메뉴 건너뛰기




Volumn 308, Issue 10, 2015, Pages C835-C847

Lens ion homeostasis relies on the assembly and/or stability of large connexin 46 gap junction plaques on the broad sides of differentiating fiber cells

Author keywords

Beaded intermediate filament; CP49; Impedance; Membrane skeleton; Tropomodulin 1

Indexed keywords

CONNEXIN 46; CONNEXIN 50; CP49 PROTEIN; F ACTIN; GAP JUNCTION PROTEIN; INTERMEDIATE FILAMENT PROTEIN; PHAKININ; SODIUM; SPECTRIN; TROPOMODULIN; TROPOMODULIN 1; UNCLASSIFIED DRUG; EYE PROTEIN; ION CHANNEL;

EID: 84930893448     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00372.2014     Document Type: Article
Times cited : (22)

References (92)
  • 3
    • 0026768033 scopus 로고
    • Spatial variations in membrane properties in the intact rat lens
    • Baldo GJ, Mathias RT. Spatial variations in membrane properties in the intact rat lens. Biophys J 63: 518-529, 1992.
    • (1992) Biophys J , vol.63 , pp. 518-529
    • Baldo, G.J.1    Mathias, R.T.2
  • 4
    • 0036343618 scopus 로고    scopus 로고
    • Lens organelle degradation
    • Bassnett S. Lens organelle degradation. Exp Eye Res 74: 1-6, 2002.
    • (2002) Exp Eye Res , vol.74 , pp. 1-6
    • Bassnett, S.1
  • 5
    • 0037374457 scopus 로고    scopus 로고
    • Morphometric analysis of fibre cell growth in the developing chicken lens
    • Bassnett S, Winzenburger PA. Morphometric analysis of fibre cell growth in the developing chicken lens. Exp Eye Res 76: 291-302, 2003.
    • (2003) Exp Eye Res , vol.76 , pp. 291-302
    • Bassnett, S.1    Winzenburger, P.A.2
  • 6
    • 0023551497 scopus 로고
    • Connexin43: A protein from rat heart homologous to a gap junction protein from liver
    • Beyer EC, Paul DL, Goodenough DA. Connexin43: a protein from rat heart homologous to a gap junction protein from liver. J Cell Biol 105: 2621-2629, 1987.
    • (1987) J Cell Biol , vol.105 , pp. 2621-2629
    • Beyer, E.C.1    Paul, D.L.2    Goodenough, D.A.3
  • 7
    • 84901989777 scopus 로고    scopus 로고
    • Massive formation of square array junctions dramatically alters cell shape but does not cause lens opacity in the cav1-KO mice
    • Biswas SK, Brako L, Lo WK. Massive formation of square array junctions dramatically alters cell shape but does not cause lens opacity in the cav1-KO mice. Exp Eye Res 125: 9-19, 2014.
    • (2014) Exp Eye Res , vol.125 , pp. 9-19
    • Biswas, S.K.1    Brako, L.2    Lo, W.K.3
  • 8
    • 68749086087 scopus 로고    scopus 로고
    • Gap junction remodeling associated with cholesterol redistribution during fiber cell maturation in the adult chicken lens
    • Biswas SK, Jiang JX, Lo WK. Gap junction remodeling associated with cholesterol redistribution during fiber cell maturation in the adult chicken lens. Mol Vis 15: 1492-1508, 2009.
    • (2009) Mol Vis , vol.15 , pp. 1492-1508
    • Biswas, S.K.1    Jiang, J.X.2    Lo, W.K.3
  • 9
    • 0021230251 scopus 로고
    • How a gap junction maintains its structure
    • Braun J, Abney JR, Owicki JC. How a gap junction maintains its structure. Nature 310: 316-318, 1984.
    • (1984) Nature , vol.310 , pp. 316-318
    • Braun, J.1    Abney, J.R.2    Owicki, J.C.3
  • 10
    • 1942445036 scopus 로고    scopus 로고
    • Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton
    • Butkevich E, Hulsmann S, Wenzel D, Shirao T, Duden R, Majoul I. Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton. Curr Biol 14: 650-658, 2004.
