain and cell extracts as CK2. FEBS Lett, 545, 161-166 (2003). (Pubitemid 36694694)
    • (2003) FEBS Letters , vol.545 , Issue.2-3 , pp. 161-166
    • Smales, C.1    Ellis, M.2    Baumber, R.3    Hussain, N.4    Desmond, H.5    Staddon, J.M.6
  • 40
    • 0037009005 scopus 로고    scopus 로고
    • Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight junction complex
    • DOI 10.1083/jcb.200206114
    • Nunbhakdi-Craig V., T. Machleidt, E. Ogris, D. Bellotto, C. L. White, 3rd and E. Sontag: Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight junction complex. J Cell Biol, 158, 967-978 (2002). (Pubitemid 35001086)
    • (2002) Journal of Cell Biology , vol.158 , Issue.5 , pp. 967-978
    • Nunbhakdi-Craig, V.1    Machleidt, T.2    Ogris, E.3    Bellotto, D.4    White Iii, C.L.5    Sontag, E.6
  • 41
    • 34249668828 scopus 로고    scopus 로고
    • Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer
    • DOI 10.1074/jbc.M610597200
    • Seth A., P. Sheth, B. C. Elias and R. Rao: Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer. J Biol Chem, 282, 11487-11498 (2007). (Pubitemid 47100808)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11487-11498
    • Seth, A.1    Sheth, P.2    Elias, B.C.3    Rao, R.4
  • 42
    • 0033551811 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces rapid phosphorylation of tight junction proteins occludin and zonula occluden 1. A potential mechanism for vascular permeability in diabetic retinopathy and tumors
    • Antonetti D. A., A. J. Barber, L. A. Hollinger, E. B. Wolpert and T. W. Gardner: Vascular endothelial growth factor induces rapid phosphorylation of tight junction proteins occludin and zonula occluden 1. A potential mechanism for vascular permeability in diabetic retinopathy and tumors. J Biol Chem, 274, 23463-23467 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 23463-23467
    • Antonetti, D.A.1    Barber, A.J.2    Hollinger, L.A.3    Wolpert, E.B.4    Gardner, T.W.5
  • 44
    • 0035971219 scopus 로고    scopus 로고
    • Regulation of tight junction permeability and occludin phosphorylation by RhoA-p160ROCK-dependent and - independent mechanisms
    • Hirase T., S. Kawashima, E. Y. M. Wong, T. Ueyama, Y. Rikitake, S. Tsukita, M. Yokoyama and J. M. Staddon: Regulation of tight junction permeability and occludin phosphorylation by RhoA-p160ROCK-dependent and - independent mechanisms. J. Biol. Chem., 276, 10423-10431 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 10423-10431
    • Hirase, T.1    Kawashima, S.2    Wong, E.Y.M.3    Ueyama, T.4    Rikitake, Y.5    Tsukita, S.6    Yokoyama, M.7    Staddon, J.M.8
  • 46
    • 0033521140 scopus 로고    scopus 로고
    • Protein interactions at the tight junction: Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3
    • Wittchen E. S., J. Haskins and B. R. Stevenson: Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3. J Biol Chem, 274, 35179-35185 (1999). (Pubitemid 129509574)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.49 , pp. 35179-35185
    • Wittchen, E.S.1    Haskins, J.2    Stevenson, B.R.3
  • 48
    • 0035864383 scopus 로고    scopus 로고
    • Cx32 but not Cx26 is associated with tight junctions in primary cultures of rat hepatocytes
    • DOI 10.1006/excr.2000.5103
    • Kojima T., Y. Kokai, H. Chiba, M. Yamamoto, Y. Mochizuki and N. Sawada: C×32 but not C×26 is associated with tight junctions in primary cultures of rat hepatocytes. Exp Cell Res, 263, 193-201 (2001). (Pubitemid 32989093)
    • (2001) Experimental Cell Research , vol.263 , Issue.2 , pp. 193-201
    • Kojima, T.1    Kokai, Y.2    Chiba, H.3    Yamamoto, M.4    Mochizuki, Y.5    Sawada, N.6
  • 49
    • 0034122209 scopus 로고    scopus 로고
    • Expression from the human occludin promoter is affected by tumor necrosis factor α and interferon γ
    • Mankertz J., S. Tavalali, H. Schmitz, A. Mankertz, E. O. Riecken, M. Fromm and J. D. Schulzke: Expression from the human occludin promoter is affected by tumor necrosis factor alpha and interferon gamma. J Cell Sci, 113, 2085-2090 (2000). (Pubitemid 30386512)
    • (2000) Journal of Cell Science , vol.113 , Issue.11 , pp. 2085-2090
    • Mankertz, J.1    Tavalali, S.2    Schmitz, H.3    Mankertz, A.4    Riecken, E.O.5    Fromm, M.6    Schulzke, J.D.7
  • 50
    • 16844368294 scopus 로고    scopus 로고
    • The JAM family of proteins
    • DOI 10.1016/j.addr.2005.01.005, Adhesion Proteins in Cellular Tight Junctions: Critical Components in the Modulation of Paracellular Permeability
    • Mandell K. J. and C. A. Parkos: The JAM family of proteins. Adv Drug Deliv Rev, 57, 857-867 (2005). (Pubitemid 40488107)
    • (2005) Advanced Drug Delivery Reviews , vol.57 , Issue.6 , pp. 857-867
    • Mandell, K.J.1    Parkos, C.A.2
  • 52
    • 15744362477 scopus 로고    scopus 로고
    • Junctional adhesion molecule 1 regulates epithelial cell morphology through effects on β1 integrins and Rap1 activity
    • DOI 10.1074/jbc.M412650200
    • Mandell K. J., B. A. Babbin, A. Nusrat and C. A. Parkos: Junctional adhesion molecule 1 regulates epithelial cell morphology through effects on beta1 integrins and Rap1 activity. J Biol Chem, 280, 11665-11674 (2005). (Pubitemid 40418481)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11665-11674
    • Mandell, K.J.1    Babbin, B.A.2    Nusrat, A.3    Parkos, C.A.4
  • 54
    • 0034623082 scopus 로고    scopus 로고
    • Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1
    • Ebnet K., C. U. Schulz, M. K. Meyer Zu Brickwedde, G. G. Pendl and D. Vestweber: Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1. J Biol Chem, 275, 27979-27988 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 27979-27988
    • Ebnet, K.1    Schulz, C.U.2    Meyer Zu Brickwedde, M.K.3    Pendl, G.G.4    Vestweber, D.5
  • 55
    • 0035937810 scopus 로고    scopus 로고
    • Association of junctional adhesion molecule with calcium/calmodulin- dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells
    • Martinez-Estrada O. M., A. Villa, F. Breviario, F. Orsenigo, E. Dejana and G. Bazzoni: Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells. J Biol Chem, 276, 9291-9296 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 9291-9296
    • Martinez-Estrada, O.M.1    Villa, A.2    Breviario, F.3    Orsenigo, F.4    Dejana, E.5    Bazzoni, G.6
  • 56
    • 0037641234 scopus 로고    scopus 로고
    • JAM4, a junctional cell adhesion molecule interacting with a tight junction protein, MAGI-1
    • DOI 10.1128/MCB.23.12.4267-4282.2003
    • Hirabayashi S., M. Tajima, I. Yao, W. Nishimura, H. Mori and Y. Hata: JAM4, a junctional cell adhesion molecule interacting with a tight junction protein, MAGI-1. Mol Cell Biol, 23, 4267-4282 (2003). (Pubitemid 36666429)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.12 , pp. 4267-4282
    • Hirabayashi, S.1    Tajima, M.2    Yao, I.3    Nishimura, W.4    Mori, H.5    Hata, Y.6
  • 57
    • 16344374495 scopus 로고    scopus 로고
    • PICK-1: A scaffold protein that interacts with Nectins and JAMs at cell junctions
    • DOI 10.1016/j.febslet.2005.03.010
    • Reymond N., S. Garrido-Urbani, J. P. Borg, P. Dubreuil and M. Lopez: PICK-1: a scaffold protein that interacts with Nectins and JAMs at cell junctions. FEBS Lett, 579, 2243-2249 (2005). (Pubitemid 40469700)
    • (2005) FEBS Letters , vol.579 , Issue.10 , pp. 2243-2249
    • Reymond, N.1    Garrido-Urbani, S.2    Borg, J.-P.3    Dubreuil, P.4    Lopez, M.5
  • 58
    • 0035898658 scopus 로고    scopus 로고
    • The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)
    • DOI 10.1093/emboj/20.14.3738
    • Ebnet K., A. Suzuki, Y. Horikoshi, T. Hirose, M. K. Meyer Zu Brickwedde, S. Ohno and D. Vestweber: The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM). EMBO J, 20, 3738-3748 (2001). (Pubitemid 32691785)
    • (2001) EMBO Journal , vol.20 , Issue.14 , pp. 3738-3748
    • Ebnet, K.1    Suzuki, A.2    Horikoshi, Y.3    Hirose, T.4    Meyer Zu Brickwedde, M.-K.5    Ohno, S.6    Vestweber, D.7
  • 61
    • 33745269374 scopus 로고    scopus 로고
    • Zonula occludens-1 function in the assembly of tight junctions in Madin-Darby canine kidney epithelial cells
    • DOI 10.1091/mbc.E05-07-0650
    • McNeil E., C. T. Capaldo and I. G. Macara: Zonula occludens-1 function in the assembly of tight junctions in Madin-Darby canine kidney epithelial cells. Mol. Biol. Cell, 17, 1922-1932 (2006). (Pubitemid 44011607)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.4 , pp. 1922-1932
    • McNeil, E.1    Capaldo, C.T.2    Macara, I.G.3
  • 62
    • 7244219999 scopus 로고    scopus 로고
    • Establishment and characterization of cultured epithelial cells lacking expression of ZO-1
    • DOI 10.1074/jbc.M406563200
    • Umeda K., T. Matsui, M. Nakayama, K. Furuse, H. Sasaki, M. Furuse and S. Tsukita: Establishment and characterization of cultured epithelial cells lacking expression of ZO-1. J. Biol. Chem., 279, 44785-44794 (2004). (Pubitemid 39430889)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.43 , pp. 44785-44794
