메뉴 건너뛰기




Volumn 6, Issue 3, 2010, Pages 168-178

Aquaporins in kidney pathophysiology

Author keywords

[No Author keywords available]

Indexed keywords

AMILORIDE; ANION; AQUAPORIN; AQUAPORIN 1; AQUAPORIN 11; AQUAPORIN 2; AQUAPORIN 3; AQUAPORIN 4; AQUAPORIN 5; AQUAPORIN 6; AQUAPORIN 7; GLYCEROL; HYDROCHLOROTHIAZIDE; LITHIUM; MEMBRANE PROTEIN; PHOSPHODIESTERASE INHIBITOR; PROSTAGLANDIN INHIBITOR; ROLIPRAM; TOLVAPTAN; TROPOMYOSIN; UNCLASSIFIED DRUG;

EID: 77649179443     PISSN: 17595061     EISSN: 1759507X     Source Type: Journal    
DOI: 10.1038/nrneph.2009.231     Document Type: Review
Times cited : (118)

References (127)
  • 1
    • 0026503030 scopus 로고    scopus 로고
    • Preston, G. M., Carroll, T. P., Guggino, W. B. & Agre, P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256, 385-387 (1992).
    • Preston, G. M., Carroll, T. P., Guggino, W. B. & Agre, P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256, 385-387 (1992).
  • 2
    • 0036083443 scopus 로고    scopus 로고
    • Aquaporins in the kidney: From molecules to medicine
    • Nielsen, S. et al. Aquaporins in the kidney: from molecules to medicine. Physiol. Rev. 82, 205-244 (2002).
    • (2002) Physiol. Rev , vol.82 , pp. 205-244
    • Nielsen, S.1
  • 3
  • 4
    • 43549112543 scopus 로고    scopus 로고
    • Rojek, A., Praetorius, J., Frøkiaer, J., Nielsen, S. & Fenton, R. A. A current view of the mammalian aquaglyceroporins. Annu. Rev. Physiol. 70, 301-327 (2008).
    • Rojek, A., Praetorius, J., Frøkiaer, J., Nielsen, S. & Fenton, R. A. A current view of the mammalian aquaglyceroporins. Annu. Rev. Physiol. 70, 301-327 (2008).
  • 5
    • 66449127399 scopus 로고    scopus 로고
    • Aquaporins: Translating bench research to human disease
    • Verkman, A. S. Aquaporins: translating bench research to human disease. J. Exp. Biol. 212, 1707-1715 (2009).
    • (2009) J. Exp. Biol , vol.212 , pp. 1707-1715
    • Verkman, A.S.1
  • 6
    • 59849095753 scopus 로고    scopus 로고
    • Sensing, signaling and sorting events in kidney epithelial cell physiology
    • Brown, D., Breton, S., Ausiello, D. A. & Marshansky, V. Sensing, signaling and sorting events in kidney epithelial cell physiology. Traffic 10, 275-284 (2009).
    • (2009) Traffic , vol.10 , pp. 275-284
    • Brown, D.1    Breton, S.2    Ausiello, D.A.3    Marshansky, V.4
  • 7
    • 67649363886 scopus 로고    scopus 로고
    • Aquaporin-2 in the "-omics" era
    • Hoffert, J. D., Chou, C. L. & Knepper, M. A. Aquaporin-2 in the "-omics" era. J. Biol. Chem. 284, 14683-14687 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 14683-14687
    • Hoffert, J.D.1    Chou, C.L.2    Knepper, M.A.3
  • 8
    • 50049087856 scopus 로고    scopus 로고
    • Physiology and pathophysiology of the vasopressin-regulated renal water reabsorption
    • Boone, M. & Deen, P. M. Physiology and pathophysiology of the vasopressin-regulated renal water reabsorption. Pflugers Arch. 456, 1005-1024 (2008).
    • (2008) Pflugers Arch , vol.456 , pp. 1005-1024
    • Boone, M.1    Deen, P.M.2
  • 9
    • 33748568155 scopus 로고    scopus 로고
    • Regulation of aquaporin-2 trafficking and its binding protein complex
    • Noda, Y. & Sasaki, S. Regulation of aquaporin-2 trafficking and its binding protein complex. Biochim. Biophys. Acta 1758, 1117-1125 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1117-1125
    • Noda, Y.1    Sasaki, S.2
  • 11
    • 0034645068 scopus 로고    scopus 로고
    • The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers
    • Kamsteeg, E. J., Heijnen, I., van Os, C. H. & Deen, P. M. The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers. J. Cell Biol. 151, 919-930 (2000).
    • (2000) J. Cell Biol , vol.151 , pp. 919-930
    • Kamsteeg, E.J.1    Heijnen, I.2    van Os, C.H.3    Deen, P.M.4
  • 12
    • 20444420877 scopus 로고    scopus 로고
    • The 4.5 A structure of human AQP2
    • Schenk, A. D. et al. The 4.5 A structure of human AQP2. J. Mol. Biol. 350, 278-289 (2005).
    • (2005) J. Mol. Biol , vol.350 , pp. 278-289
    • Schenk, A.D.1
  • 13
    • 0033582496 scopus 로고    scopus 로고
    • Protein kinase A anchoring proteins are required for vasopressin-mediated translocation of aquaporin-2 into cell membranes of renal principal cells
    • Klussmann, E., Maric, K., Wiesner, B., Beyermann, M. & Rosenthal, W. Protein kinase A anchoring proteins are required for vasopressin-mediated translocation of aquaporin-2 into cell membranes of renal principal cells. J. Biol. Chem. 274, 4934-4938 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 4934-4938
    • Klussmann, E.1    Maric, K.2    Wiesner, B.3    Beyermann, M.4    Rosenthal, W.5
  • 14
    • 2942702016 scopus 로고    scopus 로고
    • Identification of a novel A-kinase anchoring protein 18 isoform and evidence for its role in the vasopressin-induced aquaporin-2 shuttle in renal principal cells
    • Henn, V. et al. Identification of a novel A-kinase anchoring protein 18 isoform and evidence for its role in the vasopressin-induced aquaporin-2 shuttle in renal principal cells. J. Biol. Chem. 279, 26654-26665 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 26654-26665
    • Henn, V.1
  • 15
    • 56549130084 scopus 로고    scopus 로고
    • AKAP220 colocalizes with AQP2 in the inner medullary collecting ducts
    • Okutsu, R. et al. AKAP220 colocalizes with AQP2 in the inner medullary collecting ducts. Kidney Int. 74, 1429-1433 (2008).
    • (2008) Kidney Int , vol.74 , pp. 1429-1433
    • Okutsu, R.1
  • 16
    • 84875058225 scopus 로고    scopus 로고
    • Ser-256 phosphorylation dynamics of aquaporin 2 during maturation from the endoplasmic reticulum to the vesicular compartment in renal cells
    • Procino, G. et al. Ser-256 phosphorylation dynamics of aquaporin 2 during maturation from the endoplasmic reticulum to the vesicular compartment in renal cells. FASEB J. 17, 1886-1888 (2003).