    • (2004) Curr Biol , vol.14 , pp. 650-658
    • Butkevich, E.1    Hulsmann, S.2    Wenzel, D.3    Shirao, T.4    Duden, R.5    Majoul, I.6
  • 13
    • 0347382298 scopus 로고    scopus 로고
    • Probing microscopic diffusion by 2-photon flash photolysis: Measurement of isotropic and anisotropic diffusion in lens fiber cells
    • Cannell MB, Jacobs MD, Donaldson PJ, Soeller C. Probing microscopic diffusion by 2-photon flash photolysis: measurement of isotropic and anisotropic diffusion in lens fiber cells. Microsc Res Tech 63: 50-57, 2004.
    • (2004) Microsc Res Tech , vol.63 , pp. 50-57
    • Cannell, M.B.1    Jacobs, M.D.2    Donaldson, P.J.3    Soeller, C.4
  • 14
    • 0036501610 scopus 로고    scopus 로고
    • A Gja8 (Cx50) point mutation causes an alteration of α3-connexin (Cx46) in semi-dominant cataracts of Lop10 mice
    • Chang B, Wang X, Hawes NL, Ojakian R, Davisson MT, Lo WK, Gong X. A Gja8 (Cx50) point mutation causes an alteration of α3-connexin (Cx46) in semi-dominant cataracts of Lop10 mice. Hum Mol Genet 11: 507-513, 2002.
    • (2002) Hum Mol Genet , vol.11 , pp. 507-513
    • Chang, B.1    Wang, X.2    Hawes, N.L.3    Ojakian, R.4    Davisson, M.T.5    Lo, W.K.6    Gong, X.7
  • 16
    • 35548990168 scopus 로고    scopus 로고
    • The E233del mutation in BFSP2 causes a progressive autosomal dominant congenital cataract in a Chinese family
    • Cui X, Gao L, Jin Y, Zhang Y, Bai J, Feng G, Gao W, Liu P, He L, Fu S. The E233del mutation in BFSP2 causes a progressive autosomal dominant congenital cataract in a Chinese family. Mol Vis 13: 2023-2029, 2007.
    • (2007) Mol Vis , vol.13 , pp. 2023-2029
    • Cui, X.1    Gao, L.2    Jin, Y.3    Zhang, Y.4    Bai, J.5    Feng, G.6    Gao, W.7    Liu, P.8    He, L.9    Fu, S.10
  • 18
    • 67649409220 scopus 로고    scopus 로고
    • Calpain expression and activity during lens fiber cell differentiation
    • De Maria A, Shi Y, Kumar NM, Bassnett S. Calpain expression and activity during lens fiber cell differentiation. J Biol Chem 284: 13542- 13550, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 13542-13550
    • De Maria, A.1    Shi, Y.2    Kumar, N.M.3    Bassnett, S.4
  • 19
    • 33750589568 scopus 로고    scopus 로고
    • Functional characterization of a naturally occurring Cx50 truncation
    • DeRosa AM, Mui R, Srinivas M, White TW. Functional characterization of a naturally occurring Cx50 truncation. Invest Ophthalmol Vis Sci 47: 4474-4481, 2006.
    • (2006) Invest Ophthalmol Vis Sci , vol.47 , pp. 4474-4481
    • DeRosa, A.M.1    Mui, R.2    Srinivas, M.3    White, T.W.4
  • 21
    • 0036126655 scopus 로고    scopus 로고
    • pH gating of lens fibre connexins
    • Eckert R. pH gating of lens fibre connexins. Pflügers Arch 443: 843-851, 2002.
    • (2002) Pflügers Arch , vol.443 , pp. 843-851
    • Eckert, R.1
  • 22
    • 0036709318 scopus 로고    scopus 로고
    • Genetic tags for labelling live cells: Gap junctions and beyond
    • Falk M. Genetic tags for labelling live cells: gap junctions and beyond. Trends Cell Biol 12: 399-404, 2002.
    • (2002) Trends Cell Biol , vol.12 , pp. 399-404
    • Falk, M.1
  • 23
    • 0033985955 scopus 로고    scopus 로고
    • Tropomodulin and tropomyosin mediate lens cell actin cytoskeleton reorganization in vitro
    • Fischer RS, Lee A, Fowler VM. Tropomodulin and tropomyosin mediate lens cell actin cytoskeleton reorganization in vitro. Invest Ophthalmol Vis Sci 41: 166-174, 2000.
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 166-174
    • Fischer, R.S.1    Lee, A.2    Fowler, V.M.3
  • 24
    • 61849139080 scopus 로고    scopus 로고
    • Lens intermediate filaments
    • FitzGerald PG. Lens intermediate filaments. Exp Eye Res 88: 165-172, 2009.