    • Umeda, K.1    Matsui, T.2    Nakayama, M.3    Furuse, E.4    Sasaki, H.5    Furuse, M.6    Tsukita, S.7
  • 63
    • 22244455455 scopus 로고    scopus 로고
    • Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions
    • DOI 10.1146/annurev.biochem.74.082803.133339
    • Funke L., S. Dakoji and D. S. Bredt: Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions. Annu Rev Biochem, 74, 219-45 (2005). (Pubitemid 40995507)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 219-245
    • Funke, L.1    Dakoji, S.2    Bredt, D.S.3
  • 64
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to α catenin and actin filaments
    • DOI 10.1083/jcb.138.1.181
    • Itoh M, A. Nagafuchi, S. Moroi and S. Tsukita: Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments. J. Cell Biol., 138, 181-192 (1997). (Pubitemid 27337462)
    • (1997) Journal of Cell Biology , vol.138 , Issue.1 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, S.4
  • 65
    • 0030039226 scopus 로고    scopus 로고
    • Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions
    • DOI 10.1083/jcb.132.3.451
    • Rajasekaran A. K., M. Hojo, T. Huima and E. Rodriguez-Boulan: Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions. J Cell Biol, 132, 451-463 (1996). (Pubitemid 26053448)
    • (1996) Journal of Cell Biology , vol.132 , Issue.3 , pp. 451-463
    • Rajasekaran, A.K.1    Hojo, M.2    Huima, T.3    Rodriguez-Boulan, E.4
  • 66
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression
    • Balda M. S. and K. Matter: The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression. EMBO J, 19, 2024-2033 (2000). (Pubitemid 30237578)
    • (2000) EMBO Journal , vol.19 , Issue.9 , pp. 2024-2033
    • Balda, M.S.1    Matter, K.2
  • 67
    • 0347986547 scopus 로고    scopus 로고
    • The tight junction protein ZO-2 associates with Jun, Fos and C/EBP transcription factors in epithelial cells
    • DOI 10.1016/j.yexcr.2003.08.007
    • Betanzos A., M. Huerta, E. Lopez-Bayghen, E. Azuara, J. Amerena and L. Gonzalez-Mariscal: The tight junction protein ZO-2 associates with Jun, Fos and C/EBP transcription factors in epithelial cells. Exp Cell Res, 292, 51-66 (2004). (Pubitemid 38058263)
    • (2004) Experimental Cell Research , vol.292 , Issue.1 , pp. 51-66
    • Betanzos, A.1    Huerta, M.2    Lopez-Bayghen, E.3    Azuara, E.4    Amerena, J.5    Gonzalez-Mariscal, L.6
  • 68
    • 0029744106 scopus 로고    scopus 로고
    • The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts
    • DOI 10.1073/pnas.93.20.10779
    • Gottardi C. J., M. Arpin, A. S. Fanning and D. Louvard: The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cellcell contacts. Proc Natl Acad Sci U S A, 93, 10779-10784 (1996). (Pubitemid 26333066)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.20 , pp. 10779-10784
    • Gottardi, C.J.1    Arpin, M.2    Fanning, A.S.3    Louvard, D.4
  • 69
    • 0036343646 scopus 로고    scopus 로고
    • Nuclear localization of the tight junction protein ZO-2 in epithelial cells
    • Islas S., J. Vega, L. Ponce and L. Gonzalez-Mariscal: Nuclear localization of the tight junction protein ZO-2 in epithelial cells. Exp Cell Res, 274, 138-148 (2002).
    • (2002) Exp Cell Res , vol.274 , pp. 138-148
    • Islas, S.1    Vega, J.2    Ponce, L.3    Gonzalez-Mariscal, L.4
  • 71
    • 0037462794 scopus 로고    scopus 로고
    • The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B
    • DOI 10.1074/jbc.M206821200
    • Traweger A., R. Fuchs, I. A. Krizbai, T. M. Weiger, H. C. Bauer and H. Bauer: The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B. J Biol Chem, 278, 2692-2700 (2003). (Pubitemid 36801350)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.4 , pp. 2692-2700
    • Traweger, A.1    Fuchs, R.2    Krizbai, I.A.3    Weiger, T.M.4    Bauer, H.-C.5    Bauer, H.6
  • 72
    • 39849086633 scopus 로고    scopus 로고
    • Interactions of tight junctions with membrane channels and transporters
    • Rajasekaran S. A., K. W. Beyenbach and A. K. Rajasekaran: Interactions of tight junctions with membrane channels and transporters. Biochim Biophys Acta, 1778, 757-769 (2008).
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 757-769
    • Rajasekaran, S.A.1    Beyenbach, K.W.2    Rajasekaran, A.K.3
  • 73
    • 0022273197 scopus 로고
    • + gradient-coupled glucose transport as found in rabbit jejunal brush-border membrane vesicles
    • Crane R. K.: Comments and experiments on the kinetics of Na+ gradient-coupled glucose transport as found in rabbit jejunal brush-border membrane vesicles. Ann N Y Acad Sci, 456, 36-46 (1985). (Pubitemid 16110648)
    • (1985) Annals of the New York Academy of Sciences , vol.VOL. 456 , pp. 36-46
    • Crane, R.K.1
  • 74
    • 0024594966 scopus 로고
    • Membrane mechanisms in volume and pH regulation in vertebrate cells
    • Hoffmann E. K. and L. O. Simonsen: Membrane mechanisms in volume and pH regulation in vertebrate cells. Physiol Rev, 69, 315-382 (1989). (Pubitemid 19101664)
    • (1989) Physiological Reviews , vol.69 , Issue.2 , pp. 315-382
    • Hoffmann, E.K.1    Simonsen, L.O.2
  • 75
    • 0014867219 scopus 로고
    • Coupled transport of sodium and organic solutes
    • Schultz S. G. and P. F. Curran: Coupled transport of sodium and organic solutes. Physiol Rev, 50, 637-718 (1970).
    • (1970) Physiol Rev , vol.50 , pp. 637-718
    • Schultz, S.G.1    Curran, P.F.2
  • 76
    • 0022494153 scopus 로고
    • +)ATPase deduced from a cDNA
    • Shull G. E., L. K. Lane and J. B. Lingrel: Amino-acid sequence of the beta-subunit of the (Na+ + K+)ATPase deduced from a cDNA. Nature, 321, 429-431. (1986). (Pubitemid 16055493)
    • (1986) Nature , vol.321 , Issue.6068 , pp. 429-431
    • Shull, G.E.1    Lane, L.K.2    Lingrel, J.B.3
  • 77
    • 0022369722 scopus 로고
    • Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA
    • Shull G. E., A. Schwartz and J. B. Lingrel: Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA. Nature, 316, 691695. (1985).
    • (1985) Nature , vol.316 , pp. 691695
    • Shull, G.E.1    Schwartz, A.2    Lingrel, J.B.3
  • 78
    • 0039438642 scopus 로고    scopus 로고
    • The γ subunit is a specific component of the Na,K-ATPase and modulates its transport function
    • DOI 10.1093/emboj/16.14.4250
    • Beguin P., X. Wang, D. Firsov, A. Puoti, D. Claeys, J. D. Horisberger and K. Geering: The gamma subunit is a specific component of the Na, K-ATPase and modulates its transport function. Embo J, 16, 4250-4260 (1997). (Pubitemid 27298177)
    • (1997) EMBO Journal , vol.16 , Issue.14 , pp. 4250-4260
    • Beguin, P.1    Wang, X.2    Firsov, D.3    Puoti, A.4    Claeys, D.5    Horisberger, J.-D.6    Geering, K.7
  • 79
    • 33645984859 scopus 로고    scopus 로고
    • Role of FXYD proteins in ion transport
    • Garty H. and S. J. Karlish: Role of FXYD proteins in ion transport. Annu Rev Physiol, 68, 431-459 (2006).
    • (2006) Annu Rev Physiol , vol.68 , pp. 431-459
    • Garty, H.1    Karlish, S.J.2
  • 80
  • 81
    • 28644447041 scopus 로고    scopus 로고
    • Na,K-ATPase subunit heterogeneity as a mechanism for tissue-specific ion regulation
    • DOI 10.1016/j.semnephrol.2005.03.004, PII S0270929505000471, The Sodium-K ATPases
    • Blanco G.: Na, K-ATPase subunit heterogeneity as a mechanism for tissue-specific ion regulation. Semin Nephrol, 25, 292-303 (2005). (Pubitemid 41749411)
    • (2005) Seminars in Nephrology , vol.25 , Issue.5 , pp. 292-303
    • Blanco, G.1
  • 82
    • 21344467495 scopus 로고    scopus 로고
    • Regions conferring isoform-specific function in the catalytic subunit of the Na,K-pump
    • Pressley T. A., M. J. Duran and S. V. Pierre: Regions conferring isoform-specific function in the catalytic subunit of the Na, K-pump. Front Biosci, 10, 2018-2026 (2005). (Pubitemid 40905281)
    • (2005) Frontiers in Bioscience , vol.10 , Issue.SUPPL. 1 , pp. 2018-2026
    • Pressley, T.A.1    Duran, M.-J.2    Pierre, S.V.3
  • 85
    • 0025138388 scopus 로고
    • The adhesion molecule on glia (AMOG) is a homologue of the beta subunit of the Na, K-ATPase
    • Gloor S., H. Antonicek, K. J. Sweadner, S. Pagliusi, R. Frank, M. Moos and M. Schachner: The adhesion molecule on glia (AMOG) is a homologue of the beta subunit of the Na, K-ATPase. J Cell Biol, 110, 165-174 (1990).
    • (1990) J Cell Biol , vol.110 , pp. 165-174
    • Gloor, S.1    Antonicek, H.2    Sweadner, K.J.3    Pagliusi, S.4    Frank, R.5    Moos, M.6    Schachner, M.7
  • 87
    • 0024298721 scopus 로고
    • All three potential Nglycosylation sites of the dog kidney (Na+ + K+)-ATPase beta-subunit contain oligosaccharide
    • Miller R. P. and R. A. Farley: All three potential Nglycosylation sites of the dog kidney (Na+ + K+)-ATPase beta-subunit contain oligosaccharide. Biochim Biophys Acta, 954, 50-57 (1988).
