메뉴 건너뛰기




Volumn 415, Issue 1, 2011, Pages 125-130

Quantitative analysis of ascorbic acid permeability of aquaporin 0 in the lens

Author keywords

Aquaporin 0; Ascorbic acid; Channel

Indexed keywords

2,6 DICHLOROPHENOLINDOPHENOL; AQUAPORIN; AQUAPORIN 0; ASCORBIC ACID; COMPLEMENTARY RNA; UNCLASSIFIED DRUG;

EID: 80755140503     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.10.028     Document Type: Article
Times cited : (9)

References (35)
  • 1
    • 0021712623 scopus 로고
    • The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning
    • Gorin M.B., Yancey S.B., Cline J., et al. The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning. Cell 1984, 39:49-89.
    • (1984) Cell , vol.39 , pp. 49-89
    • Gorin, M.B.1    Yancey, S.B.2    Cline, J.3
  • 2
    • 0023856874 scopus 로고
    • Expression of the gene for main intrinsic polypeptide (MIP): separate spatial distributions of MIP and beta-crystallin gene transcripts in rat lens development
    • Yancey S.B., Koh K., Chung J., et al. Expression of the gene for main intrinsic polypeptide (MIP): separate spatial distributions of MIP and beta-crystallin gene transcripts in rat lens development. J. Cell Biol. 1988, 106:705-714.
    • (1988) J. Cell Biol. , vol.106 , pp. 705-714
    • Yancey, S.B.1    Koh, K.2    Chung, J.3
  • 3
    • 0028921171 scopus 로고
    • Water channel properties of major intrinsic protein of lens
    • Mulders S.M., Preston G.M., Deen P.M., et al. Water channel properties of major intrinsic protein of lens. J. Biol. Chem. 1995, 270:9010-9016.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9010-9016
    • Mulders, S.M.1    Preston, G.M.2    Deen, P.M.3
  • 4
    • 0029086075 scopus 로고
    • Ion, water and neutral solute transport in Xenopus oocytes expressing frog lens MIP
    • Kushmerick C., Rice S.J., Baldo G.J., et al. Ion, water and neutral solute transport in Xenopus oocytes expressing frog lens MIP. Exp. Eye Res. 1995, 61:351-362.
    • (1995) Exp. Eye Res. , vol.61 , pp. 351-362
    • Kushmerick, C.1    Rice, S.J.2    Baldo, G.J.3
  • 5
    • 0030031158 scopus 로고    scopus 로고
    • Mutations in the founder of the MIP gene family underlie cataract development in the mouse
    • Shiels A., Bassnett S. Mutations in the founder of the MIP gene family underlie cataract development in the mouse. Nat. Genet. 1996, 12:212-215.
    • (1996) Nat. Genet. , vol.12 , pp. 212-215
    • Shiels, A.1    Bassnett, S.2
  • 6
    • 0034118380 scopus 로고    scopus 로고
    • Missense mutations in MIP underlie autosomal dominant 'polymorphic' and lamellar cataracts linked to 12q
    • Berry V., Francis P., Kaushal S., et al. Missense mutations in MIP underlie autosomal dominant 'polymorphic' and lamellar cataracts linked to 12q. Nat. Genet. 2000, 25:15-17.
    • (2000) Nat. Genet. , vol.25 , pp. 15-17
    • Berry, V.1    Francis, P.2    Kaushal, S.3
  • 7
    • 0035874985 scopus 로고    scopus 로고
    • A 76-bp deletion in the Mip gene causes autosomal dominant cataract in Hfi mice
    • Sidjanin D.J., Parker-Wilson D.M., Neuhäuser-Klaus A., et al. A 76-bp deletion in the Mip gene causes autosomal dominant cataract in Hfi mice. Genomics 2001, 74:313-319.
    • (2001) Genomics , vol.74 , pp. 313-319
    • Sidjanin, D.J.1    Parker-Wilson, D.M.2    Neuhäuser-Klaus, A.3
  • 8
    • 0021969813 scopus 로고
    • Lens cell-to-cell channel protein: I. Self-assembly into liposomes and permeability regulation by calmodulin
    • Girsch S.J., Peracchia C. Lens cell-to-cell channel protein: I. Self-assembly into liposomes and permeability regulation by calmodulin. J. Membr. Biol. 1985, 83:217-225.