    • (2009) Exp Eye Res , vol.88 , pp. 165-172
    • FitzGerald, P.G.1
  • 25
    • 0025314680 scopus 로고
    • Tropomodulin: A cytoskeletal protein that binds to the end of erythrocyte tropomyosin and inhibits tropomyosin binding to actin
    • Fowler VM. Tropomodulin: a cytoskeletal protein that binds to the end of erythrocyte tropomyosin and inhibits tropomyosin binding to actin. J Cell Biol 111: 471-481, 1990.
    • (1990) J Cell Biol , vol.111 , pp. 471-481
    • Fowler, V.M.1
  • 26
    • 0347480271 scopus 로고    scopus 로고
    • Aberrant myofibril assembly in tropomodulin1 null mice leads to aborted heart development and embryonic lethality
    • Fritz-Six KL, Cox PR, Fischer RS, Xu B, Gregorio CC, Zoghbi HY, Fowler VM. Aberrant myofibril assembly in tropomodulin1 null mice leads to aborted heart development and embryonic lethality. J Cell Biol 163: 1033-1044, 2003.
    • (2003) J Cell Biol , vol.163 , pp. 1033-1044
    • Fritz-Six, K.L.1    Cox, P.R.2    Fischer, R.S.3    Xu, B.4    Gregorio, C.C.5    Zoghbi, H.Y.6    Fowler, V.M.7
  • 29
    • 79958056033 scopus 로고    scopus 로고
    • Lens intracellular hydrostatic pressure is generated by the circulation of sodium and modulated by gap junction coupling
    • Gao J, Sun X, Moore LC, White TW, Brink PR, Mathias RT. Lens intracellular hydrostatic pressure is generated by the circulation of sodium and modulated by gap junction coupling. J Gen Physiol 137: 507-520, 2011.
    • (2011) J Gen Physiol , vol.137 , pp. 507-520
    • Gao, J.1    Sun, X.2    Moore, L.C.3    White, T.W.4    Brink, P.R.5    Mathias, R.T.6
  • 30
    • 0034669683 scopus 로고    scopus 로고
    • Isoform-specific function and distribution of Na/K pumps in the frog lens epithelium
    • Gao J, Sun X, Yatsula V, Wymore RS, Mathias RT. Isoform-specific function and distribution of Na/K pumps in the frog lens epithelium. J Membr Biol 178: 89-101, 2000.
    • (2000) J Membr Biol , vol.178 , pp. 89-101
    • Gao, J.1    Sun, X.2    Yatsula, V.3    Wymore, R.S.4    Mathias, R.T.5
  • 32
    • 85012338162 scopus 로고
    • The binding of vimentin to human erythrocyte membranes: A model system for the study of intermediate filamentmembrane interactions
    • Georgatos SD, Marchesi VT. The binding of vimentin to human erythrocyte membranes: a model system for the study of intermediate filamentmembrane interactions. J Cell Biol 100: 1955-1961, 1985.
    • (1985) J Cell Biol , vol.100 , pp. 1955-1961
    • Georgatos, S.D.1    Marchesi, V.T.2
  • 33
    • 33748282756 scopus 로고    scopus 로고
    • A potential novel mechanism involving connexin 43 gap junction for control of Sertoli cell proliferation by thyroid hormones
    • Gilleron J, Nebout M, Scarabelli L, Senegas-Balas F, Palmero S, Segretain D, Pointis G. A potential novel mechanism involving connexin 43 gap junction for control of Sertoli cell proliferation by thyroid hormones. J Cell Physiol 209: 153-161, 2006.
    • (2006) J Cell Physiol , vol.209 , pp. 153-161
    • Gilleron, J.1    Nebout, M.2    Scarabelli, L.3    Senegas-Balas, F.4    Palmero, S.5    Segretain, D.6    Pointis, G.7
  • 34
    • 79960260136 scopus 로고    scopus 로고
    • Cytoplasmic γ-actin and tropomodulin isoforms link to the sarcoplasmic reticulum in skeletal muscle fibers
    • Gokhin DS, Fowler VM. Cytoplasmic γ-actin and tropomodulin isoforms link to the sarcoplasmic reticulum in skeletal muscle fibers. J Cell Biol 194: 105-120, 2011.