    • (1988) Biochim Biophys Acta , vol.954 , pp. 50-57
    • Miller, R.P.1    Farley, R.A.2
  • 88
    • 0034773778 scopus 로고    scopus 로고
    • The functional role of β subunits in oligomeric P-type ATPases
    • DOI 10.1023/A:1010623724749
    • Geering K.: The functional role of beta subunits in oligomeric P-type ATPases. J Bioenerg Biomembr, 33, 425-438 (2001). (Pubitemid 32988630)
    • (2001) Journal of Bioenergetics and Biomembranes , vol.33 , Issue.5 , pp. 425-438
    • Geering, K.1
  • 89
    • 14844333249 scopus 로고    scopus 로고
    • +-ATPase in epithelia depends on the association between β-subunits located in neighboring cells
    • DOI 10.1091/mbc.E04-03-0267
    • Shoshani L., R. G. Contreras, M. L. Roldan, J. Moreno, A. Lazaro, M. S. Balda, K. Matter and M. Cereijido: The polarized expression of Na+, K+-ATPase in epithelia depends on the association between beta-subunits located in neighboring cells. Mol Biol Cell, 16, 1071-1081 (2005). (Pubitemid 40349546)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.3 , pp. 1071-1081
    • Shoshani, L.1    Contreras, R.G.2    Roldan, M.L.3    Moreno, J.4    Lazaro, A.5    Balda, M.S.6    Matter, K.7    Cereijido, M.8
  • 90
    • 33845984955 scopus 로고    scopus 로고
    • 1 subunit of the Na,K-ATPase and its glycosylation in cell-cell adhesion
    • DOI 10.1074/jbc.M606507200
    • Vagin O., E. Tokhtaeva and G. Sachs: The role of the beta1 subunit of the Na, K-ATPase and its glycosylation in cell-cell adhesion. J Biol Chem, 281, 39573-39587 (2006). (Pubitemid 46041917)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.51 , pp. 39573-39587
    • Vagin, O.1    Tokhtaeva, E.2    Sachs, G.3
  • 91
    • 0027236527 scopus 로고
    • An essential role for the extracellular domain of the Na,K-ATPase β- subunit in cation occlusion
    • Lutsenko S. and J. H. Kaplan: An essential role for the extracellular domain of the Na, K-ATPase beta-subunit in cation occlusion. Biochemistry, 32, 6737-6743 (1993). (Pubitemid 23217145)
    • (1993) Biochemistry , vol.32 , Issue.26 , pp. 6737-6743
    • Lutsenko, S.1    Kaplan, J.H.2
  • 92
    • 33845661568 scopus 로고    scopus 로고
    • Janus Model of The Na,K-ATPase β-Subunit Transmembrane Domain: Distinct Faces Mediate α/β Assembly and β-β Homo-oligomerization
    • DOI 10.1016/j.jmb.2006.10.029, PII S0022283606013672
    • Barwe S. P., S. Kim, S. A. Rajasekaran, J. U. Bowie and A. K. Rajasekaran: Janus model of the Na, K-ATPase beta-subunit transmembrane domain: distinct faces mediate alpha/beta assembly and beta-beta homo-oligomerization. J Mol Biol, 365, 706-714 (2007). (Pubitemid 44960357)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.3 , pp. 706-714
    • Barwe, S.P.1    Kim, S.2    Rajasekaran, S.A.3    Bowie, J.U.4    Rajasekaran, A.K.5
  • 93
    • 0037093544 scopus 로고    scopus 로고
    • +-ATPase
    • Ivanov A. V., N. N. Modyanov and A. Askari: Role of the self-association of beta subunits in the oligomeric structure of Na+/K+-ATPase. Biochem J, 364, 293-299 (2002). (Pubitemid 34538973)
    • (2002) Biochemical Journal , vol.364 , Issue.1 , pp. 293-299
    • Ivanov, A.V.1    Modyanov, N.N.2    Askari, A.3
  • 94
    • 0027281005 scopus 로고
    • Molecular cloning and immunological characterization of the γ polypeptide, a small protein associated with the Na,K-ATPase
    • Mercer R. W., D. Biemesderfer, D. P. Bliss Jr., J. H. Collins and B. Forbush, 3rd: Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na, K-ATPase. J Cell Biol, 121, 579-586 (1993). (Pubitemid 23131269)
    • (1993) Journal of Cell Biology , vol.121 , Issue.3 , pp. 579-586
    • Mercer, R.W.1    Biemesderfer, D.2    Bliss Jr., D.P.3    Collins, J.H.4    Forbush III, B.5
  • 96
    • 34547937490 scopus 로고    scopus 로고
    • Dysadherin: A new player in cancer progression
    • DOI 10.1016/j.canlet.2007.02.018, PII S0304383507000869
    • Nam J.-S., S. Hirohashi and L. M. Wakefield: Dysadherin: A new player in cancer progression. Cancer Letters, 255, 161-169 (2007). (Pubitemid 47268636)
    • (2007) Cancer Letters , vol.255 , Issue.2 , pp. 161-169
    • Nam, J.-S.1    Hirohashi, S.2    Wakefield, L.M.3
  • 99
    • 38349112106 scopus 로고    scopus 로고
    • Regulation of Na, K-ATPase during acute lung injury
    • Lecuona E., H. E. Trejo and J. I. Sznajder: Regulation of Na, K-ATPase during acute lung injury. J Bioenerg Biomembr, 39, 391-395 (2007).
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 391-395
    • Lecuona, E.1    Trejo, H.E.2    Sznajder, J.I.3
  • 100
    • 0035550517 scopus 로고    scopus 로고
    • Interaction of Na,K-ATPase catalytic subunit with cellular proteins and other endogenous regulators
    • DOI 10.1023/A:1012432913689
    • Lopina O. D.: Interaction of Na, K-ATPase catalytic subunit with cellular proteins and other endogenous regulators. Biochemistry (Mosc), 66, 1122-1131 (2001). (Pubitemid 33099914)
    • (2001) Biochemistry (Moscow) , vol.66 , Issue.10 , pp. 1122-1131
    • Lopina, O.D.1
  • 101
    • 38049125804 scopus 로고    scopus 로고
    • Phosphorylation of phospholemman (FXYD1) by protein kinases A and C modulates distinct Na, K-ATPase isozymes
    • Bibert S., S. Roy, D. Schaer, J. D. Horisberger and K. Geering: Phosphorylation of phospholemman (FXYD1) by protein kinases A and C modulates distinct Na, K-ATPase isozymes. J Biol Chem, 283, 476-486 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 476-486
    • Bibert, S.1    Roy, S.2    Schaer, D.3    Horisberger, J.D.4    Geering, K.5
  • 103
    • 0023262074 scopus 로고
    • +)ATPase and implications for the organization of membrane domains in polarized cells
    • DOI 10.1038/328533a0
    • Nelson W. J. and P. J. Veshnock: Ankyrin binding to (Na+ + K+)ATPase and implications for the organization of membrane domains in polarized cells. Nature, 328, 533-536 (1987). (Pubitemid 17098355)
    • (1987) Nature , vol.328 , Issue.6130 , pp. 533-536
    • Nelson, W.J.1    Veshnock, P.J.2
  • 104
    • 0035863252 scopus 로고    scopus 로고
    • Interaction of the α subunit of Na,K-ATPase with, cofilin
    • DOI 10.1042/0264-6021:3530377
    • Lee K., J. Jung, M. Kim and G. Guidotti: Interaction of the alpha subunit of Na, K-ATPase with cofilin. Biochem J, 353, 377-385 (2001). (Pubitemid 32096948)
    • (2001) Biochemical Journal , vol.353 , Issue.2 , pp. 377-385
    • Lee, K.1    Jung, J.2    Kim, M.3    Guidotti, G.4
  • 105
    • 35848934128 scopus 로고    scopus 로고
    • +-ATPase
    • DOI 10.1091/mbc.E06-08-0711
    • Kimura T., P. B. Allen, A. C. Nairn and M. J. Caplan: Arrestins and spinophilin competitively regulate Na+, K+-ATPase trafficking through association with a large cytoplasmic loop of the Na+, K+-ATPase. Mol Biol Cell, 18, 4508-4518 (2007). (Pubitemid 350060177)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.11 , pp. 4508-4518
    • Kimura, T.1    Allen, P.B.2    Nairn, A.C.3    Caplan, M.J.4
  • 108
    • 27644588398 scopus 로고    scopus 로고
    • The C-terminal tail of the polycystin-1 protein interacts with the Na,K-ATPase α-subunit
    • DOI 10.1091/mbc.E05-03-0200
    • Zatti A, V. Chauvet, V. Rajendran, T. Kimura, P. Pagel and M. J. Caplan: The C-terminal tail of the polycystin-1 protein interacts with the Na, K-ATPase alphasubunit. Mol Biol Cell, 16, 5087-5093 (2005). (Pubitemid 41566822)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.11 , pp. 5087-5093
    • Zatti, A.1    Chauvet, V.2    Rajendran, V.3    Kimura, T.4    Pagel, P.5    Caplan, M.J.6
  • 111
    • 24344485458 scopus 로고    scopus 로고
    • Na/K-ATPase tethers phospholipase C and IP3 receptor into a calcium-regulatory complex
    • DOI 10.1091/mbc.E05-04-0295
    • Yuan Z., T. Cai, J. Tian, A. V. Ivanov, D. R. Giovannucci and Z. Xie: Na/K-ATPase tethers phospholipase C and IP3 receptor into a calcium-regulatory complex. Mol Biol Cell, 16, 4034-4045 (2005). (Pubitemid 41262876)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.9 , pp. 4034-4045
    • Yuan, Z.1    Cai, T.2    Tian, J.3    Ivanov, A.V.4    Giovannucci, D.R.5    Xie, Z.6
  • 113
    • 36348932053 scopus 로고    scopus 로고