    • (1985) J. Membr. Biol. , vol.83 , pp. 217-225
    • Girsch, S.J.1    Peracchia, C.2
  • 9
    • 0023607808 scopus 로고
    • Pro-oxidant activation of ocular reductants. 1: Copper and riboflavin stimulate ascorbate oxidation causing lens epithelial cytotoxicity in vitro
    • Wolff S.P., Wang G.M., Spector A. Pro-oxidant activation of ocular reductants. 1: Copper and riboflavin stimulate ascorbate oxidation causing lens epithelial cytotoxicity in vitro. Exp. Eye Res. 1987, 45:777-789.
    • (1987) Exp. Eye Res. , vol.45 , pp. 777-789
    • Wolff, S.P.1    Wang, G.M.2    Spector, A.3
  • 10
    • 0023755231 scopus 로고
    • Ascorbate free radical reductase and ascorbate redox cycle in the human lens
    • Bando M., Obazawa H. Ascorbate free radical reductase and ascorbate redox cycle in the human lens. Jpn. J. Ophthalmol. 1988, 32:176-186.
    • (1988) Jpn. J. Ophthalmol. , vol.32 , pp. 176-186
    • Bando, M.1    Obazawa, H.2
  • 11
    • 0028237665 scopus 로고
    • Polyamines mediate coronary transcapillary macromolecular transport in the calcium paradox
    • Trout J.J., Lu C.Y., Goldstone A.D., et al. Polyamines mediate coronary transcapillary macromolecular transport in the calcium paradox. J. Mol. Cell Cardiol. 1994, 26:369-377.
    • (1994) J. Mol. Cell Cardiol. , vol.26 , pp. 369-377
    • Trout, J.J.1    Lu, C.Y.2    Goldstone, A.D.3
  • 12
    • 0032582815 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of rat liver glutathione-dependent dehydroascorbate reductase
    • Ishikawa T., Casini A.F., Nishikimi M. Molecular cloning and functional expression of rat liver glutathione-dependent dehydroascorbate reductase. J. Biol. Chem. 1998, 273:28708-28712.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28708-28712
    • Ishikawa, T.1    Casini, A.F.2    Nishikimi, M.3
  • 14
    • 0032705918 scopus 로고    scopus 로고
    • Cloning and functional characterization of the human sodium-dependent vitamin C transporters hSVCT1 and hSVCT2
    • Daruwala R., Song J., Koh W.S., et al. Cloning and functional characterization of the human sodium-dependent vitamin C transporters hSVCT1 and hSVCT2. FEBS Lett. 1999, 460:480-484.
    • (1999) FEBS Lett. , vol.460 , pp. 480-484
    • Daruwala, R.1    Song, J.2    Koh, W.S.3
  • 15
    • 0026808764 scopus 로고
    • Biochemical and immunocytochemical localization of the 'GLUT5 glucose transporter' in human skeletal muscle
    • Hundal H.S., Ahmed A., Gumà A., et al. Biochemical and immunocytochemical localization of the 'GLUT5 glucose transporter' in human skeletal muscle. Biochem. J. 1992, 286:339-343.
    • (1992) Biochem. J. , vol.286 , pp. 339-343
    • Hundal, H.S.1    Ahmed, A.2    Gumà, A.3
  • 16
    • 0030839797 scopus 로고    scopus 로고
    • Glucose transporter isoforms GLUT1 and GLUT3 transport dehydroascorbic acid
    • Rumsey S.C., Kwon O., Xu G.W., et al. Glucose transporter isoforms GLUT1 and GLUT3 transport dehydroascorbic acid. J. Biol. Chem. 1997, 272:18982-18989.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18982-18989
    • Rumsey, S.C.1    Kwon, O.2    Xu, G.W.3
  • 17
    • 0034623248 scopus 로고    scopus 로고
    • Dehydroascorbic acid transport by GLUT4 in Xenopus oocytes and isolated rat adipocytes
    • Rumsey S.C., Daruwala R., Al-Hasani H., et al. Dehydroascorbic acid transport by GLUT4 in Xenopus oocytes and isolated rat adipocytes. J. Biol. Chem. 2000, 275:28246-28253.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28246-28253