    • (2011) J Cell Biol , vol.194 , pp. 105-120
    • Gokhin, D.S.1    Fowler, V.M.2
  • 36
    • 84868697480 scopus 로고    scopus 로고
    • Tmod1 and CP49 synergize to control the fiber cell geometry, transparency, and mechanical stiffness of the mouse lens
    • Gokhin DS, Nowak RB, Kim NE, Arnett EE, Chen AC, Sah RL, Clark JI, Fowler VM. Tmod1 and CP49 synergize to control the fiber cell geometry, transparency, and mechanical stiffness of the mouse lens. PLos One 7: e48734, 2012.
    • (2012) PLos One , vol.7
    • Gokhin, D.S.1    Nowak, R.B.2    Kim, N.E.3    Arnett, E.E.4    Chen, A.C.5    Sah, R.L.6    Clark, J.I.7    Fowler, V.M.8
  • 39
    • 0023427175 scopus 로고
    • Formation, distribution and dissociation of intercellular junctions in the lens
    • Gruijters WT, Kistler J, Bullivant S. Formation, distribution and dissociation of intercellular junctions in the lens. J Cell Sci 88: 351-359, 1987.
    • (1987) J Cell Sci , vol.88 , pp. 351-359
    • Gruijters, W.T.1    Kistler, J.2    Bullivant, S.3
  • 40
    • 34249082403 scopus 로고    scopus 로고
    • Connexin channel permeability to cytoplasmic molecules
    • Harris AL. Connexin channel permeability to cytoplasmic molecules. Prog Biophys Mol Biol 94: 120-143, 2007.
    • (2007) Prog Biophys Mol Biol , vol.94 , pp. 120-143
    • Harris, A.L.1
  • 41
    • 0025239385 scopus 로고
    • Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin
    • Harris AS, Morrow JS. Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin. Proc Natl Acad Sci USA 87: 3009-3013, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3009-3013
    • Harris, A.S.1    Morrow, J.S.2
  • 42
    • 28644434657 scopus 로고    scopus 로고
    • Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion
    • Hunter AW, Barker RJ, Zhu C, Gourdie RG. Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion. Mol Biol Cell 16: 5686-5698, 2005.
    • (2005) Mol Biol Cell , vol.16 , pp. 5686-5698
    • Hunter, A.W.1    Barker, R.J.2    Zhu, C.3    Gourdie, R.G.4
  • 43
    • 0346096980 scopus 로고    scopus 로고
    • Gap junction processing and redistribution revealed by quantitative optical measurements of connexin46 epitopes in the lens
    • Jacobs MD, Soeller C, Sisley AM, Cannell MB, Donaldson PJ. Gap junction processing and redistribution revealed by quantitative optical measurements of connexin46 epitopes in the lens. Invest Ophthalmol Vis Sci 45: 191-199, 2004.
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 191-199
    • Jacobs, M.D.1    Soeller, C.2    Sisley, A.M.3    Cannell, M.B.4    Donaldson, P.J.5
  • 44
    • 0033942142 scopus 로고    scopus 로고
    • Autosomal-dominant congenital cataract associated with a deletion mutation in the human beaded filament protein gene BFSP2
    • Jakobs PM, Hess JF, FitzGerald PG, Kramer P, Weleber RG, Litt M. Autosomal-dominant congenital cataract associated with a deletion mutation in the human beaded filament protein gene BFSP2. Am J Hum Genet 66: 1432-1436, 2000.
    • (2000) Am J Hum Genet , vol.66 , pp. 1432-1436
    • Jakobs, P.M.1    Hess, J.F.2    FitzGerald, P.G.3    Kramer, P.4    Weleber, R.G.5    Litt, M.6
  • 45
    • 0033012698 scopus 로고    scopus 로고
    • Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells
    • Jordan K, Solan JL, Dominguez M, Sia M, Hand A, Lampe PD, Laird DW. Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells. Mol Biol Cell 10: 2033- 2050, 1999.
    • (1999) Mol Biol Cell , vol.10 , pp. 2033-2050
    • Jordan, K.1    Solan, J.L.2    Dominguez, M.3    Sia, M.4    Hand, A.5    Lampe, P.D.6    Laird, D.W.7
  • 46
    • 84862166302 scopus 로고    scopus 로고
    • Biological role of connexin intercellular channels and hemichannels
    • Kar R, Batra N, Riquelme MA, Jiang JX. Biological role of connexin intercellular channels and hemichannels. Arch Biochem Biophys 524: 2-15, 2012.
    • (2012) Arch Biochem Biophys , vol.524 , pp. 2-15
    • Kar, R.1    Batra, N.2    Riquelme, M.A.3    Jiang, J.X.4
  • 47
    • 0023232998 scopus 로고
    • Protein processing in lens intercellular junctions: Cleavage of MP70 to MP38
    • Kistler J, Bullivant S. Protein processing in lens intercellular junctions: cleavage of MP70 to MP38. Invest Ophthalmol Vis Sci 28: 1687-1692, 1987.