    • Retinoschisin (RS1), the protein encoded by the X-linked retinoschisis gene, is anchored to the surface of retinal photoreceptor and bipolar cells through its interactions with a Na/K ATPase-SARM1 complex
    • DOI 10.1074/jbc.M706321200
    • Molday L. L., W. W. Wu and R. S. Molday: Retinoschisin (RS1), the protein encoded by the X-linked retinoschisis gene, is anchored to the surface of retinal photoreceptor and bipolar cells through its interactions with a Na/K ATPase-SARM1 complex. J Biol Chem, 282, 32792-32801 (2007). (Pubitemid 350159297)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.45 , pp. 32792-32801
    • Molday, L.L.1    Wu, W.W.H.2    Molday, R.S.3
  • 115
    • 0026803103 scopus 로고
    • A role for the Na/K-ATPase in the control of human c-fos and c-jun transcription
    • Nakagawa Y., V. Rivera and A. C. Larner: A role for the Na/K-ATPase in the control of human c-fos and c-jun transcription. J Biol Chem, 267, 8785-8788 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 8785-8788
    • Nakagawa, Y.1    Rivera, V.2    Larner, A.C.3
  • 116
    • 0030011972 scopus 로고    scopus 로고
    • Partial inhibition of Na+/K+-ATPase by ouabain induces the Ca2+-dependent expressions of early-response genes in cardiac myocytes
    • Peng M., L. Huang, Z. Xie, W. H. Huang and A. Askari: Partial inhibition of Na+/K+-ATPase by ouabain induces the Ca2+-dependent expressions of early-response genes in cardiac myocytes. J Biol Chem, 271, 10372-10378 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 10372-10378
    • Peng, M.1    Huang, L.2    Xie, Z.3    Huang, W.H.4    Askari, A.5
  • 117
    • 0032511095 scopus 로고    scopus 로고
    • +-ATPase to growth- related genes in cardiac myocytes: The roles of Ras and mitogen-activated protein kinases
    • DOI 10.1074/jbc.273.24.15249
    • Kometiani P., J. Li, L. Gnudi, B. B. Kahn, A. Askari and Z. Xie: Multiple signal transduction pathways link Na+/K+-ATPase to growth-related genes in cardiac myocytes. The roles of Ras and mitogen-activated protein kinases. J Biol Chem, 273, 15249-15256 (1998). (Pubitemid 28272826)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.24 , pp. 15249-15256
    • Kometiani, P.1    Li, J.2    Gnudi, L.3    Kahn, B.B.4    Askari, A.5    Xie, Z.6
  • 118
    • 0034623045 scopus 로고    scopus 로고
    • Involvement of Src and epidermal growth factor receptor in the signal-transducing function of Na+/K+-ATPase
    • Haas M., A. Askari and Z. Xie: Involvement of Src and epidermal growth factor receptor in the signal-transducing function of Na+/K+-ATPase. J. Biol. Chem., 275, 27832-27837 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 27832-27837
    • Haas, M.1    Askari, A.2    Xie, Z.3
  • 119
    • 0037166251 scopus 로고    scopus 로고
    • +-ATPase and the epidermal growth factor receptor relays the signal from ouabain to mitogen-activated protein kinases
    • DOI 10.1074/jbc.M111357200
    • Haas M., H. Wang, J. Tian and Z. Xie: Src-mediated inter-receptor cross-talk between the Na+/K+-ATPase and the epidermal growth factor receptor relays the signal from ouabain to mitogen-activated protein kinases. J Biol Chem, 277, 18694-18702 (2002). (Pubitemid 34952426)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.21 , pp. 18694-18702
    • Haas, M.1    Wang, H.2    Tian, J.3    Xie, Z.4
  • 120
    • 33846783324 scopus 로고    scopus 로고
    • The Na, K-ATPase receptor complex: Its organization and membership
    • Pierre S. V. and Z. Xie: The Na, K-ATPase receptor complex: its organization and membership. Cell Biochem Biophys, 46, 303-36 (2006).
    • (2006) Cell Biochem Biophys , vol.46 , pp. 303-336
    • Pierre, S.V.1    Xie, Z.2
  • 121
    • 3042805201 scopus 로고    scopus 로고
    • Ouabain induces endocytosis of plasmalemmal Na/K-ATPase in LLC-PK1 cells by a clathrin-dependent mechanism
    • DOI 10.1111/j.1523-1755.2004.00723.x
    • Liu J., R. Kesiry, S. M. Periyasamy, D. Malhotra, Z. Xie and J. I. Shapiro: Ouabain induces endocytosis of plasmalemmal Na/K-ATPase in LLC-PK1 cells by a clathrin-dependent mechanism. Kidney Int, 66, 227-241 (2004). (Pubitemid 38870098)
    • (2004) Kidney International , vol.66 , Issue.1 , pp. 227-241
    • Liu, J.1    Kesiry, R.2    Periyasamy, S.M.3    Malhotra, D.4    Xie, Z.5    Shapiro, J.I.6
  • 124
    • 11144243671 scopus 로고    scopus 로고
    • The α1 isoform of Na,K-ATPase regulates cardiac contractility and functionally interacts and co-localizes with the Na/Ca exchanger in heart
    • DOI 10.1074/jbc.M410737200
    • Dostanic I., J. Schultz Jel, J. N. Lorenz and J. B. Lingrel: The alpha 1 isoform of Na, K-ATPase regulates cardiac contractility and functionally interacts and colocalizes with the Na/Ca exchanger in heart. J Biol Chem, 279, 54053-54061 (2004). (Pubitemid 40053139)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.52 , pp. 54053-54061
    • Dostanic, I.1    Schultz, J.E.J.2    Lorenz, J.N.3    Lingrel, J.B.4
  • 125
    • 0035204822 scopus 로고    scopus 로고
    • Signal-transducing function of Na+-K+-ATPase is essential for ouabain's effect on (Ca2+)i in rat cardiac myocytes
    • Tian J., X. Gong and Z. Xie: Signal-transducing function of Na+-K+-ATPase is essential for ouabain's effect on (Ca2+)i in rat cardiac myocytes. Am J Physiol Heart Circ Physiol, 281, H1899-H1907 (2001).
    • (2001) Am J Physiol Heart Circ Physiol , vol.281
    • Tian, J.1    Gong, X.2    Xie, Z.3
  • 126
    • 0033516649 scopus 로고    scopus 로고
    • Intracellular reactive oxygen species mediate the linkage of Na+/K+-ATPase to hypertrophy and its marker genes in cardiac myocytes
    • Xie Z., P. Kometiani, J. Liu, J. Li, J. I. Shapiro and A. Askari: Intracellular reactive oxygen species mediate the linkage of Na+/K+-ATPase to hypertrophy and its marker genes in cardiac myocytes. J Biol Chem, 274, 19323-19328 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 19323-19328
    • Xie, Z.1    Kometiani, P.2    Liu, J.3    Li, J.4    Shapiro, J.I.5    Askari, A.6
  • 130
    • 0024383791 scopus 로고
    • Dissecting tumor cell invasion: Epithelial cells acquire invasive properties after the loss of uvomorulin-mediated cell-cell adhesion
    • Behrens J., M. M. Mareel, F. M. Van Roy and W. Birchmeier: Dissecting tumor cell invasion: epithelial cells acquire invasive properties after the loss of uvomorulin-mediated cell-cell adhesion. J. Cell Biol., 108, 2435-2447 (1989). (Pubitemid 19168932)
    • (1989) Journal of Cell Biology , vol.108 , Issue.6 , pp. 2435-2447
    • Behrens, J.1    Mareel, M.M.2    Van Roy, F.M.3    Birchmeier, W.4
  • 132
    • 0032514134 scopus 로고    scopus 로고
    • Structural and functional regulation of tight junctions by RhoA and Rac1 small GTPases
    • DOI 10.1083/jcb.142.1.101
    • Jou T.-S., E. E. Schneeberger and W. James Nelson: Structural and functional regulation of tight junctions by RhoA and Rac1 small GTPases. J. Cell Biol., 142, 101-115 (1998). (Pubitemid 28341143)
    • (1998) Journal of Cell Biology , vol.142 , Issue.1 , pp. 101-115
    • Jou, T.-S.1    Schneeberger, E.E.2    Nelson, W.J.3
  • 134
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells
    • DOI 10.1083/jcb.139.4.1047
    • Takaishi K., T. Sasaki, H. Kotani, H. Nishioka and Y. Takai: Regulation of cell-cell adhesion by Rac and Rho Small G proteins in MDCK Cells. J. Cell Biol., 139, 1047-1059 (1997). (Pubitemid 27508574)
    • (1997) Journal of Cell Biology , vol.139 , Issue.4 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 136
    • 0023678998 scopus 로고
    • Mammalian blastocyst: Transport functions in a developing epithelium
    • Biggers J. D., J. E. Bell and D. J. Benos: Mammalian blastocyst: transport functions in a developing epithelium. Am J Physiol, 255, C419-432 (1988).
    • (1988) Am J Physiol , vol.255
    • Biggers, J.D.1    Bell, J.E.2    Benos, D.J.3
  • 137
    • 0000170879 scopus 로고
    • Development of the blastocyst: Role of cell polarity in cavitation and cell differentiation
    • Ed B. Bavister. Plenum Publishing Co. New York
    • Wiley L.: Development of the blastocyst: role of cell polarity in cavitation and cell differentiation. In: The Mammalian Preimplantation Embryo: Regulation of Growth and Differentiation in vitro. Ed B. Bavister. Plenum Publishing Co., New York (1987).