    • (2003) FASEB J , vol.17 , pp. 1886-1888
    • Procino, G.1
  • 17
    • 0036829071 scopus 로고    scopus 로고
    • The role of putative phosphorylation sites in the targeting and shuttling of the aquaporin-2 water channel
    • van Balkom, B. W. et al. The role of putative phosphorylation sites in the targeting and shuttling of the aquaporin-2 water channel. J. Biol. Chem. 277, 41473-41479 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 41473-41479
    • van Balkom, B.W.1
  • 18
    • 0033756528 scopus 로고    scopus 로고
    • Nitric oxide and atrial natriuretic factor stimulate cGMP-dependent membrane insertion of aquaporin 2 in renal epithelial cells
    • Bouley, R. et al. Nitric oxide and atrial natriuretic factor stimulate cGMP-dependent membrane insertion of aquaporin 2 in renal epithelial cells. J. Clin. Invest. 106, 1115-1126 (2000).
    • (2000) J. Clin. Invest , vol.106 , pp. 1115-1126
    • Bouley, R.1
  • 19
    • 18744371290 scopus 로고    scopus 로고
    • Stimulation of AQP2 membrane insertion in renal epithelial cells in vitro and in vivo by the cGMP phosphodiesterase inhibitor sildenafil citrate (Viagra)
    • Bouley, R. et al. Stimulation of AQP2 membrane insertion in renal epithelial cells in vitro and in vivo by the cGMP phosphodiesterase inhibitor sildenafil citrate (Viagra). Am. J. Physiol. Renal Physiol. 288, F1103-F1112 (2005).
    • (2005) Am. J. Physiol. Renal Physiol , vol.288
    • Bouley, R.1
  • 20
    • 42949157341 scopus 로고    scopus 로고
    • Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin
    • Fenton, R. A. et al. Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin. Proc. Natl Acad. Sci. USA 105, 3134-3139 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 3134-3139
    • Fenton, R.A.1
  • 21
    • 33846890894 scopus 로고    scopus 로고
    • Dynamics of aquaporin-2 serine-261 phosphorylation in response to short-term vasopressin treatment in collecting duct
    • Hoffert, J. D. et al. Dynamics of aquaporin-2 serine-261 phosphorylation in response to short-term vasopressin treatment in collecting duct. Am. J. Physiol. Renal Physiol. 292, F691-F700 (2007).
    • (2007) Am. J. Physiol. Renal Physiol , vol.292
    • Hoffert, J.D.1
  • 22
    • 49949107593 scopus 로고    scopus 로고
    • The phosphorylation state of serine 256 is dominant over that of serine 261 in the regulation of AQP2 trafficking in renal epithelial cells
    • Lu, H. J. et al. The phosphorylation state of serine 256 is dominant over that of serine 261 in the regulation of AQP2 trafficking in renal epithelial cells. Am. J. Physiol. Renal Physiol. 295, F290-F294 (2008).
    • (2008) Am. J. Physiol. Renal Physiol , vol.295
    • Lu, H.J.1
  • 23
    • 58349117208 scopus 로고    scopus 로고
    • Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells
    • Moeller, H. B., Knepper, M. A. & Fenton, R. A. Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells. Kidney Int. 75, 295-303 (2009).
    • (2009) Kidney Int , vol.75 , pp. 295-303
    • Moeller, H.B.1    Knepper, M.A.2    Fenton, R.A.3
  • 24
    • 66049117458 scopus 로고    scopus 로고
    • Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: Evidence against channel gating
    • Moeller, H. B., MacAulay, N., Knepper, M. A. & Fenton, R. A. Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: evidence against channel gating. Am. J. Physiol. Renal Physiol. 296, F649-F657 (2009).
    • (2009) Am. J. Physiol. Renal Physiol , vol.296
    • Moeller, H.B.1    MacAulay, N.2    Knepper, M.A.3    Fenton, R.A.4
  • 25
    • 43749122617 scopus 로고    scopus 로고
    • Calcium signaling in vasopressin-induced aquaporin-2 trafficking
    • Balasubramanian, L., Sham, J. S. & Yip, K. P. Calcium signaling in vasopressin-induced aquaporin-2 trafficking. Pflugers Arch. 456, 747-754 (2008).
    • (2008) Pflugers Arch , vol.456 , pp. 747-754
    • Balasubramanian, L.1    Sham, J.S.2    Yip, K.P.3
  • 26
    • 17044377499 scopus 로고    scopus 로고
    • Identification of a multiprotein "motor" complex binding to water channel aquaporin-2
    • Noda, Y., Horikawa, S., Katayama, Y. & Sasaki, S. Identification of a multiprotein "motor" complex binding to water channel aquaporin-2. Biochem. Biophys. Res. Commun. 330, 1041-1047 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.330 , pp. 1041-1047
    • Noda, Y.1    Horikawa, S.2    Katayama, Y.3    Sasaki, S.4
  • 27
    • 0037223654 scopus 로고    scopus 로고
    • Cyclic AMP is sufficient for triggering the exocytic recruitment of aquaporin-2 in renal epithelial cells
    • 88-93
    • Lorenz, D. et al. Cyclic AMP is sufficient for triggering the exocytic recruitment of aquaporin-2 in renal epithelial cells. EMBO Rep. 4, 88-93 (2003).
    • (2003) EMBO Rep , vol.4
    • Lorenz, D.1
  • 28
    • 21644471863 scopus 로고    scopus 로고
    • extracellular calcium antagonizes forskolin-induced aquaporin 2 trafficking in collecting duct cells
    • Procino, G. et al. extracellular calcium antagonizes forskolin-induced aquaporin 2 trafficking in collecting duct cells. Kidney Int. 66, 2245-2255 (2004).
    • (2004) Kidney Int , vol.66 , pp. 2245-2255
    • Procino, G.1
  • 29
    • 17644413525 scopus 로고    scopus 로고
    • Bidirectional regulation of AQP2 trafficking and recycling: Involvement of AQP2-S256 phosphorylation
    • Nejsum, L. N., Zelenina, M., Aperia, A., Frøkiaer, J. & Nielsen, S. Bidirectional regulation of AQP2 trafficking and recycling: involvement of AQP2-S256 phosphorylation. Am. J. Physiol. Renal Physiol. 288, F930-F938 (2005).
    • (2005) Am. J. Physiol. Renal Physiol , vol.288
    • Nejsum, L.N.1    Zelenina, M.2    Aperia, A.3    Frøkiaer, J.4    Nielsen, S.5
  • 30
    • 34548021899 scopus 로고    scopus 로고
    • Long-term aldosterone treatment induces decreased apical but increased basolateral expression of AQP2 in CCD of rat kidney
    • de Seigneux, S. et al. Long-term aldosterone treatment induces decreased apical but increased basolateral expression of AQP2 in CCD of rat kidney. Am. J. Physiol. Renal Physiol. 293, F87-F99 (2007).
    • (2007) Am. J. Physiol. Renal Physiol , vol.293
    • de Seigneux, S.1
  • 31
    • 0035658684 scopus 로고    scopus 로고
    • Rho inhibits cAMP-induced translocation of aquaporin-2 into the apical membrane of renal cells
    • Tamma, G. et al. Rho inhibits cAMP-induced translocation of aquaporin-2 into the apical membrane of renal cells. Am. J. Physiol. Renal Physiol. 281, F1092-F1101 (2001).