    • (1987) Invest Ophthalmol Vis Sci , vol.28 , pp. 1687-1692
    • Kistler, J.1    Bullivant, S.2
  • 48
    • 0030028301 scopus 로고    scopus 로고
    • The gap junction communication channel
    • Kumar NM, Gilula NB. The gap junction communication channel. Cell 84: 381-388, 1996.
    • (1996) Cell , vol.84 , pp. 381-388
    • Kumar, N.M.1    Gilula, N.B.2
  • 49
    • 0029558579 scopus 로고
    • The ultrastructure of epithelial and fiber cells in the crystalline lens
    • Kuszak JR. The ultrastructure of epithelial and fiber cells in the crystalline lens. Int Rev Cytol 163: 305-350, 1995.
    • (1995) Int Rev Cytol , vol.163 , pp. 305-350
    • Kuszak, J.R.1
  • 50
    • 0842331131 scopus 로고    scopus 로고
    • Fibre cell organization in crystalline lenses
    • Kuszak JR, Zoltoski RK, Sivertson C. Fibre cell organization in crystalline lenses. Exp Eye Res 78: 673-687, 2004.
    • (2004) Exp Eye Res , vol.78 , pp. 673-687
    • Kuszak, J.R.1    Zoltoski, R.K.2    Sivertson, C.3
  • 52
    • 0034007480 scopus 로고    scopus 로고
    • Stabilization and remodeling of the membrane skeleton during lens fiber cell differentiation and maturation
    • Lee A, Fischer RS, Fowler VM. Stabilization and remodeling of the membrane skeleton during lens fiber cell differentiation and maturation. Dev Dyn 217: 257-270, 2000.
    • (2000) Dev Dyn , vol.217 , pp. 257-270
    • Lee, A.1    Fischer, R.S.2    Fowler, V.M.3
  • 53
    • 0035827604 scopus 로고    scopus 로고
    • Caspase remodeling of the spectrin membrane skeleton during lens development and aging
    • Lee A, Morrow JS, Fowler VM. Caspase remodeling of the spectrin membrane skeleton during lens development and aging. J Biol Chem 276: 20735-20742, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 20735-20742
    • Lee, A.1    Morrow, J.S.2    Fowler, V.M.3
  • 54
    • 34047265311 scopus 로고    scopus 로고
    • Regional differences in cystine accumulation point to a sutural delivery pathway to the lens core
    • Li L, Lim J, Jacobs MD, Kistler J, Donaldson PJ. Regional differences in cystine accumulation point to a sutural delivery pathway to the lens core. Invest Ophthalmol Vis Sci 48: 1253-1260, 2007.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 1253-1260
    • Li, L.1    Lim, J.2    Jacobs, M.D.3    Kistler, J.4    Donaldson, P.J.5
  • 55
    • 24644461194 scopus 로고    scopus 로고
    • Molecular characterization of the cystine/glutamate exchanger and the excitatory amino acid transporters in the rat lens
    • Lim J, Lam YC, Kistler J, Donaldson PJ. Molecular characterization of the cystine/glutamate exchanger and the excitatory amino acid transporters in the rat lens. Invest Ophthalmol Vis Sci 46: 2869-2877, 2005.
    • (2005) Invest Ophthalmol Vis Sci , vol.46 , pp. 2869-2877
    • Lim, J.1    Lam, Y.C.2    Kistler, J.3    Donaldson, P.J.4
  • 56
    • 33744914329 scopus 로고    scopus 로고
    • Molecular identification and characterisation of the glycine transporter (GLYT1) and the glutamine/ glutamate transporter (ASCT2) in the rat lens
    • Lim J, Lorentzen KA, Kistler J, Donaldson PJ. Molecular identification and characterisation of the glycine transporter (GLYT1) and the glutamine/ glutamate transporter (ASCT2) in the rat lens. Exp Eye Res 83: 447-455, 2006.
    • (2006) Exp Eye Res , vol.83 , pp. 447-455
    • Lim, J.1    Lorentzen, K.A.2    Kistler, J.3    Donaldson, P.J.4
  • 57
    • 0028204934 scopus 로고
    • Actin filament bundles are associated with fiber gap junctions in the primate lens
    • Lo WK, Mills A, Kuck JF. Actin filament bundles are associated with fiber gap junctions in the primate lens. Exp Eye Res 58: 189-196, 1994.