    • (1987) Mammalian Preimplantation Embryo: Regulation of Growth and Differentiation in Vitro
    • Wiley, L.1
  • 138
    • 0023518424 scopus 로고
    • Expression and distribution of cell adhesion molecule uvomorulin in mouse preimplantation embryos
    • DOI 10.1016/0012-1606(87)90498-2
    • Vestweber D., A. Gossler, K. Boller and R. Kemler: Expression and distribution of cell adhesion molecule uvomorulin in mouse preimplantation embryos. Dev Biol, 124, 451-456 (1987). (Pubitemid 18003719)
    • (1987) Developmental Biology , vol.124 , Issue.2 , pp. 451-456
    • Vestweber, D.1    Gossler, A.2    Boller, K.3    Kemler, R.4
  • 139
    • 3543102129 scopus 로고    scopus 로고
    • Molecular regulation of blastocyst formation
    • DOI 10.1016/j.anireprosci.2004.04.004, PII S0378432004000569
    • Watson A. J., D. R. Natale and L. C. Barcroft: Molecular regulation of blastocyst formation. Anim Reprod Sci, 82-83, 583-592 (2004). (Pubitemid 39027086)
    • (2004) Animal Reproduction Science , vol.82-83 , pp. 583-592
    • Watson, A.J.1    Natale, D.R.2    Barcroft, L.C.3
  • 140
    • 36549003561 scopus 로고    scopus 로고
    • Tight junctions containing claudin 4 and 6 are essential for blastocyst formation in preimplantation mouse embryos
    • DOI 10.1016/j.ydbio.2007.09.049, PII S0012160607013991
    • Moriwaki K., S. Tsukita and M. Furuse: Tight junctions containing claudin 4 and 6 are essential for blastocyst formation in preimplantation mouse embryos. Dev Biol, 312, 509-522 (2007). (Pubitemid 350183973)
    • (2007) Developmental Biology , vol.312 , Issue.2 , pp. 509-522
    • Moriwaki, K.1    Tsukita, S.2    Furuse, M.3
  • 141
    • 0035350690 scopus 로고    scopus 로고
    • Regulation of blastocyst formation
    • Watson A. J. and L. C. Barcroft: Regulation of blastocyst formation. Front Biosci, 6, D708-730 (2001).
    • (2001) Front Biosci , vol.6
    • Watson, A.J.1    Barcroft, L.C.2
  • 142
    • 2442495047 scopus 로고    scopus 로고
    • Deletion of the Na/K-ATPase α1-subunit gene (Atp1a1) does not prevent cavitation of the preimplantation mouse embryo
    • DOI 10.1016/j.mod.2004.04.005, PII S0925477304000863
    • Barcroft L. C., A. E. Moseley, J. B. Lingrel and A. J. Watson: Deletion of the Na/K-ATPase alpha1-subunit gene (Atp1a1) does not prevent cavitation of the preimplantation mouse embryo. Mech Dev, 121, 417-426 (2004). (Pubitemid 38624537)
    • (2004) Mechanisms of Development , vol.121 , Issue.5 , pp. 417-426
    • Barcroft, L.C.1    Moseley, A.E.2    Lingrel, J.B.3    Watson, A.J.4
  • 143
    • 30044440094 scopus 로고    scopus 로고
    • +-ATPase regulates tight junction formation and function during mouse preimplantation development
    • DOI 10.1016/j.ydbio.2005.11.004, PII S0012160605007761
    • Violette M. I., P. Madan and A. J. Watson: Na+/K+ - ATPase regulates tight junction formation and function during mouse preimplantation development. Dev Biol, 289, 406-419 (2006). (Pubitemid 43049943)
    • (2006) Developmental Biology , vol.289 , Issue.2 , pp. 406-419
    • Violette, M.I.1    Madan, P.2    Watson, A.J.3
  • 144
    • 34249708977 scopus 로고    scopus 로고
    • Na/K-ATPase β1 subunit expression is required for blastocyst formation and normal assembly of trophectoderm tight junction-associated proteins
    • DOI 10.1074/jbc.M700696200
    • Madan P., K. Rose and A. J. Watson: Na/K-ATPase beta1 subunit expression is required for blastocyst formation and normal assembly of trophectoderm tight junction-associated proteins. J Biol Chem, 282, 12127-12134 (2007). (Pubitemid 47100727)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.16 , pp. 12127-12134
    • Madan, P.1    Rose, K.2    Watson, A.J.3
  • 145
    • 4644264088 scopus 로고    scopus 로고
    • Specific PKC isoforms regulate blastocoel formation during mouse preimplantation development
    • DOI 10.1016/j.ydbio.2004.07.027, PII S0012160604005019
    • Eckert J. J., A. McCallum, A. Mears, M. G. Rumsby, I. T. Cameron and T. P. Fleming: Specific PKC isoforms regulate blastocoel formation during mouse preimplantation development. Dev Biol, 274, 384-401 (2004). (Pubitemid 39295728)
    • (2004) Developmental Biology , vol.274 , Issue.2 , pp. 384-401
    • Eckert, J.J.1    McCallum, A.2    Mears, A.3    Rumsby, M.G.4    Cameron, I.T.5    Fleming, T.P.6
  • 146
    • 4644308410 scopus 로고    scopus 로고
    • Cloning, mapping, and developmental expression of a sixth zebrafish Na,K-ATPase α1 subunit gene (atp1a1a.5)
    • DOI 10.1016/S0925-4773(03)00118-7, PII S0925477303001187
    • Blasiole B., V. Canfield, A. Degrave, C. Thisse, B. Thisse, J. Rajarao and R. Levenson: Cloning, mapping, and developmental expression of a sixth zebrafish Na, K-ATPase alpha1 subunit gene (atp1a1a.5). Mech Dev, 119 Suppl 1, S211-214 (2002). (Pubitemid 39658712)
    • (2002) Mechanisms of Development , vol.119 , Issue.SUPPL. 1
    • Blasiole, B.1    Canfield, V.2    Degrave, A.3    Thisse, C.4    Thisse, B.5    Rajarao, J.6    Levenson, R.7
  • 148
    • 0036158180 scopus 로고    scopus 로고
    • Two Na,K-ATPase β2 subunit isoforms are differentially expressed within the central nervous system and sensory organs during zebrafish embryogenesis
    • DOI 10.1002/dvdy.10045
    • Rajarao J. R., V. A. Canfield, B. Loppin, B. Thisse, C. Thisse, Y. L. Yan, J. H. Postlethwait and R. Levenson: Two Na, K-ATPase beta 2 subunit isoforms are differentially expressed within the central nervous system and sensory organs during zebrafish embryogenesis. Dev Dyn, 223, 254-261 (2002). (Pubitemid 34113403)
    • (2002) Developmental Dynamics , vol.223 , Issue.2 , pp. 254-261
    • Rajarao, J.R.1    Canfield, V.A.2    Loppin, B.3    Thisse, B.4    Thisse, C.5    Yan, Y.-L.6    Postlethwait, J.H.7    Levenson, R.8
  • 150
    • 0026776131 scopus 로고
    • Patterning the zebrafish heart tube: Acquisition of anteroposterior polarity
    • Stainier D. Y. and M. C. Fishman: Patterning the zebrafish heart tube: acquisition of anteroposterior polarity. Dev Biol, 153, 91-101 (1992).
    • (1992) Dev Biol , vol.153 , pp. 91-101
    • Stainier, D.Y.1    Fishman, M.C.2
  • 151
    • 0035209808 scopus 로고    scopus 로고
    • Cardiac patterning and morphogenesis in zebrafish
    • DOI 10.1002/dvdy.1243
    • Yelon D.: Cardiac patterning and morphogenesis in zebrafish. Dev Dyn, 222, 552-563 (2001). (Pubitemid 33136327)
    • (2001) Developmental Dynamics , vol.222 , Issue.4 , pp. 552-563
    • Yelon, D.1
  • 152
    • 0033215267 scopus 로고    scopus 로고
    • Restricted expression of cardiac myosin genes reveals regulated aspects of heart tube assembly in zebrafish
    • DOI 10.1006/dbio.1999.9406
    • Yelon D., S. A. Horne and D. Y. Stainier: Restricted expression of cardiac myosin genes reveals regulated aspects of heart tube assembly in zebrafish. Dev Biol, 214, 23-37 (1999). (Pubitemid 29463353)
    • (1999) Developmental Biology , vol.214 , Issue.1 , pp. 23-37
    • Yelon, D.1    Horne, S.A.2    Stainier, D.Y.R.3
  • 153
    • 0347288573 scopus 로고    scopus 로고
    • Na,K-ATPase is essential for embryonic heart development in the zebrafish
    • DOI 10.1242/dev.00844
    • Shu X., K. Cheng, N. Patel, F. Chen, E. Joseph, H. J. Tsai and J. N. Chen: Na, K-ATPase is essential for embryonic heart development in the zebrafish. Development, 130, 6165-6173 (2003). (Pubitemid 38008816)
    • (2003) Development , vol.130 , Issue.25 , pp. 6165-6173
    • Shu, X.1    Cheng, K.2    Patel, N.3    Chen, F.4    Joseph, E.5    Tsai, H.-J.6    Chen, J.-N.7
  • 156
    • 0035797939 scopus 로고    scopus 로고
    • Convergence of distinct pathways to heart patterning revealed by the small molecule concentramide and the mutation heart-and-soul
    • DOI 10.1016/S0960-9822(01)00482-1
    • Peterson R. T., J. D. Mably, J. N. Chen and M. C. Fishman: Convergence of distinct pathways to heart patterning revealed by the small molecule concentramide and the mutation heart-and-soul. Curr Biol, 11, 1481-1491 (2001). (Pubitemid 32931009)
    • (2001) Current Biology , vol.11 , Issue.19 , pp. 1481-1491
    • Peterson, R.T.1    Mably, J.D.2    Chen, J.-N.3    Fishman, M.C.4
  • 157
    • 31644435347 scopus 로고    scopus 로고
    • Heart and soul/PRKCi and nagie oko/Mpp5 regulate myocardial coherence and remodeling during cardiac morphogenesis
    • DOI 10.1242/dev.02182
    • Rohr S., N. Bit-Avragim and S. Abdelilah-Seyfried: Heart and soul/PRKCi and nagie oko/Mpp5 regulate myocardial coherence and remodeling during cardiac morphogenesis. Development, 133, 107-115 (2006). (Pubitemid 43169325)
    • (2006) Development , vol.133 , Issue.1 , pp. 107-115
    • Rohr, S.1    Bit-Avragim, N.2    Abdelilah-Seyfried, S.3
  • 158
    • 34547576923 scopus 로고    scopus 로고
    • Genetic control of single lumen formation in the zebrafish gut
    • DOI 10.1038/ncb1621, PII NCB1621
    • Bagnat M., I. D. Cheung, K. E. Mostov and D. Y. Stainier: Genetic control of single lumen formation in the zebrafish gut. Nat Cell Biol, 9, 954-960 (2007). (Pubitemid 47190450)
    • (2007) Nature Cell Biology , vol.9 , Issue.8 , pp. 954-960
    • Bagnat, M.1    Cheung, I.D.2    Mostov, K.E.3    Stainier, D.Y.R.4
  • 159
    • 0020394307 scopus 로고
    • The ultrastructure of the larval malpighian tubules of a saline-water mosquito
    • Bradley T. J., A. M. Stuart and P. Satir: The ultrastructure of the larval malpighian tubules of a saline-water mosquito. Tissue Cell, 14, 759-773 (1982).