    • (2001) Am. J. Physiol. Renal Physiol , vol.281
    • Tamma, G.1
  • 32
    • 0041384186 scopus 로고    scopus 로고
    • The prostaglandin e2 analogue sulprostone antagonizes vasopressin-induced antidiuresis through activation of Rho
    • Tamma, G. et al. The prostaglandin e2 analogue sulprostone antagonizes vasopressin-induced antidiuresis through activation of Rho. J. Cell Sci. 116, 3285-3294 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 3285-3294
    • Tamma, G.1
  • 33
    • 33645271493 scopus 로고    scopus 로고
    • Bradykinin signaling counteracts cAMP-elicited aquaporin 2 translocation in renal cells
    • Tamma, G., Carmosino, M., Svelto, M. & valenti, G. Bradykinin signaling counteracts cAMP-elicited aquaporin 2 translocation in renal cells. J. Am. Soc. Nephrol. 16, 2881-2889 (2005).
    • (2005) J. Am. Soc. Nephrol , vol.16 , pp. 2881-2889
    • Tamma, G.1    Carmosino, M.2    Svelto, M.3    valenti, G.4
  • 34
    • 2942532738 scopus 로고    scopus 로고
    • Aquaporin-2 trafficking is regulated by PDZ-domain containing protein SPA-1
    • Noda, Y. et al. Aquaporin-2 trafficking is regulated by PDZ-domain containing protein SPA-1. FEBS Lett. 568, 139-145 (2004).
    • (2004) FEBS Lett , vol.568 , pp. 139-145
    • Noda, Y.1
  • 35
    • 1842714198 scopus 로고    scopus 로고
    • Specific recruitment of SPA-1 to the immunological synapse: Involvement of actin-bundling protein actinin
    • Harazaki, M. et al. Specific recruitment of SPA-1 to the immunological synapse: involvement of actin-bundling protein actinin. Immunol. Lett. 92, 221-226 (2004).
    • (2004) Immunol. Lett , vol.92 , pp. 221-226
    • Harazaki, M.1
  • 36
    • 33750552767 scopus 로고    scopus 로고
    • Role of SPA-1 in phenotypes of chronic myelogenous leukemia induced by BCR-ABL-expressing hematopoietic progenitors in a mouse model
    • Kometani, K. et al. Role of SPA-1 in phenotypes of chronic myelogenous leukemia induced by BCR-ABL-expressing hematopoietic progenitors in a mouse model. Cancer Res. 66, 9967-9976 (2006).
    • (2006) Cancer Res , vol.66 , pp. 9967-9976
    • Kometani, K.1
  • 37
    • 0034834960 scopus 로고    scopus 로고
    • Three families with autosomal dominant nephrogenic diabetes insipidus caused by aquaporin-2 mutations in the C-terminus
    • Kuwahara, M. et al. Three families with autosomal dominant nephrogenic diabetes insipidus caused by aquaporin-2 mutations in the C-terminus. Am. J. Hum. Genet. 69, 738-748 (2001).
    • (2001) Am. J. Hum. Genet , vol.69 , pp. 738-748
    • Kuwahara, M.1
  • 38
    • 30944433609 scopus 로고    scopus 로고
    • The C-terminal tail of aquaporin-2 determines apical trafficking
    • Kuwahara, M., Asai, T., Terada, Y. & Sasaki, S. The C-terminal tail of aquaporin-2 determines apical trafficking. Kidney Int. 68, 1999-2009 (2005).
    • (2005) Kidney Int , vol.68 , pp. 1999-2009
    • Kuwahara, M.1    Asai, T.2    Terada, Y.3    Sasaki, S.4
  • 40
    • 49749127665 scopus 로고    scopus 로고
    • Reciprocal interaction with G-actin and tropomyosin is essential for aquaporin-2 trafficking
    • Noda, Y. et al. Reciprocal interaction with G-actin and tropomyosin is essential for aquaporin-2 trafficking. J. Cell Biol. 182, 587-601 (2008).
    • (2008) J. Cell Biol , vol.182 , pp. 587-601
    • Noda, Y.1
  • 41
    • 43749123303 scopus 로고    scopus 로고
    • The role of actin remodeling in the trafficking of intracellular vesicles, transporters, and channels: Focusing on aquaporin-2
    • Noda, Y. & Sasaki, S. The role of actin remodeling in the trafficking of intracellular vesicles, transporters, and channels: focusing on aquaporin-2. Pflugers Arch. 456, 737-745 (2008).
    • (2008) Pflugers Arch , vol.456 , pp. 737-745
    • Noda, Y.1    Sasaki, S.2
  • 42
    • 47549110360 scopus 로고    scopus 로고
    • Actin-binding channels
    • Noda, Y. & Sasaki, S. Actin-binding channels. Prog. Brain Res. 170, 551-557 (2008).
    • (2008) Prog. Brain Res , vol.170 , pp. 551-557
    • Noda, Y.1    Sasaki, S.2
  • 43
    • 24344454782 scopus 로고    scopus 로고
    • Differential regulation of AQP2 trafficking in endosomes by microtubules and actin filaments
    • Tajika, Y. et al. Differential regulation of AQP2 trafficking in endosomes by microtubules and actin filaments. Histochem. Cell Biol. 124, 1-12 (2005).
    • (2005) Histochem. Cell Biol , vol.124 , pp. 1-12
    • Tajika, Y.1
  • 44
    • 10344239445 scopus 로고    scopus 로고
    • Non-muscle myosin II and myosin light chain kinase are downstream targets for vasopressin signaling in the renal collecting duct
    • Chou, C. L. et al. Non-muscle myosin II and myosin light chain kinase are downstream targets for vasopressin signaling in the renal collecting duct. J. Biol. Chem. 279, 49026-49035 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 49026-49035
    • Chou, C.L.1
  • 45
    • 33846197918 scopus 로고    scopus 로고
    • A role of myosin Vb and Rab11-FIP2 in the aquaporin-2 shuttle
    • Nedvetsky, P. I. et al. A role of myosin Vb and Rab11-FIP2 in the aquaporin-2 shuttle. Traffic 8, 110-123 (2007).
    • (2007) Traffic , vol.8 , pp. 110-123
    • Nedvetsky, P.I.1
  • 46
    • 47649098483 scopus 로고    scopus 로고
    • AQP2 exocytosis in the renal collecting duct - involvement of SNARE isoforms and the regulatory role of Munc18b
    • Procino, G. et al. AQP2 exocytosis in the renal collecting duct - involvement of SNARE isoforms and the regulatory role of Munc18b. J. Cell Sci. 121, 2097-2106 (2008).
