메뉴 건너뛰기




Volumn 46, Issue 9, 2005, Pages 3247-3255

Regulation of lens cell-to-cell communication by activation of PKCγ and disassembly of Cx50 channels

Author keywords

[No Author keywords available]

Indexed keywords

4ALPHA PHORBOL DIDECANOATE; CAVEOLIN 1; CONNEXIN 50; GAP JUNCTION PROTEIN; LUCIFER YELLOW; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C GAMMA; SERINE; THREONINE; UNCLASSIFIED DRUG; CAV PROTEIN, RAT; CAVEOLIN; CX46 PROTEIN, RAT; EYE PROTEIN; ION CHANNEL; ISOQUINOLINE DERIVATIVE; PROTEIN KINASE C;

EID: 27244457253     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.04-1504     Document Type: Article
Times cited : (36)

References (32)
  • 1
    • 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. 1997;77:21-50.
    • (1997) Physiol Rev , vol.77 , pp. 21-50
    • Mathias, R.T.1    Rae, J.L.2    Baldo, G.J.3
  • 2
    • 0035985057 scopus 로고    scopus 로고
    • Structural and functional diversity of connexin genes in the mouse and human genome
    • Willecke K, Eiberger J, Degen J, et al. Structural and functional diversity of connexin genes in the mouse and human genome. Biol Chem. 2002;383:725-37.
    • (2002) Biol Chem , vol.383 , pp. 725-737
    • Willecke, K.1    Eiberger, J.2    Degen, J.3
  • 3
    • 0014097086 scopus 로고
    • Hexagonal array of subunits in intercellular junctions of the mouse heart and liver
    • Revel JP, Karnovsky MJ. Hexagonal array of subunits in intercellular junctions of the mouse heart and liver. J Cell Biol. 1967;33:C7-C12.
    • (1967) J Cell Biol , vol.33
    • Revel, J.P.1    Karnovsky, M.J.2
  • 4
    • 0019624299 scopus 로고
    • Junctional intercellular communication: The cell-to-cell membrane channel
    • Loewenstein WR. Junctional intercellular communication: the cell-to-cell membrane channel. Physiol Rev. 1981;61:829-913.
    • (1981) Physiol Rev , vol.61 , pp. 829-913
    • Loewenstein, W.R.1
  • 5
    • 0018905597 scopus 로고
    • Structure of the junction between communicating cells
    • Unwin PN, Zampighi G. Structure of the junction between communicating cells. Nature. 1980;283:545-549.
    • (1980) Nature , vol.283 , pp. 545-549
    • Unwin, P.N.1    Zampighi, G.2
  • 6
    • 0019471073 scopus 로고
    • Gap Junctional conductance is a simple and sensitive function of intracellular pH
    • Spray DC, Harris AL, Bennett MV. Gap Junctional conductance is a simple and sensitive function of intracellular pH. Science. 1981;211:712-715.
    • (1981) Science , vol.211 , pp. 712-715
    • Spray, D.C.1    Harris, A.L.2    Bennett, M.V.3
  • 7
    • 0022380837 scopus 로고
    • Diacylglycerol downregulates Junctional membrane permeability: TMB-8 blocks this effect
    • Yada T, Rose B, Loewenstein WR. Diacylglycerol downregulates Junctional membrane permeability: TMB-8 blocks this effect. J Membr Biol. 1985;88:217-232.
    • (1985) J Membr Biol , vol.88 , pp. 217-232
    • Yada, T.1    Rose, B.2    Loewenstein, W.R.3
  • 8
    • 0034013263 scopus 로고    scopus 로고
    • PKC isoenzymes in the chicken lens and TPA-induced effects on intercellular communication
    • Berthoud VM, Westphale EM, Grigoryeva A, Beyer EC. PKC isoenzymes in the chicken lens and TPA-induced effects on intercellular communication. Invest Ophthalmol Vis Sci. 2000;41:850-858.
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 850-858
    • Berthoud, V.M.1    Westphale, E.M.2    Grigoryeva, A.3    Beyer, E.C.4
  • 9
    • 0037193468 scopus 로고    scopus 로고
    • Dislocation and degradation from the ER are regulated by cytosolic stress
    • VanSlyke JK, Musil LS. Dislocation and degradation from the ER are regulated by cytosolic stress. J Cell Biol. 2002;157:381-394.
    • (2002) J Cell Biol , vol.157 , pp. 381-394
    • Vanslyke, J.K.1    Musil, L.S.2
  • 11
    • 0019302480 scopus 로고
    • Interaction of anesthetics with electrical synapses
    • Johnston MF, Simon SA, Ramon F. Interaction of anesthetics with electrical synapses. Nature. 1980;286:498-500.
    • (1980) Nature , vol.286 , pp. 498-500
    • Johnston, M.F.1    Simon, S.A.2    Ramon, F.3