    • (1982) Tissue Cell , vol.14 , pp. 759-773
    • Bradley, T.J.1    Stuart, A.M.2    Satir, P.3
  • 160
    • 4444352406 scopus 로고    scopus 로고
    • A junctional problem of apical proportions: Epithelial tube-size control by septate junctions in the Drosophila tracheal system
    • DOI 10.1016/j.ceb.2004.07.008, PII S0955067404001073
    • Wu V. M. and G. J. Beitel: A junctional problem of apical proportions: epithelial tube-size control by septate junctions in the Drosophila tracheal system. Curr Opin Cell Biol, 16, 493-499 (2004). (Pubitemid 39201233)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.5 , pp. 493-499
    • Wu, V.M.1    Beitel, G.J.2
  • 161
    • 0038457822 scopus 로고    scopus 로고
    • + ATPase are essential for septate junction function in Drosophila
    • DOI 10.1083/jcb.200212054
    • Genova J. L. and R. G. Fehon: Neuroglian, Gliotactin, and the Na+/K+ ATPase are essential for septate junction function in Drosophila. J Cell Biol, 161, 979-989 (2003). (Pubitemid 36718430)
    • (2003) Journal of Cell Biology , vol.161 , Issue.5 , pp. 979-989
    • Genova, J.L.1    Fehon, R.G.2
  • 162
    • 33846471264 scopus 로고    scopus 로고
    • A pump-independent function of the Na,K-ATPase is required for epithelial junction and tracheal tube-size control
    • DOI 10.1242/dev.02710
    • Paul S. M., M. J. Palladino and G. J. Beitel: A pumpindependent function of the Na, K-ATPase is required for epithelial junction function and tracheal tube-size control. Development, 134, 147-155 (2007). (Pubitemid 46152715)
    • (2007) Development , vol.134 , Issue.1 , pp. 147-155
    • Paul, S.M.1    Palladino, M.J.2    Beitel, G.J.3
  • 163
    • 0141891960 scopus 로고    scopus 로고
    • + ATPase is required for septate junction function and epithelial tube-size control in the Drosophila tracheal system
    • DOI 10.1242/dev.00691
    • Paul S. M., M. Ternet, P. M. Salvaterra and G. J. Beitel: The Na+/K+ ATPase is required for septate junction function and epithelial tube-size control in the Drosophila tracheal system. Development, 130, 4963-4974 (2003). (Pubitemid 37321878)
    • (2003) Development , vol.130 , Issue.20 , pp. 4963-4974
    • Paul, S.M.1    Ternet, M.2    Salvaterra, P.M.3    Beitel, G.J.4
  • 164
    • 0037442821 scopus 로고    scopus 로고
    • + ATPase alpha subunit mutants
    • Palladino M. J., J. E. Bower, R. Kreber and B. Ganetzky: Neural dysfunction and neurodegeneration in Drosophila Na+/K+ ATPase alpha subunit mutants. J Neurosci, 23, 1276-1286 (2003). (Pubitemid 36258906)
    • (2003) Journal of Neuroscience , vol.23 , Issue.4 , pp. 1276-1286
    • Palladino, M.J.1    Bower, J.E.2    Kreber, R.3    Ganetzky, B.4
  • 165
    • 12844282801 scopus 로고    scopus 로고
    • Fractionation of the epithelial apical junctional complex: Reassessment of protein distributions in different substructures
    • DOI 10.1091/mbc.E04-09-0827
    • Vogelmann R. and W. J. Nelson: Fractionation of the epithelial apical junctional complex: reassessment of protein distributions in different substructures. Mol Biol Cell, 16, 701-716 (2005). (Pubitemid 40165566)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.2 , pp. 701-716
    • Vogelmann, R.1    Nelson, W.J.2
  • 167
    • 0038106252 scopus 로고    scopus 로고
    • The type 3 inositol 1,4,5-trisphosphate receptor is concentrated at the tight junction level in polarized MDCK cells
    • DOI 10.1242/jcs.00482
    • Colosetti P., R. E. Tunwell, C. Cruttwell, J. P. Arsanto, J. P. Mauger and D. Cassio: The type 3 inositol 1, 4, 5-trisphosphate receptor is concentrated at the tight junction level in polarized MDCK cells. J Cell Sci, 116, 2791-2803 (2003). (Pubitemid 36857230)
    • (2003) Journal of Cell Science , vol.116 , Issue.13 , pp. 2791-2803
    • Colosetti, P.1    Tunwell, R.E.A.2    Cruttwell, C.3    Arsanto, J.-P.4    Mauger, J.-P.5    Cassio, D.6
  • 168
    • 13244260780 scopus 로고    scopus 로고
    • Ra1A interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity
    • DOI 10.1038/sj.emboj.7600497
    • Frankel P., A. Aronheim, E. Kavanagh, M. S. Balda, K. Matter, T. D. Bunney and C. J. Marshall: RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity. EMBO J, 24, 54-62 (2005). (Pubitemid 40188463)
    • (2005) EMBO Journal , vol.24 , Issue.1 , pp. 54-62
    • Frankel, P.1    Aronheim, A.2    Kavanagh, E.3    Balda, M.S.4    Matter, K.5    Bunney, T.D.6    Marshall, C.J.7
  • 169
    • 38349191968 scopus 로고    scopus 로고
    • Inverse correlation between the extent of Nglycan branching and intercellular adhesion in epithelia. Contribution of the Na, K-ATPase beta1 subunit
    • Vagin O., E. Tokhtaeva, I. Yakubov, E. Shevchenko and G. Sachs: Inverse correlation between the extent of Nglycan branching and intercellular adhesion in epithelia. Contribution of the Na, K-ATPase beta1 subunit. J Biol Chem, 283, 2192-2202 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 2192-2202
    • Vagin, O.1    Tokhtaeva, E.2    Yakubov, I.3    Shevchenko, E.4    Sachs, G.5
  • 170
    • 0023273938 scopus 로고
    • Biochemical and functional characterization of a novel neuron-glia adhesion molecule that is involved in neuronal migration
    • DOI 10.1083/jcb.104.6.1587
    • Antonicek H., E. Persohn and M. Schachner: Biochemical and functional characterization of a novel neuron-glia adhesion molecule that is involved in neuronal migration. J Cell Biol, 104, 1587-1595 (1987). (Pubitemid 17104528)
    • (1987) Journal of Cell Biology , vol.104 , Issue.6 , pp. 1587-1595
    • Antonicek, H.1    Persohn, E.2    Schachner, M.3
  • 171
    • 0027156375 scopus 로고
    • Structures of the complex glycans found on the β-subunit of (Na,K)- ATPase
    • Treuheit M. J., C. E. Costello and T. L. Kirley: Structures of the complex glycans found on the beta-subunit of (Na, K)-ATPase. J Biol Chem, 268, 13914-13919 (1993). (Pubitemid 23195504)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.19 , pp. 13914-13919
    • Treuheit, M.J.1    Costello, C.E.2    Kirley, T.L.3
  • 173
    • 38349136271 scopus 로고    scopus 로고
    • The roles of the Na, K-ATPase beta 1 subunit in pump sorting and epithelial integrity
    • Vagin O., G. Sachs and E. Tokhtaeva: The roles of the Na, K-ATPase beta 1 subunit in pump sorting and epithelial integrity. J Bioenerg Biomembr, 39, 367-372 (2007).
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 367-372
    • Vagin, O.1    Sachs, G.2    Tokhtaeva, E.3
  • 175
    • 2342487353 scopus 로고    scopus 로고
    • Na+-K+-ATPase-mediated signal transduction: From protein interaction to cellular function
    • Xie Z. and T. Cai: Na+-K+-ATPase-mediated signal transduction: from protein interaction to cellular function. Mol Interv, 3, 157-168 (2003).
    • (2003) Mol Interv , vol.3 , pp. 157-168
    • Xie, Z.1    Cai, T.2
  • 176
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley A. J. and A. Hall: The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell, 70, 389-399 (1992).