    • (2008) J. Cell Sci , vol.121 , pp. 2097-2106
    • Procino, G.1
  • 47
    • 35349011524 scopus 로고    scopus 로고
    • Heat shock protein 70 interacts with aquaporin-2 and regulates its trafficking
    • Lu, H. A. et al. Heat shock protein 70 interacts with aquaporin-2 and regulates its trafficking. J. Biol. Chem. 282, 28721-28732 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 28721-28732
    • Lu, H.A.1
  • 48
    • 36749006124 scopus 로고    scopus 로고
    • MAL decreases the internalization of the aquaporin-2 water channel
    • Kamsteeg, E. J. et al. MAL decreases the internalization of the aquaporin-2 water channel. Proc. Natl Acad. Sci. USA 104, 16696-16701 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 16696-16701
    • Kamsteeg, E.J.1
  • 49
    • 33845307572 scopus 로고    scopus 로고
    • Short-chain ubiquitination mediates the regulated endocytosis of the aquaporin-2 water channel
    • Klumperman, J. & Deen, P. M. Short-chain ubiquitination mediates the regulated endocytosis of the aquaporin-2 water channel. Proc. Natl Acad. Sci. USA 103, 18344-18349 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 18344-18349
    • Klumperman, J.1    Deen, P.M.2
  • 50
    • 65649113317 scopus 로고    scopus 로고
    • LIP5 Interacts with aquaporin 2 and facilitates its lysosomal degradation
    • van Balkom, B. W. et al. LIP5 Interacts with aquaporin 2 and facilitates its lysosomal degradation. J. Am. Soc. Nephrol. 20, 990-1001 (2009).
    • (2009) J. Am. Soc. Nephrol , vol.20 , pp. 990-1001
    • van Balkom, B.W.1
  • 51
    • 15044340613 scopus 로고    scopus 로고
    • Hypertonicity regulates the aquaporin-2 promoter independently of arginine vasopressin
    • Kasono, K. et al. Hypertonicity regulates the aquaporin-2 promoter independently of arginine vasopressin. Nephrol. Dial. Transplant. 20, 509-515 (2005).
    • (2005) Nephrol. Dial. Transplant , vol.20 , pp. 509-515
    • Kasono, K.1
  • 52
    • 51749096176 scopus 로고    scopus 로고
    • Hypotonicity reduces the activity of murine aquaporin-2 promoter induced by dibutyryl cAMP
    • Saito, T. et al. Hypotonicity reduces the activity of murine aquaporin-2 promoter induced by dibutyryl cAMP. Exp. Physiol. 93, 1147-1156 (2008).
    • (2008) Exp. Physiol , vol.93 , pp. 1147-1156
    • Saito, T.1
  • 53
    • 55549099927 scopus 로고    scopus 로고
    • Acute hypertonicity alters aquaporin-2 trafficking and induces a MAPK-dependent accumulation at the plasma membrane of renal epithelial cells
    • Hasler, U. et al. Acute hypertonicity alters aquaporin-2 trafficking and induces a MAPK-dependent accumulation at the plasma membrane of renal epithelial cells. J. Biol. Chem. 283, 26643-26661 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 26643-26661
    • Hasler, U.1
  • 54
    • 0037428485 scopus 로고    scopus 로고
    • Hypertonicity is involved in redirecting the aquaporin-2 water channel into the basolateral, instead of the apical, plasma membrane of renal epithelial cells
    • van Balkom, B. W. et al. Hypertonicity is involved in redirecting the aquaporin-2 water channel into the basolateral, instead of the apical, plasma membrane of renal epithelial cells. J. Biol. Chem. 278, 1101-1107 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 1101-1107
    • van Balkom, B.W.1
  • 55
    • 0035310427 scopus 로고    scopus 로고
    • Receptor-mediated control of regulatory volume decrease (RVD) and apoptotic volume decrease (AVD)
    • Okada, Y. et al. Receptor-mediated control of regulatory volume decrease (RVD) and apoptotic volume decrease (AVD). J. Physiol. 532, 3-16 (2001).
    • (2001) J. Physiol , vol.532 , pp. 3-16
    • Okada, Y.1
  • 56
    • 33847053310 scopus 로고    scopus 로고
    • Hypotonicity induces aquaporin-2 internalization and cytosol-to-membrane translocation of ICln in renal cells
    • Tamma, G. et al. Hypotonicity induces aquaporin-2 internalization and cytosol-to-membrane translocation of ICln in renal cells. Endocrinology 148, 1118-1130 (2007).
    • (2007) Endocrinology , vol.148 , pp. 1118-1130
    • Tamma, G.1
  • 57
    • 70350339129 scopus 로고    scopus 로고
    • Aquaporin-2 regulates cell volume recovery via tropomyosin
    • Li, Y. H. et al. Aquaporin-2 regulates cell volume recovery via tropomyosin. Int. J. Biochem. Cell Biol. 41, 2466-2476 (2009).
    • (2009) Int. J. Biochem. Cell Biol , vol.41 , pp. 2466-2476
    • Li, Y.H.1
  • 58
    • 44349191700 scopus 로고    scopus 로고
    • Aquaporin 2 mutations in nephrogenic diabetes insipidus
    • Loonen, A. J., Knoers, N. v., van Os, C. H. & Deen, P. M. Aquaporin 2 mutations in nephrogenic diabetes insipidus. Semin. Nephrol. 28, 252-265 (2008).
    • (2008) Semin. Nephrol , vol.28 , pp. 252-265
    • Loonen, A.J.1    Knoers, N.V.2    van Os, C.H.3    Deen, P.M.4
  • 59
    • 73349112896 scopus 로고    scopus 로고
    • p.R254Q mutation in the aquaporin-2 water channel causing dominant nephrogenic diabetes insipidus is due to a lack of arginine vasopressin-induced phosphorylation
    • Savelkoul, P. J. et al. p.R254Q mutation in the aquaporin-2 water channel causing dominant nephrogenic diabetes insipidus is due to a lack of arginine vasopressin-induced phosphorylation. Hum. Mutat. 30, e891-e903 (2009).
    • (2009) Hum. Mutat , vol.30
    • Savelkoul, P.J.1
  • 60
    • 33645248184 scopus 로고    scopus 로고
    • Lack of arginine vasopressin-induced phosphorylation of aquaporin-2 mutant AQP2-R254L explains dominant nephrogenic diabetes insipidus
    • de Mattia, F. et al. Lack of arginine vasopressin-induced phosphorylation of aquaporin-2 mutant AQP2-R254L explains dominant nephrogenic diabetes insipidus. J. Am. Soc. Nephrol. 16, 2872-2880 (2005).
    • (2005) J. Am. Soc. Nephrol , vol.16 , pp. 2872-2880
    • de Mattia, F.1
  • 61
    • 38649110187 scopus 로고    scopus 로고
    • Missorting of the Aquaporin-2 mutant e258K to multivesicular bodies/lysosomes in dominant NDI is associated with its monoubiquitination and increased phosphorylation by PKC but is due to the loss of e258
    • Kamsteeg, E. J. et al. Missorting of the Aquaporin-2 mutant e258K to multivesicular bodies/lysosomes in dominant NDI is associated with its monoubiquitination and increased phosphorylation by PKC but is due to the loss of e258. Pflugers Arch. 455, 1041-1054 (2008).
    • (2008) Pflugers Arch , vol.455 , pp. 1041-1054
    • Kamsteeg, E.J.1
  • 62
    • 0037793030 scopus 로고    scopus 로고
    • Pathogenesis of nephrogenic diabetes insipidus by aquaporin-2 C-terminus mutations
    • Asai, T. et al. Pathogenesis of nephrogenic diabetes insipidus by aquaporin-2 C-terminus mutations. Kidney Int. 64, 2-10 (2003).
    • (2003) Kidney Int , vol.64 , pp. 2-10
    • Asai, T.1
  • 63
    • 33749011145 scopus 로고    scopus 로고
    • Sohara, e. et al. Pathogenesis and treatment of autosomal-dominant nephrogenic diabetes insipidus caused by an aquaporin 2 mutation. Proc. Natl Acad. Sci. USA 103, 14217-14222 (2006).