  • 12
    • 0026039335 scopus 로고
    • Influence of tissue acidification and halothane anesthesia on hepatic electrical and biochemical properties during ischemia
    • Kehrer G, Aminalai A, Burger E, et al. Influence of tissue acidification and halothane anesthesia on hepatic electrical and biochemical properties during ischemia. Z Gastroenterol. 1991;29:22-30.
    • (1991) Z Gastroenterol , vol.29 , pp. 22-30
    • Kehrer, G.1    Aminalai, A.2    Burger, E.3
  • 13
    • 0344420042 scopus 로고    scopus 로고
    • Protein kinase Cγ regulation of gap junction activity through caveolin-1-containing lipid rafts
    • Lin D, Zhou J, Zelenka PS, Takemoto DJ. Protein kinase Cγ regulation of gap junction activity through caveolin-1-containing lipid rafts. Invest Ophthalmol Vis Sci. 2003;44:5259-5268.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 5259-5268
    • Lin, D.1    Zhou, J.2    Zelenka, P.S.3    Takemoto, D.J.4
  • 14
    • 0037336079 scopus 로고    scopus 로고
    • IGF-I-induced phosphorylation of connexin 43 by PKCγ: Regulation of gap junctions in rabbit lens epithelial cells
    • Lin D, Boyle DL, Takemoto DJ. IGF-I-induced phosphorylation of connexin 43 by PKCγ: regulation of gap junctions in rabbit lens epithelial cells. Invest Ophthalmol Vis Sci. 2003;44:1160-1168.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 1160-1168
    • Lin, D.1    Boyle, D.L.2    Takemoto, D.J.3
  • 15
    • 0032903938 scopus 로고    scopus 로고
    • Functional and morphological correlates of connexin50 expressed in Xenopus laevis oocytes
    • Zampighi GA, Loo DD, Kreman M, Eskandari S, Wright EM. Functional and morphological correlates of connexin50 expressed in Xenopus laevis oocytes. J Gen Physiol. 1999;113:507-524.
    • (1999) J Gen Physiol , vol.113 , pp. 507-524
    • Zampighi, G.A.1    Loo, D.D.2    Kreman, M.3    Eskandari, S.4    Wright, E.M.5
  • 16
    • 0023818426 scopus 로고
    • Homology between gap junction proteins in lens, heart and liver
    • Kistler, J, Christie D, Bullivant S. Homology between gap junction proteins in lens, heart and liver. Nature 1988;331:721-723.
    • (1988) Nature , vol.331 , pp. 721-723
    • Kistler, J.1    Christie, D.2    Bullivant, S.3
  • 17
    • 0029127695 scopus 로고
    • Purification of bovine lens cell-to-cell channels composed of connexin44 and connexinSO
    • Konig N, Zampighi GA. Purification of bovine lens cell-to-cell channels composed of connexin44 and connexinSO. J Cell Sci. 1995;108:3091-3098.
    • (1995) J Cell Sci , vol.108 , pp. 3091-3098
    • Konig, N.1    Zampighi, G.A.2
  • 19
    • 0035789150 scopus 로고    scopus 로고
    • Synthesis and evaluation of novel aldose reductase inhibitors: Effects on lens protein kinase Cγ
    • Lewis S, Karrer J, Saleh S, et al. Synthesis and evaluation of novel aldose reductase inhibitors: Effects on lens protein kinase Cγ. Mol Vis. 2001;7:164-171.
    • (2001) Mol Vis , vol.7 , pp. 164-171
    • Lewis, S.1    Karrer, J.2    Saleh, S.3
  • 20
    • 0027385138 scopus 로고
    • Effects of phorbol ester on protein kinase C activity and effects of depletion of its activity on thyrotrophin, forskolin and 8′-bromoadenosine 3′,5′-cyclic monophosphate-induced [3H]thymidine incorporation in rat FRTL-5 cells
    • Akiguchi I, Izumi M, Nagataki S. Effects of phorbol ester on protein kinase C activity and effects of depletion of its activity on thyrotrophin, forskolin and 8′-bromoadenosine 3′,5′-cyclic monophosphate-induced [3H]thymidine incorporation in rat FRTL-5 cells. J Endocrinol. 1993;138:379-389.
    • (1993) J Endocrinol , vol.138 , pp. 379-389
    • Akiguchi, I.1    Izumi, M.2    Nagataki, S.3
  • 21
    • 0037799250 scopus 로고    scopus 로고
    • Synergy of epidermal growth factor and 12(S)hydroxyeicosatetraenoate on protein kinase C activation in lens epithelial cells
    • Zhou J, Fariss RN, Zelenka PS. Synergy of epidermal growth factor and 12(S)hydroxyeicosatetraenoate on protein kinase C activation in lens epithelial cells. J Biol Chem. 2003;278:5388-5398.
    • (2003) J Biol Chem , vol.278 , pp. 5388-5398