    • (1994) Exp Eye Res , vol.58 , pp. 189-196
    • Lo, W.K.1    Mills, A.2    Kuck, J.F.3
  • 58
    • 0029969576 scopus 로고    scopus 로고
    • Gap junction structures and distribution patterns of immunoreactive connexins 46 and 50 in lens regrowths of rhesus monkeys
    • Lo WK, Shaw AP, Takemoto LJ, Grossniklaus HE, Tigges M. Gap junction structures and distribution patterns of immunoreactive connexins 46 and 50 in lens regrowths of rhesus monkeys. Exp Eye Res 62: 171-180, 1996.
    • (1996) Exp Eye Res , vol.62 , pp. 171-180
    • Lo, W.K.1    Shaw, A.P.2    Takemoto, L.J.3    Grossniklaus, H.E.4    Tigges, M.5
  • 59
    • 25844484633 scopus 로고    scopus 로고
    • Distribution and dynamics of gap junction channels revealed in living cells
    • Lopez P, Balicki D, Buehler LK, Falk MM, Chen SC. Distribution and dynamics of gap junction channels revealed in living cells. Cell Commun Adhes 8: 237-242, 2001.
    • (2001) Cell Commun Adhes , vol.8 , pp. 237-242
    • Lopez, P.1    Balicki, D.2    Buehler, L.K.3    Falk, M.M.4    Chen, S.C.5
  • 61
    • 33847696641 scopus 로고    scopus 로고
    • Many faces of drebrin: From building dendritic spines and stabilizing gap junctions to shaping neuritelike cell processes
    • Majoul I, Shirao T, Sekino Y, Duden R. Many faces of drebrin: from building dendritic spines and stabilizing gap junctions to shaping neuritelike cell processes. Histochem Cell Biol 127: 355-361, 2007.
    • (2007) Histochem Cell Biol , vol.127 , pp. 355-361
    • Majoul, I.1    Shirao, T.2    Sekino, Y.3    Duden, R.4
  • 63
    • 0031014473 scopus 로고    scopus 로고
    • Physiological properties of the normal lens
    • Mathias RT, Rae JL, Baldo GJ. Physiological properties of the normal lens. Physiol Rev 77: 21-50, 1997.
    • (1997) Physiol Rev , vol.77 , pp. 21-50
    • Mathias, R.T.1    Rae, J.L.2    Baldo, G.J.3
  • 64
    • 0019433301 scopus 로고
    • The lens as a nonuniform spherical syncytium
    • Mathias RT, Rae JL, Eisenberg RS. The lens as a nonuniform spherical syncytium. Biophys J 34: 61-83, 1981.
    • (1981) Biophys J , vol.34 , pp. 61-83
    • Mathias, R.T.1    Rae, J.L.2    Eisenberg, R.S.3
  • 65
    • 74949108062 scopus 로고    scopus 로고
    • Lens gap junctions in growth, differentiation, and homeostasis
    • Mathias RT, White TW, Gong X. Lens gap junctions in growth, differentiation, and homeostasis. Physiol Rev 90: 179-206, 2010.
    • (2010) Physiol Rev , vol.90 , pp. 179-206
    • Mathias, R.T.1    White, T.W.2    Gong, X.3
  • 66
    • 58149326918 scopus 로고    scopus 로고
    • Tropomodulin1 is required in the heart but not the yolk sac for mouse embryonic development
    • McKeown CR, Nowak RB, Moyer J, Sussman MA, Fowler VM. Tropomodulin1 is required in the heart but not the yolk sac for mouse embryonic development. Circ Res 103: 1241-1248, 2008.
    • (2008) Circ Res , vol.103 , pp. 1241-1248
    • McKeown, C.R.1    Nowak, R.B.2    Moyer, J.3    Sussman, M.A.4    Fowler, V.M.5
  • 67
    • 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 BR, Krushinsky A, Kistler J, Donaldson PJ. Expression patterns for glucose transporters GLUT1 and GLUT3 in the normal rat lens and in models of diabetic cataract. Invest Ophthalmol Vis Sci 44: 3458-3466, 2003.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 3458-3466
    • Merriman-Smith, B.R.1    Krushinsky, A.2    Kistler, J.3    Donaldson, P.J.4
  • 68
    • 77957735364 scopus 로고    scopus 로고
    • Tropomodulin 1-null mice have a mild spherocytic elliptocytosis with appearance of tropomodulin 3 in red blood cells and disruption of the membrane skeleton
    • Moyer JD, Nowak RB, Kim NE, Larkin SK, Peters LL, Hartwig J, Kuypers FA, Fowler VM. Tropomodulin 1-null mice have a mild spherocytic elliptocytosis with appearance of tropomodulin 3 in red blood cells and disruption of the membrane skeleton. Blood 116: 2590-2599, 2010.