    • Sohara, e. et al. Pathogenesis and treatment of autosomal-dominant nephrogenic diabetes insipidus caused by an aquaporin 2 mutation. Proc. Natl Acad. Sci. USA 103, 14217-14222 (2006).
  • 64
  • 65
    • 15044356752 scopus 로고    scopus 로고
    • Lithium treatment inhibits renal GSK-3 activity and promotes cyclooxygenase 2-dependent polyuria
    • Rao, R. et al. Lithium treatment inhibits renal GSK-3 activity and promotes cyclooxygenase 2-dependent polyuria. Am. J. Physiol. Renal Physiol. 288, F642-F649 (2005).
    • (2005) Am. J. Physiol. Renal Physiol , vol.288
    • Rao, R.1
  • 66
    • 42149146711 scopus 로고    scopus 로고
    • Proteomic analysis of lithium-induced nephrogenic diabetes insipidus: Mechanisms for aquaporin 2 down-regulation and cellular proliferation
    • Nielsen, J. et al. Proteomic analysis of lithium-induced nephrogenic diabetes insipidus: mechanisms for aquaporin 2 down-regulation and cellular proliferation. Proc. Natl Acad. Sci. USA 105, 3634-3639 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 3634-3639
    • Nielsen, J.1
  • 68
    • 68249162271 scopus 로고    scopus 로고
    • Acute and chronic metabolic acidosis interferes with aquaporin-2 translocation in the rat kidney collecting ducts
    • Mouri, T. et al. Acute and chronic metabolic acidosis interferes with aquaporin-2 translocation in the rat kidney collecting ducts. Hypertens. Res. 32, 358-363 (2009).
    • (2009) Hypertens. Res , vol.32 , pp. 358-363
    • Mouri, T.1
  • 69
    • 33746586548 scopus 로고    scopus 로고
    • Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus
    • Robben, J. H., Knoers, N. V. & Deen, P. M. Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus. Am. J. Physiol. Renal Physiol. 291, F257-F270 (2006).
    • (2006) Am. J. Physiol. Renal Physiol , vol.291
    • Robben, J.H.1    Knoers, N.V.2    Deen, P.M.3
  • 70
    • 16644391083 scopus 로고    scopus 로고
    • Antidiuretic effect of hydrochlorothiazide in lithium-induced nephrogenic diabetes insipidus is associated with upregulation of aquaporin-2, Na-Cl cotransporter, and epithelial sodium channel
    • Kim, G. H. et al. Antidiuretic effect of hydrochlorothiazide in lithium-induced nephrogenic diabetes insipidus is associated with upregulation of aquaporin-2, Na-Cl cotransporter, and epithelial sodium channel. J. Am. Soc. Nephrol. 15, 2836-2843 (2004).
    • (2004) J. Am. Soc. Nephrol , vol.15 , pp. 2836-2843
    • Kim, G.H.1
  • 71
    • 70349655689 scopus 로고    scopus 로고
    • A selective eP4 PGe2 receptor agonist alleviates disease in a new mouse model of X-linked nephrogenic diabetes insipidus
    • Li, J. H. et al. A selective eP4 PGe2 receptor agonist alleviates disease in a new mouse model of X-linked nephrogenic diabetes insipidus. J. Clin. Invest. 119, 3115-3126 (2009).
    • (2009) J. Clin. Invest , vol.119 , pp. 3115-3126
    • Li, J.H.1
  • 72
    • 54349101783 scopus 로고    scopus 로고
    • Novel treatment for lithium-induced nephrogenic diabetes insipidus rat model using the Sendai-virus vector carrying aquaporin 2 gene
    • Suga, H. et al. Novel treatment for lithium-induced nephrogenic diabetes insipidus rat model using the Sendai-virus vector carrying aquaporin 2 gene. Endocrinology 149, 5803-5810 (2008).
    • (2008) Endocrinology , vol.149 , pp. 5803-5810
    • Suga, H.1
  • 73
    • 0019861237 scopus 로고
    • Radioimmunoassay of plasma arginine vasopressin in hyponatremic patients with congestive heart failure
    • Szatalowicz, V. L. et al. Radioimmunoassay of plasma arginine vasopressin in hyponatremic patients with congestive heart failure. N. Engl. J. Med. 305, 263-266 (1981).
    • (1981) N. Engl. J. Med , vol.305 , pp. 263-266
    • Szatalowicz, V.L.1
  • 74
    • 44449114684 scopus 로고    scopus 로고
    • Schrier, R. W. vasopressin and aquaporin 2 in clinical disorders of water homeostasis. Semin. Nephrol. 28, 289-296 (2008).
    • Schrier, R. W. vasopressin and aquaporin 2 in clinical disorders of water homeostasis. Semin. Nephrol. 28, 289-296 (2008).
  • 75
    • 0030922702 scopus 로고    scopus 로고
    • Congestive heart failure in rats is associated with increased expression and targeting of aquaporin-2 water channel in collecting duct
    • Nielsen, S. et al. Congestive heart failure in rats is associated with increased expression and targeting of aquaporin-2 water channel in collecting duct. Proc. Natl Acad. Sci. USA 94, 5450-5455 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5450-5455
    • Nielsen, S.1
  • 76
    • 0030899402 scopus 로고    scopus 로고
    • Upregulation of aquaporin-2 water channel expression in chronic heart failure
    • Xu, D. L. et al. Upregulation of aquaporin-2 water channel expression in chronic heart failure. J. Clin. Invest. 99, 1500-1505 (1997).
    • (1997) J. Clin. Invest , vol.99 , pp. 1500-1505
    • Xu, D.L.1
  • 77
    • 11144355788 scopus 로고    scopus 로고
    • effects of tolvaptan, a vasopressin antagonist, in patients hospitalized with worsening heart failure: A randomized controlled trial
    • Gheorghiade, M. et al. effects of tolvaptan, a vasopressin antagonist, in patients hospitalized with worsening heart failure: a randomized controlled trial. JAMA 291, 1963-1971 (2004).
    • (2004) JAMA , vol.291 , pp. 1963-1971
    • Gheorghiade, M.1
  • 78
    • 33751005260 scopus 로고    scopus 로고
    • SALT Investigators. Tolvaptan, a selective oral vasopressin V2-receptor antagonist, for hyponatremia
    • Schrier, R. W. et al.; SALT Investigators. Tolvaptan, a selective oral vasopressin V2-receptor antagonist, for hyponatremia. N. Engl. J. Med. 355, 2099-2112 (2006).
    • (2006) N. Engl. J. Med , vol.355 , pp. 2099-2112
    • Schrier, R.W.1
  • 79
    • 33646054125 scopus 로고    scopus 로고
    • Aquaretic effect of lixivaptan, an oral non-peptide, selective V2 receptor vasopressin antagonist, in the New York Heart Association functional class II and III chronic heart failure patients
    • Abraham, W. T., Shamshirsaz, A. A., McFann, K., Oren, R. M. & Schrier, R. W. Aquaretic effect of lixivaptan, an oral non-peptide, selective V2 receptor vasopressin antagonist, in the New York Heart Association functional class II and III chronic heart failure patients. J. Am. Coll. Cardiol. 47, 1615-1621 (2006).
