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Volumn 10, Issue 4, 2004, Pages 150-157

Constitutive opsin signaling: Night blindness or retinal degeneration?

Author keywords

[No Author keywords available]

Indexed keywords

11 CIS RETINAL; CALCIUM; CALCIUM CHANNEL; CYCLIC GMP; OPSIN; RETINA S ANTIGEN; RETINOL; RETINOL DEHYDROGENASE; RHODOPSIN KINASE; SCHIFF BASE; TRANSDUCIN;

EID: 1642603437     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molmed.2004.02.009     Document Type: Article
Times cited : (41)

References (56)
  • 1
    • 0141707934 scopus 로고    scopus 로고
    • Spontaneous activity of opsin apoprotein is a cause of Leber congenital amaurosis
    • Woodruff M.L., et al. Spontaneous activity of opsin apoprotein is a cause of Leber congenital amaurosis. Nat. Genet. 35:2003;158-164.
    • (2003) Nat. Genet. , vol.35 , pp. 158-164
    • Woodruff, M.L.1
  • 2
    • 0027444823 scopus 로고
    • Photoreceptor degeneration in vitamin a deprivation and retinitis pigmentosa: The equivalent light hypothesis
    • Fain G.L., Lisman J.E. Photoreceptor degeneration in vitamin A deprivation and retinitis pigmentosa: the equivalent light hypothesis. Exp. Eye Res. 57:1993;335-340.
    • (1993) Exp. Eye Res. , vol.57 , pp. 335-340
    • Fain, G.L.1    Lisman, J.E.2
  • 3
    • 0032590225 scopus 로고    scopus 로고
    • 2+, and photoreceptor death: New evidence for the equivalent-light hypothesis from arrestin knockout mice
    • 2+, and photoreceptor death: new evidence for the equivalent-light hypothesis from arrestin knockout mice. Invest. Ophthalmol. Vis. Sci. 40:1999;2770-2772.
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 2770-2772
    • Fain, G.L.1    Lisman, J.E.2
  • 4
    • 0033744611 scopus 로고    scopus 로고
    • Molecular genetics of Oguchi disease, fundus albipunctatus, and other forms of stationary night blindness: LVII Edward Jackson memorial lecture
    • Dryja T.P. Molecular genetics of Oguchi disease, fundus albipunctatus, and other forms of stationary night blindness: LVII Edward Jackson memorial lecture. Am. J. Ophthalmol. 130:2000;547-563.
    • (2000) Am. J. Ophthalmol. , vol.130 , pp. 547-563
    • Dryja, T.P.1
  • 6
    • 0030842611 scopus 로고    scopus 로고
    • Prolonged photoresponses in transgenic mouse rods lacking arrestin
    • Xu J., et al. Prolonged photoresponses in transgenic mouse rods lacking arrestin. Nature. 389:1997;505-509.
    • (1997) Nature , vol.389 , pp. 505-509
    • Xu, J.1
  • 7
    • 0033616582 scopus 로고    scopus 로고
    • Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase
    • Chen C.-K., et al. Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase. Proc. Natl. Acad. Sci. U. S. A. 96:1999;3718-3722.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 3718-3722
    • Chen, C.-K.1
  • 8
    • 17344366357 scopus 로고    scopus 로고
    • Rpe65 is necessary for production of 11-cis-vitamin a in the retinal visual cycle
    • Redmond T.M., et al. Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle. Nat. Genet. 20:1998;344-351.
    • (1998) Nat. Genet. , vol.20 , pp. 344-351
    • Redmond, T.M.1
  • 9
    • 0037174995 scopus 로고    scopus 로고
    • 11-cis-retinal reduces constitutive opsin phosphorylation and improves quantum catch in retinoid-deficient mouse rod photoreceptors
    • Ablonczy Z., et al. 11-cis-retinal reduces constitutive opsin phosphorylation and improves quantum catch in retinoid-deficient mouse rod photoreceptors. J. Biol. Chem. 277:2002;40491-40498.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40491-40498
    • Ablonczy, Z.1
  • 10
    • 0037251512 scopus 로고    scopus 로고
    • -/- mice during development and aging