    • Rumsey, S.C.1    Daruwala, R.2    Al-Hasani, H.3
  • 18
    • 0042343871 scopus 로고    scopus 로고
    • Expression patterns for glucose transporters GLUT1 and GLUT3 in the normal rat lens and in models of diabetic cataract
    • Merriman-Smith B.R., Krushinsky A., Kistler J., et al. Expression patterns for glucose transporters GLUT1 and GLUT3 in the normal rat lens and in models of diabetic cataract. Invest. Ophthalmol. Vis. Sci. 2003, 44:2458-2466.
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 2458-2466
    • Merriman-Smith, B.R.1    Krushinsky, A.2    Kistler, J.3
  • 19
    • 0034775202 scopus 로고    scopus 로고
    • Vitamin C transport in human lens epithelial cells: evidence for the presence of SVCT2
    • Kannan R., Stolz A., Ji Q., et al. Vitamin C transport in human lens epithelial cells: evidence for the presence of SVCT2. Exp. Eye Res. 2001, 73:159-165.
    • (2001) Exp. Eye Res. , vol.73 , pp. 159-165
    • Kannan, R.1    Stolz, A.2    Ji, Q.3
  • 20
    • 0032700497 scopus 로고    scopus 로고
    • Differential expression of facilitative glucose transporters GLUT1 and GLUT3 in the lens
    • Merriman-Smith R., Donaldson P., Kistler J. Differential expression of facilitative glucose transporters GLUT1 and GLUT3 in the lens. Invest. Ophthalmol. Vis. Sci. 1999, 40:3224-3230.
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 3224-3230
    • Merriman-Smith, R.1    Donaldson, P.2    Kistler, J.3
  • 21
    • 0024497439 scopus 로고
    • Ascorbic acid metabolism and polyol pathway in diabetes
    • Yue D.K., McLennan S., Fisher E., et al. Ascorbic acid metabolism and polyol pathway in diabetes. Diabetes 1989, 38:257-261.
    • (1989) Diabetes , vol.38 , pp. 257-261
    • Yue, D.K.1    McLennan, S.2    Fisher, E.3
  • 22
    • 0026737280 scopus 로고
    • Decreased ascorbic acid entry into cornea of streptozotocin-diabetic rats and guinea-pigs
    • DiMattio J. Decreased ascorbic acid entry into cornea of streptozotocin-diabetic rats and guinea-pigs. Exp. Eye Res. 1992, 55:337-344.
    • (1992) Exp. Eye Res. , vol.55 , pp. 337-344
    • DiMattio, J.1
  • 23
    • 0026775963 scopus 로고
    • Alterations in ascorbic acid transport into the lens of streptozotocin-induced diabetic rats and guinea pigs
    • DiMattio J. Alterations in ascorbic acid transport into the lens of streptozotocin-induced diabetic rats and guinea pigs. Invest. Ophthalmol. Vis. Sci. 1992, 33:2926-2935.
    • (1992) Invest. Ophthalmol. Vis. Sci. , vol.33 , pp. 2926-2935
    • DiMattio, J.1
  • 24
    • 85043352215 scopus 로고    scopus 로고
    • The role of ascorbic acid transporter in the lens of streptozotocin-induced diabetic rat
    • [Epub ahead of print].
    • Y. Nakazawa, M. Oka, M. Bando, et al. The role of ascorbic acid transporter in the lens of streptozotocin-induced diabetic rat, Biomed. Pharmacother. [Epub ahead of print].
    • Biomed. Pharmacother.
    • Nakazawa, Y.1    Oka, M.2    Bando, M.3
  • 25
    • 59849101790 scopus 로고    scopus 로고
    • Influx mechanism of 2',3'-dideoxyinosine and uridine at the blood-placenta barrier
    • Sato K., Sai Y., Nishimura T., et al. Influx mechanism of 2',3'-dideoxyinosine and uridine at the blood-placenta barrier. Placenta 2009, 30:263-269.
    • (2009) Placenta , vol.30 , pp. 263-269
    • Sato, K.1    Sai, Y.2    Nishimura, T.3
  • 26
    • 28444455734 scopus 로고    scopus 로고
    • Changes of MIP26K linked with cataract formation and maturation in the lenses of the Shumiya Cataract Rat