    • (2006) J. Am. Coll. Cardiol , vol.47 , pp. 1615-1621
    • Abraham, W.T.1    Shamshirsaz, A.A.2    McFann, K.3    Oren, R.M.4    Schrier, R.W.5
  • 80
    • 33947719178 scopus 로고    scopus 로고
    • Short-term clinical effects of tolvaptan, an oral vasopressin antagonist, in patients hospitalized for heart failure: The EVEREST Clinical Status Trials
    • Gheorghiade, M. et al. Short-term clinical effects of tolvaptan, an oral vasopressin antagonist, in patients hospitalized for heart failure: the EVEREST Clinical Status Trials. JAMA 297, 1332-1343 (2007).
    • (2007) JAMA , vol.297 , pp. 1332-1343
    • Gheorghiade, M.1
  • 81
    • 0028814505 scopus 로고
    • Increased gene expression of water channel in cirrhotic rat kidneys
    • Asahina, Y. et al. Increased gene expression of water channel in cirrhotic rat kidneys. Hepatology 21, 169-173 (1995).
    • (1995) Hepatology , vol.21 , pp. 169-173
    • Asahina, Y.1
  • 82
    • 0344806948 scopus 로고    scopus 로고
    • Therapy of hyponatremia in cirrhosis with a vasopressin receptor antagonist: A randomized double-blind multicenter trial
    • Gerbes, A. L. et al. Therapy of hyponatremia in cirrhosis with a vasopressin receptor antagonist: a randomized double-blind multicenter trial. Gastroenterology 124, 933-939 (2003).
    • (2003) Gastroenterology , vol.124 , pp. 933-939
    • Gerbes, A.L.1
  • 83
    • 0032030773 scopus 로고    scopus 로고
    • Upregulation of aquaporin 2 water channel expression in pregnant rats
    • Ohara, M. et al. Upregulation of aquaporin 2 water channel expression in pregnant rats. J. Clin. Invest. 101, 1076-1083 (1998).
    • (1998) J. Clin. Invest , vol.101 , pp. 1076-1083
    • Ohara, M.1
  • 84
    • 7844247177 scopus 로고    scopus 로고
    • Temporal relationships between hormonal and hemodynamic changes in early human pregnancy
    • Chapman, A. B. et al. Temporal relationships between hormonal and hemodynamic changes in early human pregnancy. Kidney Int. 54, 2056-2063 (1998).
    • (1998) Kidney Int , vol.54 , pp. 2056-2063
    • Chapman, A.B.1
  • 85
    • 0030661811 scopus 로고    scopus 로고
    • Reduced renal medullary water channel expression in puromycin aminonucleoside-induced nephrotic syndrome
    • Apostol, E. et al. Reduced renal medullary water channel expression in puromycin aminonucleoside-induced nephrotic syndrome. J. Am. Soc. Nephrol. 8, 15-24 (1997).
    • (1997) J. Am. Soc. Nephrol , vol.8 , pp. 15-24
    • Apostol, E.1
  • 86
    • 0021139597 scopus 로고
    • Renal water handling in minimal change nephrotic syndrome
    • Bohlin, A. B. & Berg, U. Renal water handling in minimal change nephrotic syndrome. Int. J. Pediat. Nephrol. 5, 93-98 (1984).
    • (1984) Int. J. Pediat. Nephrol , vol.5 , pp. 93-98
    • Bohlin, A.B.1    Berg, U.2
  • 87
    • 0031836231 scopus 로고    scopus 로고
    • Concentrating defect in experimental nephrotic syndrome: Altered expression of aquaporins and thick ascending limb Na+ transporters
    • Fernández-Llama, P. et al. Concentrating defect in experimental nephrotic syndrome: altered expression of aquaporins and thick ascending limb Na+ transporters. Kidney Int. 54, 170-179 (1998).
    • (1998) Kidney Int , vol.54 , pp. 170-179
    • Fernández-Llama, P.1
  • 88
    • 47549086678 scopus 로고    scopus 로고
    • Pathophysiological role of aquaporin-2 in impaired water excretion
    • Ishikawa, S. E., Saito, T., Saito, T., Kasono, K. & Funayama, H. Pathophysiological role of aquaporin-2 in impaired water excretion. Prog. Brain Res. 170, 581-588 (2008).
    • (2008) Prog. Brain Res , vol.170 , pp. 581-588
    • Ishikawa, S.E.1    Saito, T.2    Saito, T.3    Kasono, K.4    Funayama, H.5
  • 89
    • 0031001022 scopus 로고    scopus 로고
    • Acute aquaresis by the nonpeptide arginine vasopressin (AVP) antagonist OPC-31260 improves hyponatremia in patients with syndrome of inappropriate secretion of antidiuretic hormone (SIADH)
    • Saito, T. et al. Acute aquaresis by the nonpeptide arginine vasopressin (AVP) antagonist OPC-31260 improves hyponatremia in patients with syndrome of inappropriate secretion of antidiuretic hormone (SIADH). J. Clin. Endocrinol. Metab. 82, 1054-1057 (1997).
    • (1997) J. Clin. Endocrinol. Metab , vol.82 , pp. 1054-1057
    • Saito, T.1
  • 90
    • 20244371679 scopus 로고    scopus 로고
    • BSC1 inhibition complements effects of vasopressin V2 receptor antagonist on hyponatremia in SIADH rats
    • Kazama, I. et al. BSC1 inhibition complements effects of vasopressin V2 receptor antagonist on hyponatremia in SIADH rats. Kidney Int. 67, 1855-1867 (2005).
    • (2005) Kidney Int , vol.67 , pp. 1855-1867
    • Kazama, I.1
  • 91
    • 0029007846 scopus 로고
    • Urinary excretion of aquaporin-2 in patients with diabetes insipidus
    • Kanno, K. et al. Urinary excretion of aquaporin-2 in patients with diabetes insipidus. N. Engl. J. Med. 332, 1540-1545 (1995).
    • (1995) N. Engl. J. Med , vol.332 , pp. 1540-1545
    • Kanno, K.1
  • 92
    • 4444226979 scopus 로고    scopus 로고
    • Identification and proteomic profiling of exosomes in human urine
    • Pisitkun, T., Shen, R. F. & Knepper, M. A. Identification and proteomic profiling of exosomes in human urine. Proc. Natl Acad. Sci. USA 101, 13368-13373 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 13368-13373
    • Pisitkun, T.1    Shen, R.F.2    Knepper, M.A.3
  • 93
    • 0032845180 scopus 로고    scopus 로고
    • Selective V2-receptor vasopressin antagonism decreases urinary aquaporin-2 excretion in patients with chronic heart failure
    • Martin, P. Y. et al. Selective V2-receptor vasopressin antagonism decreases urinary aquaporin-2 excretion in patients with chronic heart failure. J. Am. Soc. Nephrol. 10, 2165-2170 (1999).
    • (1999) J. Am. Soc. Nephrol , vol.10 , pp. 2165-2170
    • Martin, P.Y.1
  • 94
    • 0038637372 scopus 로고    scopus 로고
    • Increased urinary excretion of aquaporin 2 in patients with liver cirrhosis
    • Ivarsen, P. et al. Increased urinary excretion of aquaporin 2 in patients with liver cirrhosis. Gut 52, 1194-1199 (2003).