    • (2010) Blood , vol.116 , pp. 2590-2599
    • Moyer, J.D.1    Nowak, R.B.2    Kim, N.E.3    Larkin, S.K.4    Peters, L.L.5    Hartwig, J.6    Kuypers, F.A.7    Fowler, V.M.8
  • 69
    • 0035750745 scopus 로고    scopus 로고
    • Characterization of the association of connexins and ZO-1 in the lens
    • Nielsen PA, Baruch A, Giepmans BN, Kumar NM. Characterization of the association of connexins and ZO-1 in the lens. Cell Commun Adhes 8: 213-217, 2001.
    • (2001) Cell Commun Adhes , vol.8 , pp. 213-217
    • Nielsen, P.A.1    Baruch, A.2    Giepmans, B.N.3    Kumar, N.M.4
  • 71
    • 70349926142 scopus 로고    scopus 로고
    • Tropomodulin1 is required for membrane skeleton organization and hexagonal geometry of fiber cells in the mouse lens
    • Nowak RB, Fischer RS, Zoltoski RK, Kuszak JR, Fowler VM. Tropomodulin1 is required for membrane skeleton organization and hexagonal geometry of fiber cells in the mouse lens. J Cell Biol 186: 915-928, 2009.
    • (2009) J Cell Biol , vol.186 , pp. 915-928
    • Nowak, R.B.1    Fischer, R.S.2    Zoltoski, R.K.3    Kuszak, J.R.4    Fowler, V.M.5
  • 72
    • 84864102947 scopus 로고    scopus 로고
    • Tropomodulin 1 constrains fiber cell geometry during elongation and maturation in the lens cortex
    • Nowak RB, Fowler VM. Tropomodulin 1 constrains fiber cell geometry during elongation and maturation in the lens cortex. J Histochem Cytochem 60: 414-427, 2012.
    • (2012) J Histochem Cytochem , vol.60 , pp. 414-427
    • Nowak, R.B.1    Fowler, V.M.2
  • 73
    • 43149087359 scopus 로고    scopus 로고
    • The function of filensin and phakinin in lens transparency
    • Oka M, Kudo H, Sugama N, Asami Y, Takehana M. The function of filensin and phakinin in lens transparency. Mol Vis 14: 815-822, 2008.
    • (2008) Mol Vis , vol.14 , pp. 815-822
    • Oka, M.1    Kudo, H.2    Sugama, N.3    Asami, Y.4    Takehana, M.5
  • 74
    • 0019786296 scopus 로고
    • Lens differentiation in vertebrates. A review of cellular and molecular features
    • Piatigorsky J. Lens differentiation in vertebrates. A review of cellular and molecular features. Differentiation 19: 134-153, 1981.
    • (1981) Differentiation , vol.19 , pp. 134-153
    • Piatigorsky, J.1
  • 76
    • 0036023359 scopus 로고    scopus 로고
    • Disruption of Gja8 (α8-connexin) in mice leads to microphthalmia associated with retardation of lens growth and lens fiber maturation
    • Rong P, Wang X, Niesman I, Wu Y, Benedetti LE, Dunia I, Levy E, Gong X. Disruption of Gja8 (α8-connexin) in mice leads to microphthalmia associated with retardation of lens growth and lens fiber maturation. Development 129: 167-174, 2002.
    • (2002) Development , vol.129 , pp. 167-174
    • Rong, P.1    Wang, X.2    Niesman, I.3    Wu, Y.4    Benedetti, L.E.5    Dunia, I.6    Levy, E.7    Gong, X.8
  • 77
    • 1642407845 scopus 로고    scopus 로고
    • Regulation of connexin biosynthesis, assembly, gap junction formation, and removal
    • Segretain D, Falk MM. Regulation of connexin biosynthesis, assembly, gap junction formation, and removal. Biochim Biophys Acta 1662: 3-21, 2004.