    • Matsubara Y., Oka M., Shumiya S., et al. Changes of MIP26K linked with cataract formation and maturation in the lenses of the Shumiya Cataract Rat. J. Jap. Soc. Cat. Res. 2003, 15:47-49.
    • (2003) J. Jap. Soc. Cat. Res. , vol.15 , pp. 47-49
    • Matsubara, Y.1    Oka, M.2    Shumiya, S.3
  • 27
    • 80755135884 scopus 로고    scopus 로고
    • Lentoid body formation and expression of major intrinsic polypeptide (MIP) 26 on a PTFE membrane
    • Oka M., Shimizu K., Nakamura K., et al. Lentoid body formation and expression of major intrinsic polypeptide (MIP) 26 on a PTFE membrane. J. Jap. Soc. Cat. Res. 2004, 16:63-68.
    • (2004) J. Jap. Soc. Cat. Res. , vol.16 , pp. 63-68
    • Oka, M.1    Shimizu, K.2    Nakamura, K.3
  • 28
    • 0039687656 scopus 로고
    • Vitamin methods: a simple potentiometric method for determining ascorbic acid, suitable for use with coloured extracts
    • Harris L.J., Mapson L.W., Wang Y.L. Vitamin methods: a simple potentiometric method for determining ascorbic acid, suitable for use with coloured extracts. Biochem. J. 1942, 36:183-195.
    • (1942) Biochem. J. , vol.36 , pp. 183-195
    • Harris, L.J.1    Mapson, L.W.2    Wang, Y.L.3
  • 29
    • 0025720430 scopus 로고
    • Ascorbic acid protects lipids in human plasma and low-density lipoprotein against oxidative damage
    • Frei B. Ascorbic acid protects lipids in human plasma and low-density lipoprotein against oxidative damage. Am. J. Clin. Nutr. 1991, 54:1113-1118.
    • (1991) Am. J. Clin. Nutr. , vol.54 , pp. 1113-1118
    • Frei, B.1
  • 30
    • 0032724347 scopus 로고    scopus 로고
    • On the role of vitamin C and other antioxidants in atherogenesis and vascular dysfunction
    • Frei B. On the role of vitamin C and other antioxidants in atherogenesis and vascular dysfunction. Proc. Soc. Exp. Biol. Med. 1999, 222:196-204.
    • (1999) Proc. Soc. Exp. Biol. Med. , vol.222 , pp. 196-204
    • Frei, B.1
  • 31
    • 0021916801 scopus 로고
    • Permeability and gating of lens gap junction channels incorporated into liposomes
    • Peracchia C., Girsch S.J. Permeability and gating of lens gap junction channels incorporated into liposomes. Curr. Eye Res. 1985, 4:431-439.
    • (1985) Curr. Eye Res. , vol.4 , pp. 431-439
    • Peracchia, C.1    Girsch, S.J.2
  • 32
    • 0021789405 scopus 로고
    • Major intrinsic polypeptide (MIP26K) from lens membrane: reconstitution into vesicles and inhibition of channel forming activity by peptide antiserum
    • Gooden M., Rintoul D., Takehana M., et al. Major intrinsic polypeptide (MIP26K) from lens membrane: reconstitution into vesicles and inhibition of channel forming activity by peptide antiserum. Biochem. Biophys. Res. Commun. 1985, 30:993-999.
    • (1985) Biochem. Biophys. Res. Commun. , vol.30 , pp. 993-999
    • Gooden, M.1    Rintoul, D.2    Takehana, M.3
  • 33
    • 0032854603 scopus 로고    scopus 로고
    • The role of MIP in lens fiber cell membrane transport
    • Varadaraj K., Kushmerick C., Baldo G.J., et al. The role of MIP in lens fiber cell membrane transport. J. Membr. Biol. 1999, 170:191-203.
    • (1999) J. Membr. Biol. , vol.170 , pp. 191-203
    • Varadaraj, K.1    Kushmerick, C.2    Baldo, G.J.3
  • 34
    • 73449099306 scopus 로고    scopus 로고
    • The membrane proteome of the mouse lens fiber cell
    • Bassnett S., Wilmarth P.A., David L.L. The membrane proteome of the mouse lens fiber cell. Mol. Vis. 2009, 15:2448-2463.
    • (2009) Mol. Vis. , vol.15 , pp. 2448-2463
    • Bassnett, S.1    Wilmarth, P.A.2    David, L.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.