    • (2003) Gut , vol.52 , pp. 1194-1199
    • Ivarsen, P.1
  • 95
    • 0034866721 scopus 로고    scopus 로고
    • Urinary excretion of aquaporin-2 water channel during pregnancy
    • Buemi, M. et al. Urinary excretion of aquaporin-2 water channel during pregnancy. Cell. Physiol. Biochem. 11, 203-208 (2001).
    • (2001) Cell. Physiol. Biochem , vol.11 , pp. 203-208
    • Buemi, M.1
  • 96
    • 0035040061 scopus 로고    scopus 로고
    • Close association of urinary excretion of aquaporin-2 with appropriate and inappropriate arginine vasopressin-dependent antidiuresis in hyponatremia in elderly subjects
    • Ishikawa, S. et al. Close association of urinary excretion of aquaporin-2 with appropriate and inappropriate arginine vasopressin-dependent antidiuresis in hyponatremia in elderly subjects. J. Clin. Endocrinol. Metab. 86, 1665-1671 (2001).
    • (2001) J. Clin. Endocrinol. Metab , vol.86 , pp. 1665-1671
    • Ishikawa, S.1
  • 97
    • 44349175657 scopus 로고    scopus 로고
    • Dissecting the roles of aquaporins in renal pathophysiology using transgenic mice
    • Verkman, A. S. Dissecting the roles of aquaporins in renal pathophysiology using transgenic mice. Semin. Nephrol. 28, 217-226 (2008).
    • (2008) Semin. Nephrol , vol.28 , pp. 217-226
    • Verkman, A.S.1
  • 98
    • 0033955098 scopus 로고    scopus 로고
    • Requirement of aquaporin-1 for NaCl-driven water transport across descending vasa recta
    • Pallone, T. L., edwards, A., Ma, T., Silldorff, E. P. & Verkman, A. S. Requirement of aquaporin-1 for NaCl-driven water transport across descending vasa recta. J. Clin. Invest. 105, 215-222 (2000).
    • (2000) J. Clin. Invest , vol.105 , pp. 215-222
    • Pallone, T.L.1    edwards, A.2    Ma, T.3    Silldorff, E.P.4    Verkman, A.S.5
  • 99
    • 0035913207 scopus 로고    scopus 로고
    • Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1
    • King, L. S., Choi, M., Fernandez, P. C., Cartron, J. P. & Agre, P. Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1. N. Engl. J. Med. 345, 175-179 (2001).
    • (2001) N. Engl. J. Med , vol.345 , pp. 175-179
    • King, L.S.1    Choi, M.2    Fernandez, P.C.3    Cartron, J.P.4    Agre, P.5
  • 100
    • 0037306652 scopus 로고    scopus 로고
    • Renal aquaporin water channels: From molecules to human disease
    • Schrier, R. W. & Cadnapaphornchai, M. A. Renal aquaporin water channels: from molecules to human disease. Prog. Biophys. Mol. Biol. 81, 117-131 (2003).
    • (2003) Prog. Biophys. Mol. Biol , vol.81 , pp. 117-131
    • Schrier, R.W.1    Cadnapaphornchai, M.A.2
  • 101
    • 17144379334 scopus 로고    scopus 로고
    • Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption
    • Saadoun, S., Papadopoulos, M. C., Hara-Chikuma, M. & Verkman, A. S. Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption. Nature 434, 786-792 (2005).
    • (2005) Nature , vol.434 , pp. 786-792
    • Saadoun, S.1    Papadopoulos, M.C.2    Hara-Chikuma, M.3    Verkman, A.S.4
  • 102
    • 33645457522 scopus 로고    scopus 로고
    • Aquaporin-1 facilitates epithelial cell migration in kidney proximal tubule
    • Hara-Chikuma, M. & Verkman, A. S. Aquaporin-1 facilitates epithelial cell migration in kidney proximal tubule. J. Am. Soc. Nephrol. 17, 39-45 (2006).
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 39-45
    • Hara-Chikuma, M.1    Verkman, A.S.2
  • 103
    • 48249098273 scopus 로고    scopus 로고
    • Role of AQP1 in endotoxemia-induced acute kidney injury
    • Wang, W. et al. Role of AQP1 in endotoxemia-induced acute kidney injury. Am. J. Physiol. Renal Physiol. 294, F1473-F1480 (2008).
    • (2008) Am. J. Physiol. Renal Physiol , vol.294
    • Wang, W.1
  • 104
    • 0036889503 scopus 로고    scopus 로고
    • Regulation of collecting duct AQP3 expression: Response to mineralocorticoid
    • Kwon, T. H. et al. Regulation of collecting duct AQP3 expression: response to mineralocorticoid. Am. J. Physiol. Renal Physiol. 283, F1403-F1421 (2002).
    • (2002) Am. J. Physiol. Renal Physiol , vol.283
    • Kwon, T.H.1
  • 105
    • 0037195785 scopus 로고    scopus 로고
    • AQP3 deficiency in humans and the molecular basis of a novel blood group system, GIL
    • Roudier, N. et al. AQP3 deficiency in humans and the molecular basis of a novel blood group system, GIL. J. Biol. Chem. 277, 45854-45859 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 45854-45859
    • Roudier, N.1
  • 106
    • 0030909563 scopus 로고    scopus 로고
    • Very high single channel water permeability of aquaporin-4 in baculovirus-infected insect cells and liposomes reconstituted with purified aquaporin-4
    • Yang, B., van Hoek, A. N. & Verkman, A. S. Very high single channel water permeability of aquaporin-4 in baculovirus-infected insect cells and liposomes reconstituted with purified aquaporin-4. Biochemistry 36, 7625-7632 (1997).
    • (1997) Biochemistry , vol.36 , pp. 7625-7632
    • Yang, B.1    van Hoek, A.N.2    Verkman, A.S.3
  • 108
    • 66449091749 scopus 로고    scopus 로고
    • Vasopressin-induced differential stimulation of AQP4 splice variants regulates the in-membrane assembly of orthogonal arrays
    • van Hoek, A. N. et al. Vasopressin-induced differential stimulation of AQP4 splice variants regulates the in-membrane assembly of orthogonal arrays. Am. J. Physiol. Renal Physiol. 296, F1396-F1404 (2009).
    • (2009) Am. J. Physiol. Renal Physiol , vol.296
    • van Hoek, A.N.1
  • 109
    • 29144521255 scopus 로고    scopus 로고
    • Implications of the aquaporin-4 structure on array formation and cell adhesion
    • Hiroaki, Y. et al. Implications of the aquaporin-4 structure on array formation and cell adhesion. J. Mol. Biol. 355, 628-639 (2006).
    • (2006) J. Mol. Biol , vol.355 , pp. 628-639
    • Hiroaki, Y.1
  • 110
    • 66149097844 scopus 로고    scopus 로고
    • Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductance
    • Ho, J. D. et al. Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductance. Proc. Natl Acad. Sci. USA 106, 7437-7442 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 7437-7442
    • Ho, J.D.1
  • 111
    • 61449324888 scopus 로고    scopus 로고
    • pH regulated anion permeability of aquaporin-6
    • Yasui, M. pH regulated anion permeability of aquaporin-6. Handb. Exp. Pharmacol. 190, 299-308 (2009).