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 179
    • 0038146915 scopus 로고    scopus 로고
    • Expression of kinase-inactive c-Src delays oxidative stress-induced disassembly and accelerates calcium-mediated reassembly of tight junctions in the Caco-2 cell monolayer
    • DOI 10.1074/jbc.M211710200
    • Basuroy S., P. Sheth, D. Kuppuswamy, S. Balasubramanian, R. M. Ray and R. K. Rao: Expression of kinase-inactive c-Src delays oxidative stress-induced disassembly and accelerates calcium-mediated reassembly of tight junctions in the Caco-2 cell monolayer. J Biol Chem, 278, 11916-11924 (2003). (Pubitemid 36800164)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 11916-11924
    • Basuroy, S.1    Sheth, P.2    Kuppuswamy, D.3    Balasubramanian, S.4    Ray, R.M.5    Rao, R.K.6
  • 180
    • 0034099223 scopus 로고    scopus 로고
    • Restoration of tight junction structure and barrier function by down- regulation of the mitogen-activated protein kinase pathway in Ras-transformed Madin-Darby canine kidney cells
    • Chen Y., Q. Lu, E. E. Schneeberger and D. A. Goodenough: Restoration of tight junction structure and barrier function by down-regulation of the mitogen-activated protein kinase pathway in ras-transformed Madin-Darby canine kidney cells. Mol Biol Cell, 11, 849-862 (2000). (Pubitemid 30159306)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.3 , pp. 849-862
    • Chen, Y.-H.1    Lu, Q.2    Schneeberger, E.E.3    Goodenough, D.A.4
  • 181
    • 0344688189 scopus 로고    scopus 로고
    • Activation of ERK1/2 MAP kinase pathway induces tight junction disruption in human corneal epithelial cells
    • DOI 10.1016/j.exer.2003.09.002
    • Wang Y., J. Zhang, X. J. Yi and F. S. Yu: Activation of ERK1/2 MAP kinase pathway induces tight junction disruption in human corneal epithelial cells. Exp Eye Res, 78, 125-136 (2004). (Pubitemid 37518251)
    • (2004) Experimental Eye Research , vol.78 , Issue.1 , pp. 125-136
    • Wang, Y.1    Zhang, J.2    Yi, X.-J.3    Yu, F.-S.X.4
  • 182
    • 30044442771 scopus 로고    scopus 로고
    • MAPK interacts with occludin and mediates EGF-induced prevention of tight junction disruption by hydrogen peroxide
    • DOI 10.1042/BJ20050959
    • Basuroy S., A. Seth, B. Elias, A. P. Naren and R. Rao: MAPK interacts with occludin and mediates EGF-induced prevention of tight junction disruption by hydrogen peroxide. Biochem J, 393, 69-77 (2006). (Pubitemid 43049303)
    • (2006) Biochemical Journal , vol.393 , Issue.1 , pp. 69-77
    • Basuroy, S.1    Seth, A.2    Elias, B.3    Naren, A.P.4    Rao, R.5
  • 183
    • 33750489040 scopus 로고    scopus 로고
    • Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling
    • DOI 10.1038/sj.emboj.7601384, PII 7601384
    • Wang Y., D. Du, L. Fang, G. Yang, C. Zhang, R. Zeng, A. Ullrich, F. Lottspeich and Z. Chen: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J, 25, 5058-5070 (2006). (Pubitemid 44658524)
    • (2006) EMBO Journal , vol.25 , Issue.21 , pp. 5058-5070
    • Wang, Y.1    Du, D.2    Fang, L.3    Yang, G.4    Zhang, C.5    Zeng, R.6    Ullrich, A.7    Lottspeich, F.8    Chen, Z.9
  • 184
    • 0024467201 scopus 로고
    • Sodium as a mediator of non-phorbol tumor promoter action. Down-modulation of the epidermal growth factor receptor by palytoxin
    • Wattenberg E. V., K. L. Byron, M. L. Villereal, H. Fujiki and M. R. Rosner: Sodium as a mediator of nonphorbol tumor promoter action. Down-modulation of the epidermal growth factor receptor by palytoxin. J Biol Chem, 264, 14668-14673 (1989). (Pubitemid 19237280)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.25 , pp. 14668-14673
    • Wattenberg, E.V.1    Byron, K.L.2    Villereal, M.L.3    Fujiki, H.4    Rosner, M.R.5
  • 185
    • 0024529251 scopus 로고
    • Palytoxin down-modulates the epidermal growth factor receptor through a sodium-dependent pathway
    • Wattenberg E. V., P. L. McNeil, H. Fujiki and M. R. Rosner: Palytoxin down-modulates the epidermal growth factor receptor through a sodium-dependent pathway. J Biol Chem, 264, 213-219 (1989). (Pubitemid 19027593)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.1 , pp. 213-219
    • Wattenberg, E.V.1    McNeil, P.L.2    Fujiki, H.3    Rosner, M.R.4
  • 187
    • 1842736450 scopus 로고    scopus 로고
    • Large Diameter of Palytoxin-induced Na/K Pump Channels and Modulation of Palytoxin Interaction by Na/K Pump Ligands
    • DOI 10.1085/jgp.200308964
    • Artigas P. and D. C. Gadsby: Large diameter of palytoxin-induced Na/K pump channels and modulation of palytoxin interaction by Na/K pump ligands. J Gen Physiol, 123, 357-376 (2004). (Pubitemid 38469280)
    • (2004) Journal of General Physiology , vol.123 , Issue.4 , pp. 357-376
    • Artigas, P.1    Gadsby, D.C.2
  • 188
    • 29144447613 scopus 로고    scopus 로고
    • Epidermal growth factor receptor is a common element in the signaling pathways activated by cell volume changes in isosmotic, hyposmotic or hyperosmotic conditions
    • DOI 10.1007/s11064-005-8837-5
    • Lezama R., A. Diaz-Tellez, G. Ramos-Mandujano, L. Oropeza and H. Pasantes-Morales: Epidermal growth factor receptor is a common element in the signaling pathways activated by cell volume changes in isosmotic, hyposmotic or hyperosmotic conditions. Neurochem Res, 30, 1589-1597 (2005). (Pubitemid 41813723)
    • (2005) Neurochemical Research , vol.30 , Issue.12 , pp. 1589-1597
    • Lezama, R.1    Diaz-Tellez, A.2    Ramos-Mandujano, G.3    Oropeza, L.4    Pasantes-Morales, H.5
  • 189
    • 34249105226 scopus 로고    scopus 로고
    • Identification of protein kinase C as an intermediate in NA, K-atpase beta-subunit mediated lamellipodia formation and suppression of cell motility in carcinoma cells
    • DOI 10.1170/T759
    • Barwe S. P., S. A. Rajasekaran and A. K. Rajasekaran: Identification of protein kinase C as an intermediate in Na, K-ATPase beta-subunit mediated lamellipodia formation and suppression of cell motility in carcinoma cells. Cell Mol Biol, 52, 41-47 (2006). (Pubitemid 46799704)
    • (2006) Cellular and Molecular Biology , vol.52 , Issue.8 , pp. 41-47
    • Barwe, S.P.1    Rajasekaran, S.A.2    Rajasekaran, A.K.3
  • 190
    • 28644439932 scopus 로고    scopus 로고
    • Multiple functions of Na,K-ATPase in epithelial cells
    • DOI 10.1016/j.semnephrol.2005.03.008, PII S0270929505000513, The Sodium-K ATPases
    • Rajasekaran S. A., S. P. Barwe and A. K. Rajasekaran: Multiple functions of Na, K-ATPase in epithelial cells. Semin Nephrol, 25, 328-334 (2005). (Pubitemid 41749415)
    • (2005) Seminars in Nephrology , vol.25 , Issue.5 , pp. 328-334
    • Rajasekaran, S.A.1    Barwe, S.P.2    Rajasekaran, A.K.3
  • 191
    • 0035053279 scopus 로고    scopus 로고
    • +-ATPase by interferon γ down-regulates intestinal epithelial transport and barrier function
    • Sugi K., M. W. Musch, M. Field and E. B. Chang: Inhibition of Na+, K+-ATPase by interferon gamma down-regulates intestinal epithelial transport and barrier function. Gastroenterology, 120, 1393-1403 (2001). (Pubitemid 32322313)
    • (2001) Gastroenterology , vol.120 , Issue.6 , pp. 1393-1403
    • Sugi, K.1    Musch, M.W.2    Field, M.3    Chang, E.B.4
  • 192
    • 2342431153 scopus 로고    scopus 로고
    • The transcription factor Snail downregulates the tight junction components independently of E-cadherin downregulation
    • DOI 10.1242/jcs.01004
    • Ohkubo T. and M. Ozawa: The transcription factor Snail downregulates the tight junction components independently of E-cadherin downregulation. J Cell Sci, 117, 1675-1685 (2004). (Pubitemid 38559300)
    • (2004) Journal of Cell Science , vol.117 , Issue.9 , pp. 1675-1685
    • Ohkubo, T.1    Ozawa, M.2
  • 193
    • 33847282998 scopus 로고    scopus 로고
    • Raf 1 represses expression of the tight junction protein occludin via activation of the zinc-finger transcription factor slug
    • Wang Z., P. Wade, K. J. Mandell, A. Akyildiz, C. A. Parkos, R. J. Mrsny and A. Nusrat: Raf 1 represses expression of the tight junction protein occludin via activation of the zinc-finger transcription factor slug. Oncogene, 26, 1222-1230 (2007).
    • (2007) Oncogene , vol.26 , pp. 1222-1230
    • Wang, Z.1    Wade, P.2    Mandell, K.J.3    Akyildiz, A.4    Parkos, C.A.5    Mrsny, R.J.6    Nusrat, A.7
  • 194
    • 45549105086 scopus 로고    scopus 로고
    • The transcription factor snail represses Crumbs3 expression and disrupts apico-basal polarity complexes
    • Whiteman E. L., C. J. Liu, E. R. Fearon and B. Margolis: The transcription factor snail represses Crumbs3 expression and disrupts apico-basal polarity complexes. Oncogene (2008).
    • (2008) Oncogene
    • Whiteman, E.L.1    Liu, C.J.2    Fearon, E.R.3    Margolis, B.4
  • 196
    • 0023510866 scopus 로고
    • Structural basis for physiological regulation of paracellular pathways in intestinal epithelia
    • Madara J. L. and J. R. Pappenheimer: Structural basis for physiological regulation of paracellular pathways in intestinal epithelia. J Membr Biol, 100, 149-164 (1987). (Pubitemid 18004072)
    • (1987) Journal of Membrane Biology , vol.100 , Issue.2 , pp. 149-164
    • Madara, J.L.1    Pappenheimer, J.R.2
  • 197
    • 0034527745 scopus 로고    scopus 로고
    • +-glucose cotransport
    • DOI 10.1023/A:1026682900586
    • Turner J. R., D. E. Cohen, R. J. Mrsny and J. L. Madara: Noninvasive in vivo analysis of human small intestinal paracellular absorption: regulation by Na+-glucose cotransport. Dig Dis Sci, 45, 2122-2126 (2000). (Pubitemid 32060380)
    • (2000) Digestive Diseases and Sciences , vol.45 , Issue.11 , pp. 2122-2126
    • Turner, J.R.1    Cohen, D.E.2    Mrsny, R.J.3    Madara, J.L.4
  • 198
    • 0030669302 scopus 로고    scopus 로고
    • Physiological regulation of epithelial tight junctions is associated with myosin light-chain phosphorylation
    • Turner J. R., B. K. Rill, S. L. Carlson, D. Carnes, R. Kerner, R. J. Mrsny and J. L. Madara: Physiological regulation of epithelial tight junctions is associated with myosin light-chain phosphorylation. Am J Physiol, 273, C1378-1385 (1997).