    • (2004) Biochim Biophys Acta , vol.1662 , pp. 3-21
    • Segretain, D.1    Falk, M.M.2
  • 79
    • 34247127422 scopus 로고    scopus 로고
    • Inbred FVB/N mice are mutant at the cp49/Bfsp2 locus and lack beaded filament proteins in the lens
    • Simirskii VN, Lee RS, Wawrousek EF, Duncan MK. Inbred FVB/N mice are mutant at the cp49/Bfsp2 locus and lack beaded filament proteins in the lens. Invest Ophthalmol Vis Sci 47: 4931-4934, 2006.
    • (2006) Invest Ophthalmol Vis Sci , vol.47 , pp. 4931-4934
    • Simirskii, V.N.1    Lee, R.S.2    Wawrousek, E.F.3    Duncan, M.K.4
  • 83
    • 0035754245 scopus 로고    scopus 로고
    • Role of cytoskeletal elements in the recruitment of Cx43-GFP and Cx26-YFP into gap junctions
    • Thomas T, Jordan K, Laird DW. Role of cytoskeletal elements in the recruitment of Cx43-GFP and Cx26-YFP into gap junctions. Cell Commun Adhes 8: 231-236, 2001.
    • (2001) Cell Commun Adhes , vol.8 , pp. 231-236
    • Thomas, T.1    Jordan, K.2    Laird, D.W.3
  • 84
    • 0032557460 scopus 로고    scopus 로고
    • Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes
    • Toyofuku T, Yabuki M, Otsu K, Kuzuya T, Hori M, Tada M. Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes. J Biol Chem 273: 12725-12731, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 12725-12731
    • Toyofuku, T.1    Yabuki, M.2    Otsu, K.3    Kuzuya, T.4    Hori, M.5    Tada, M.6
  • 85
    • 84861871637 scopus 로고    scopus 로고
    • Magnetic resonance and confocal imaging of solute penetration into the lens reveals a zone of restricted extracellular space diffusion
    • Vaghefi E, Walker K, Pontre BP, Jacobs MD, Donaldson PJ. Magnetic resonance and confocal imaging of solute penetration into the lens reveals a zone of restricted extracellular space diffusion. Am J Physiol Regul Integr Comp Physiol 302: R1250-R1259, 2012.
    • (2012) Am J Physiol Regul Integr Comp Physiol , vol.302 , pp. R1250-R1259
    • Vaghefi, E.1    Walker, K.2    Pontre, B.P.3    Jacobs, M.D.4    Donaldson, P.J.5
  • 88
    • 0032476578 scopus 로고    scopus 로고
    • Targeted ablation of connexin50 in mice results in microphthalmia and zonular pulverulent cataracts
    • White TW, Goodenough DA, Paul DL. Targeted ablation of connexin50 in mice results in microphthalmia and zonular pulverulent cataracts. J Cell Biol 143: 815-825, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 815-825
    • White, T.W.1    Goodenough, D.A.2    Paul, D.L.3
  • 89
    • 0028233519 scopus 로고
    • Identification and characterization of tropomodulin and tropomyosin in the adult rat lens
    • Woo MK, Fowler VM. Identification and characterization of tropomodulin and tropomyosin in the adult rat lens. J Cell Sci 107: 1359-1367, 1994.
    • (1994) J Cell Sci , vol.107 , pp. 1359-1367
    • Woo, M.K.1    Fowler, V.M.2
  • 90
    • 85027946629 scopus 로고    scopus 로고
    • Tropomodulins: Pointed-end capping proteins that regulate actin filament architecture in diverse cell types
    • Yamashiro S, Gokhin DS, Kimura S, Nowak RB, Fowler VM. Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types. Cytoskeleton 69: 337-370, 2012.
    • (2012) Cytoskeleton , vol.69 , pp. 337-370
    • Yamashiro, S.1    Gokhin, D.S.2    Kimura, S.3    Nowak, R.B.4    Fowler, V.M.5
  • 92
    • 33846012542 scopus 로고    scopus 로고
    • Progressive sutural cataract associated with a BFSP2 mutation in a Chinese family
    • Zhang L, Gao L, Li Z, Qin W, Gao W, Cui X, Feng G, Fu S, He L, Liu P. Progressive sutural cataract associated with a BFSP2 mutation in a Chinese family. Mol Vis 12: 1626-1631, 2006.
    • (2006) Mol Vis , vol.12 , pp. 1626-1631
    • Zhang, L.1    Gao, L.2    Li, Z.3    Qin, W.4    Gao, W.5    Cui, X.6    Feng, G.7    Fu, S.8    He, L.9    Liu, P.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.