    • (2009) Handb. Exp. Pharmacol , vol.190 , pp. 299-308
    • Yasui, M.1
  • 112
    • 0033547240 scopus 로고    scopus 로고
    • Rapid gating and anion permeability of an intracellular aquaporin
    • Yasui, M. et al. Rapid gating and anion permeability of an intracellular aquaporin. Nature 402, 184-187 (1999).
    • (1999) Nature , vol.402 , pp. 184-187
    • Yasui, M.1
  • 113
    • 0033545980 scopus 로고    scopus 로고
    • Aquaporin-6: An intracellular vesicle water channel protein in renal epithelia
    • Yasui, M., Kwon, T. H., Knepper, M. A., Nielsen, S. & Agre, P. Aquaporin-6: an intracellular vesicle water channel protein in renal epithelia. Proc. Natl Acad. Sci. USA 96, 5808-5813 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 5808-5813
    • Yasui, M.1    Kwon, T.H.2    Knepper, M.A.3    Nielsen, S.4    Agre, P.5
  • 114
    • 0034856292 scopus 로고    scopus 로고
    • expression and immunolocalization of AQP6 in intercalated cells of the rat kidney collecting duct
    • Ohshiro, K. et al. expression and immunolocalization of AQP6 in intercalated cells of the rat kidney collecting duct. Arch. Histol. Cytol. 64, 329-338 (2001).
    • (2001) Arch. Histol. Cytol , vol.64 , pp. 329-338
    • Ohshiro, K.1
  • 115
    • 0037131175 scopus 로고    scopus 로고
    • Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63
    • Ikeda, M. et al. Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63. J. Biol. Chem. 277, 39873-39879 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 39873-39879
    • Ikeda, M.1
  • 116
    • 0032493276 scopus 로고    scopus 로고
    • CIC-5, the chloride channel mutated in Dent's disease, colocalizes with the proton pump in endocytotically active kidney cells
    • Günther, W., Lüchow, A., Cluzeaud, F., Vandewalle, A. & Jentsch, T. J. CIC-5, the chloride channel mutated in Dent's disease, colocalizes with the proton pump in endocytotically active kidney cells. Proc. Natl Acad. Sci. USA 95, 8075-8080 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8075-8080
    • Günther, W.1    Lüchow, A.2    Cluzeaud, F.3    Vandewalle, A.4    Jentsch, T.J.5
  • 117
    • 0033534733 scopus 로고    scopus 로고
    • Mutational analysis demonstrates that CIC-4 and CIC-5 directly mediate plasma membrane currents
    • Friedrich, T., Breiderhoff, T. & Jentsch, T. J. Mutational analysis demonstrates that CIC-4 and CIC-5 directly mediate plasma membrane currents. J. Biol. Chem. 274, 896-902 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 896-902
    • Friedrich, T.1    Breiderhoff, T.2    Jentsch, T.J.3
  • 118
    • 13844310859 scopus 로고    scopus 로고
    • Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution
    • Liu, K. et al. Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution. Proc. Natl Acad. Sci. USA 102, 2192-2197 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 2192-2197
    • Liu, K.1
  • 119
    • 18144401213 scopus 로고    scopus 로고
    • Progressive adipocyte hypertrophy in aquaporin-7-deficient mice: Adipocyte glycerol permeability as a novel regulator of fat accumulation
    • Hara-Chikuma, M. et al. Progressive adipocyte hypertrophy in aquaporin-7-deficient mice: adipocyte glycerol permeability as a novel regulator of fat accumulation. J. Biol. Chem. 280, 15493-15496 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 15493-15496
    • Hara-Chikuma, M.1
  • 120
    • 0034649121 scopus 로고    scopus 로고
    • Localization of aquaporin-7 in rat and mouse kidney using RT-PCR, immunoblotting, and immunocytochemistry
    • Nejsum, L. N. et al. Localization of aquaporin-7 in rat and mouse kidney using RT-PCR, immunoblotting, and immunocytochemistry. Biochem. Biophys. Res. Commun. 277, 164-170 (2000).
    • (2000) Biochem. Biophys. Res. Commun , vol.277 , pp. 164-170
    • Nejsum, L.N.1
  • 121
    • 27944431760 scopus 로고    scopus 로고
    • Defective water and glycerol transport in the proximal tubules of AQP7 knockout mice
    • Sohara, E. et al. Defective water and glycerol transport in the proximal tubules of AQP7 knockout mice. Am. J. Physiol. Renal Physiol. 289, F1195-F1200 (2005).
    • (2005) Am. J. Physiol. Renal Physiol , vol.289
    • Sohara, E.1
  • 122
    • 33748547734 scopus 로고    scopus 로고
    • Physiological roles of AQP7 in the kidney: Lessons from AQP7 knockout mice
    • Sohara, E., Rai, T., Sasaki, S. & Uchida, S. Physiological roles of AQP7 in the kidney: lessons from AQP7 knockout mice. Biochim. Biophys. Acta 1758, 1106-1110 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1106-1110
    • Sohara, E.1    Rai, T.2    Sasaki, S.3    Uchida, S.4
  • 123
    • 85047699748 scopus 로고    scopus 로고
    • Human aquaporin adipose (AQPap) gene. Genomic structure, promoter analysis and functional mutation
    • Kondo, H. et al. Human aquaporin adipose (AQPap) gene. Genomic structure, promoter analysis and functional mutation. Eur. J. Biochem. 269, 1814-1826 (2002).
    • (2002) Eur. J. Biochem , vol.269 , pp. 1814-1826
    • Kondo, H.1
  • 124
    • 10944255127 scopus 로고    scopus 로고
    • Molecular mechanisms and drug development in aquaporin water channel diseases: Aquaporin superfamily (superaquaporins): expansion of aquaporins restricted to multicellular organisms
    • Morishita, Y., Sakube, Y., Sasaki, S. & Ishibashi, K. Molecular mechanisms and drug development in aquaporin water channel diseases: aquaporin superfamily (superaquaporins): expansion of aquaporins restricted to multicellular organisms. J. Pharmacol. Sci. 96, 276-279 (2004).
    • (2004) J. Pharmacol. Sci , vol.96 , pp. 276-279
    • Morishita, Y.1    Sakube, Y.2    Sasaki, S.3    Ishibashi, K.4
  • 125
    • 16244383536 scopus 로고    scopus 로고
    • Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar cells
    • Itoh, T. et al. Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar cells. Biochem. Biophys. Res. Commun. 330, 832-838 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.330 , pp. 832-838
    • Itoh, T.1
  • 126
    • 33748560815 scopus 로고    scopus 로고
    • Aquaporin subfamily with unusual NPA boxes
    • Ishibashi, K. Aquaporin subfamily with unusual NPA boxes. Biochim. Biophys. Acta 1758, 989-993 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 989-993
    • Ishibashi, K.1
  • 127
    • 23844498483 scopus 로고    scopus 로고
    • Disruption of aquaporin-11 produces polycystic kidneys following vacuolization of the proximal tubule
    • Morishita, Y. et al. Disruption of aquaporin-11 produces polycystic kidneys following vacuolization of the proximal tubule. Mol. Cell. Biol. 25, 7770-7779 (2005).
    • (2005) Mol. Cell. Biol , vol.25 , pp. 7770-7779
    • Morishita, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.