    • (1997) Am J Physiol , vol.273
    • Turner, J.R.1    Rill, B.K.2    Carlson, S.L.3    Carnes, D.4    Kerner, R.5    Mrsny, R.J.6    Madara, J.L.7
  • 201
    • 0017918451 scopus 로고
    • Membrane cation transport and the control of proliferation of mammalian cells
    • Kaplan J. G.: Membrane cation transport and the control of proliferation of mammalian cells. Annu Rev Physiol, 40, 19-41 (1978).
    • (1978) Annu Rev Physiol , vol.40 , pp. 19-41
    • Kaplan, J.G.1
  • 202
    • 0018088023 scopus 로고
    • Alteration of sodium transport in mouse mammary epithelium associated with neoplastic transformation
    • Shen S. S., S. T. Hamamoto, H. A. Bern and R. A. Steinhardt: Alteration of sodium transport in mouse mammary epithelium associated with neoplastic transformation. Cancer Res, 38, 1356-61 (1978). (Pubitemid 8323338)
    • (1978) Cancer Research , vol.38 , Issue.5 , pp. 1356-1361
    • Shen, S.S.1    Hamamoto, S.T.2    Bern, H.A.3    Steinhardt, R.A.4
  • 203
    • 21344468869 scopus 로고    scopus 로고
    • NA/K-ATPase, endogenous digitalis-like compounds and cancer development - A hypothesis
    • Weidemann H.: Na/K-ATPase, endogenous digitalis like compounds and cancer development - a hypothesis. Front Biosci, 10, 2165-76 (2005). (Pubitemid 40905290)
    • (2005) Frontiers in Bioscience , vol.10 , Issue.SUPPL. 1 , pp. 2165-2176
    • Weidemann, H.1
  • 204
    • 0026200152 scopus 로고
    • Inhibition of the Na+, K (+)-ATPase pump during induction of experimental colon cancer
    • Davies R. J., G. I. Sandle and S. M. Thompson: Inhibition of the Na+, K (+)-ATPase pump during induction of experimental colon cancer. Cancer Biochem Biophys, 12, 81-94 (1991).
    • (1991) Cancer Biochem Biophys , vol.12 , pp. 81-94
    • Davies, R.J.1    Sandle, G.I.2    Thompson, S.M.3
  • 205
    • 0022566579 scopus 로고
    • Properties of Na+/K+ ATPase and alkaline phosphatase alter during spontaneous and radiation-induced leukemogenesis in mice
    • Gonta-Grabiec K., W. Rossowski and I. Szumiel: Properties of Na+/K+ ATPase and alkaline phosphatase alter during spontaneous and radiation-induced leukemogenesis in mice. Neoplasma, 33, 141-155 (1986).
    • (1986) Neoplasma , vol.33 , pp. 141-155
    • Gonta-Grabiec, K.1    Rossowski, W.2    Szumiel, I.3
  • 206
    • 0032866353 scopus 로고    scopus 로고
    • Reduced expression of β-subunit of NA,K-ATPase in human clear-cell renal cell carcinoma
    • DOI 10.1016/S0022-5347(05)68629-6
    • Rajasekaran S. A., W. J. Ball, Jr., N. H. Bander, H. Liu, J. D. Pardee and A. K. Rajasekaran: Reduced expression of beta-subunit of Na, K-ATPase in human clear-cell renal cell carcinoma. J Urol, 162, 574-580 (1999). (Pubitemid 29434399)
    • (1999) Journal of Urology , vol.162 , Issue.2 , pp. 574-580
    • Rajasekaran, S.A.1    Ball Jr., W.J.2    Bander, N.H.3    Liu, H.4    Pardee, J.D.5    Rajasekaran, A.K.6
  • 208
    • 1842737653 scopus 로고    scopus 로고
    • +-ATPase α3-isoform and down-regulation of the α1-isoform in human colorectal cancer
    • DOI 10.1016/S0014-5793(04)00292-3, PII S0014579304002923
    • Sakai H., T. Suzuki, M. Maeda, Y. Takahashi, N. Horikawa, T. Minamimura, K. Tsukada and N. Takeguchi: Up-regulation of Na (+), K (+)-ATPase alpha 3-isoform and down-regulation of the alpha1-isoform in human colorectal cancer. FEBS Lett, 563, 151-154 (2004). (Pubitemid 38471590)
    • (2004) FEBS Letters , vol.563 , Issue.1-3 , pp. 151-154
    • Sakai, H.1    Suzuki, T.2    Maeda, M.3    Takahashi, Y.4    Horikawa, N.5    Minamimura, T.6    Tsukada, K.7    Takeguchi, N.8
  • 210
    • 2942609688 scopus 로고    scopus 로고
    • Epithelial Na, K-ATPase expression is down-regulated in canine prostate cancer; a possible consequence of metabolic transformation in the process of prostate malignancy
    • Mobasheri A., R. Fox, I. Evans, F. Cullingham, P. Martin-Vasallo and C. S. Foster: Epithelial Na, K-ATPase expression is down-regulated in canine prostate cancer; a possible consequence of metabolic transformation in the process of prostate malignancy. Cancer Cell Int, 3, 8 (2003).
    • (2003) Cancer Cell Int , vol.3 , pp. 8
    • Mobasheri, A.1    Fox, R.2    Evans, I.3    Cullingham, F.4    Martin-Vasallo, P.5    Foster, C.S.6
  • 211
    • 0025812383 scopus 로고
    • Tissue-specific expression of Na, K-ATPase beta-subunit. Does beta 2 expression correlate with tumorigenesis?
    • Akopyanz N. S., N. E. Broude, E. P. Bekman, E. O. Marzen and E. D. Sverdlov: Tissue-specific expression of Na, K-ATPase beta-subunit. Does beta 2 expression correlate with tumorigenesis? FEBS Lett, 289, 8-10 (1991).
    • (1991) FEBS Lett , vol.289 , pp. 8-10
    • Akopyanz, N.S.1    Broude, N.E.2    Bekman, E.P.3    Marzen, E.O.4    Sverdlov, E.D.5
  • 213
    • 0037446091 scopus 로고    scopus 로고
    • Analysis of the Na,K-ATpase α- and β-subunit expression profiles of bladder cancer using tissue microarrays
    • DOI 10.1002/cncr.11267
    • Espineda C., D. B. Seligson, W. James Ball, Jr., J. Rao, A. Palotie, S. Horvath, Y. Huang, T. Shi and A. K. Rajasekaran: Analysis of the Na, K-ATPase alpha- and beta-subunit expression profiles of bladder cancer using tissue microarrays. Cancer, 97, 1859-1868 (2003). (Pubitemid 36397259)
    • (2003) Cancer , vol.97 , Issue.8 , pp. 1859-1868
    • Espineda, C.1    Seligson, D.B.2    Ball Jr., W.J.3    Rao, J.4    Palotie, A.5    Horvath, S.6    Huang, Y.7    Shi, T.8    Rajasekaran, A.K.9
  • 214
    • 9244251969 scopus 로고    scopus 로고
    • Identification and cloning of genes displaying elevated expression as a consequence of metastatic progression in human melanoma cells by rapid subtraction hybridization
    • DOI 10.1016/j.gene.2004.09.002, PII S0378111904005530
    • Boukerche H., Z. Z. Su, D. C. Kang and P. B. Fisher: Identification and cloning of genes displaying elevated expression as a consequence of metastatic progression in human melanoma cells by rapid subtraction hybridization. Gene, 343, 191-201 (2004). (Pubitemid 39551043)
    • (2004) Gene , vol.343 , Issue.1 , pp. 191-201
    • Boukerche, H.1    Su, Z.-Z.2    Kang, D.-C.3    Fisher, P.B.4
  • 215
    • 33646569462 scopus 로고    scopus 로고
    • Function of FXYD proteins, regulators of Na,K-ATPase
    • DOI 10.1007/s10863-005-9476-x
    • Geering K.: Function of FXYD proteins, regulators of Na, K-ATPase. J Bioenerg Biomembr, 37, 387-392 (2005). (Pubitemid 43725163)
    • (2005) Journal of Bioenergetics and Biomembranes , vol.37 , Issue.6 , pp. 387-392
    • Geering, K.1
  • 218
    • 0023881549 scopus 로고
    • Inverse relationship between colonic (Na+ + K+)-ATPase activity and degree of mucosal inflammation in inflammatory bowel disease
    • Allgayer H., W. Kruis, G. Paumgartner, B. Wiebecke, L. Brown and E. Erdmann: Inverse relationship between colonic (Na+ + K+)-ATPase activity and degree of mucosal inflammation in inflammatory bowel disease. Dig Dis Sci, 33, 417-422 (1988).
    • (1988) Dig Dis Sci , vol.33 , pp. 417-422
    • Allgayer, H.1    Kruis, W.2    Paumgartner, G.3    Wiebecke, B.4    Brown, L.5    Erdmann, E.6
  • 219
    • 0024326116 scopus 로고
    • Na,K-ATPase activity in rectal mucosa of children with ulcerative colitis and Crohn's disease
    • Ejderhamn J., Y. Finkel and B. Strandvik: Na, K-ATPase activity in rectal mucosa of children with ulcerative colitis and Crohn's disease. Scand J Gastroenterol, 24, 1121-1125 (1989). (Pubitemid 19275599)
    • (1989) Scandinavian Journal of Gastroenterology , vol.24 , Issue.9 , pp. 1121-1125
    • Ejderhamn, J.1    Finkel, Y.2    Strandvik, B.3
  • 220
    • 0021226244 scopus 로고
    • Decreased colonic Na-K-ATPase activity in active ulcerative colitis
    • Rachmilewitz D., F. Karmeli and P. Sharon: Decreased colonic Na-K-ATPase activity in active ulcerative colitis. Isr J Med Sci, 20, 681-684 (1984). (Pubitemid 14035879)
    • (1984) Israel Journal of Medical Sciences , vol.20 , Issue.8 , pp. 681-684
    • Rachmilewitz, D.1    Karmeli, F.2    Sharon, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.