    • Zhou, J.1    Fariss, R.N.2    Zelenka, P.S.3
  • 22
    • 10644227206 scopus 로고    scopus 로고
    • Differential phosphorylation of connexin46 and connexin50 by H2O2 activation of protein kinase Cγ
    • Lin D, Lobell S, Jewell A, Takemoto DJ. Differential phosphorylation of connexin46 and connexin50 by H2O2 activation of protein kinase Cγ. Mol Vis. 2004;10:688-695.
    • (2004) Mol Vis , vol.10 , pp. 688-695
    • Lin, D.1    Lobell, S.2    Jewell, A.3    Takemoto, D.J.4
  • 23
    • 0033776421 scopus 로고    scopus 로고
    • Epithelial organization of the mammalian lens
    • Zampighi GA, Eskandari S, Kreman M. Epithelial organization of the mammalian lens. Exp Eye Res. 2000;71:415-435.
    • (2000) Exp Eye Res , vol.71 , pp. 415-435
    • Zampighi, G.A.1    Eskandari, S.2    Kreman, M.3
  • 24
    • 0346496124 scopus 로고    scopus 로고
    • Distribution of connexin50 channels and hemichannels in lens fibers: A structural approach
    • Zampighi GA. Distribution of connexin50 channels and hemichannels in lens fibers: a structural approach. Cell Commun Adhes. 2003;10:265-270.
    • (2003) Cell Commun Adhes , vol.10 , pp. 265-270
    • Zampighi, G.A.1
  • 26
    • 0028828220 scopus 로고
    • Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins: Application to the immunogold labeling of intercellular junctional complexes
    • Fujimoto K. Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins: application to the immunogold labeling of intercellular junctional complexes. J Cell Sci. 1995;108:3443-3449.
    • (1995) J Cell Sci , vol.108 , pp. 3443-3449
    • Fujimoto, K.1
  • 27
    • 0032952188 scopus 로고    scopus 로고
    • Direct immunogold labeling of connexins and aquaporin-4 in freeze-fracture replicas of liver, brain, and spinal cord: Factors limiting quantitative analysis
    • Rash JE, Yasumura T. Direct immunogold labeling of connexins and aquaporin-4 in freeze-fracture replicas of liver, brain, and spinal cord: factors limiting quantitative analysis. Cell Tissue Res. 1999;296:307-321.
    • (1999) Cell Tissue Res , vol.296 , pp. 307-321
    • Rash, J.E.1    Yasumura, T.2
  • 28
    • 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. 1998;143:815-825.
    • (1998) J Cell Biol , vol.143 , pp. 815-825
    • White, T.W.1    Goodenough, D.A.2    Paul, D.L.3
  • 29
    • 0036023359 scopus 로고    scopus 로고
    • Disruption of Gja8 (alpha8 connexin) in mice leads to microphthalmia associated with retardation of lens growth and lens fiber maturation
    • Rong P, Wang X, Niesman I, et al. Disruption of Gja8 (alpha8 connexin) in mice leads to microphthalmia associated with retardation of lens growth and lens fiber maturation. Development. 2002;129:167-174.
    • (2002) Development , vol.129 , pp. 167-174
    • Rong, P.1    Wang, X.2    Niesman, I.3
  • 30
    • 0034717680 scopus 로고    scopus 로고
    • Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication
    • Lampe PD, TenBroek EM, Burt JM, Kurata WE, Johnson RG, Lau AF. Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication. J Cell Biol. 2000;149:1503-1512.
    • (2000) J Cell Biol , vol.149 , pp. 1503-1512
    • Lampe, P.D.1    Tenbroek, E.M.2    Burt, J.M.3    Kurata, W.E.4    Johnson, R.G.5    Lau, A.F.6
  • 31
    • 0035789829 scopus 로고    scopus 로고
    • PKC-γ phosphorylation of connexin 46 in the lens cortex
    • Saleh SM, Takemoto LJ, Zoukhri D, Takemoto DJ. PKC-γ phosphorylation of connexin 46 in the lens cortex. Mol Vis. 2001;7:240-246.
    • (2001) Mol Vis , vol.7 , pp. 240-246
    • Saleh, S.M.1    Takemoto, L.J.2    Zoukhri, D.3    Takemoto, D.J.4
  • 32
    • 0037035519 scopus 로고    scopus 로고
    • Connexin family members target to lipid raft domains and interact with caveolin-1
    • Schubert AL, Schubert W, Spray DC, Lisanti MP. Connexin family members target to lipid raft domains and interact with caveolin-1. Biochemistry. 2002;41:5754-5764.
    • (2002) Biochemistry , vol.41 , pp. 5754-5764
    • Schubert, A.L.1    Schubert, W.2    Spray, D.C.3    Lisanti, M.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.