    • -/- mice during development and aging. Invest. Ophthalmol. Vis. Sci. 44:2003;310-315.
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 310-315
    • Rohrer, B.1
  • 11
    • 0029993990 scopus 로고    scopus 로고
    • Activating mutations of rhodopsin and other G protein-coupled receptors
    • Rao V.R., Oprian D.D. Activating mutations of rhodopsin and other G protein-coupled receptors. Annu. Rev. Biophys. Biomol. Struct. 25:1996;287-314.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 287-314
    • Rao, V.R.1    Oprian, D.D.2
  • 12
    • 0037465429 scopus 로고    scopus 로고
    • Characterization of rhodopsin congenital night blindness mutant T94I
    • Gross A.K., et al. Characterization of rhodopsin congenital night blindness mutant T94I. Biochemistry. 42:2003;2009-2015.
    • (2003) Biochemistry , vol.42 , pp. 2009-2015
    • Gross, A.K.1
  • 13
    • 0037465424 scopus 로고    scopus 로고
    • Slow binding of retinal to rhodopsin mutants G90D and T94D
    • Gross A.K., et al. Slow binding of retinal to rhodopsin mutants G90D and T94D. Biochemistry. 42:2003;2002-2008.
    • (2003) Biochemistry , vol.42 , pp. 2002-2008
    • Gross, A.K.1
  • 14
    • 0037743559 scopus 로고    scopus 로고
    • Opsin activation as a cause of congenital night blindness
    • Jin S., et al. Opsin activation as a cause of congenital night blindness. Nat. Neurosci. 6:2003;731-735.
    • (2003) Nat. Neurosci. , vol.6 , pp. 731-735
    • Jin, S.1
  • 15
    • 0027248024 scopus 로고
    • Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness
    • Dryja T.P., et al. Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness. Nat. Genet. 4:1993;280-283.
    • (1993) Nat. Genet. , vol.4 , pp. 280-283
    • Dryja, T.P.1
  • 16
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • Rao V.R., et al. Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature. 367:1994;639-641.
    • (1994) Nature , vol.367 , pp. 639-641
    • Rao, V.R.1
  • 17
    • 0035425947 scopus 로고    scopus 로고
    • Constitutive 'light' adaptation in rods from G90D rhodopsin: A mechanism for human congenital nightblindness without rod cell loss
    • Sieving P.A., et al. Constitutive 'light' adaptation in rods from G90D rhodopsin: a mechanism for human congenital nightblindness without rod cell loss. J. Neurosci. 21:2001;5449-5460.
    • (2001) J. Neurosci. , vol.21 , pp. 5449-5460
    • Sieving, P.A.1
  • 18
    • 0028798659 scopus 로고
    • Dark-light: Model for nightblindness from the human rhodopsin Gly-90→Asp mutation
    • Sieving P.A., et al. Dark-light: model for nightblindness from the human rhodopsin Gly-90→Asp mutation. Proc. Natl. Acad. Sci. U. S. A. 92:1995;880-884.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 880-884
    • Sieving, P.A.1
  • 19
    • 0037458628 scopus 로고    scopus 로고
    • Unusual thermal and conformational properties of the rhodopsin congenital night blindness mutant Thr-94-Ile
    • Ramon E., et al. Unusual thermal and conformational properties of the rhodopsin congenital night blindness mutant Thr-94-Ile. J. Biol. Chem. 278:2003;6427-6432.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6427-6432
    • Ramon, E.1
  • 20
    • 0028005422 scopus 로고
    • Bleached pigment activates transduction in isolated rods of the salamander retina
    • Cornwall M.C., Fain G.L. Bleached pigment activates transduction in isolated rods of the salamander retina. J. Physiol. 480:1994;261-279.
    • (1994) J. Physiol. , vol.480 , pp. 261-279
    • Cornwall, M.C.1    Fain, G.L.2
  • 21
    • 0343580431 scopus 로고    scopus 로고
    • A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin
    • Melia T.J. Jr, et al. A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin. Biophys. J. 73:1997;3182-3191.
    • (1997) Biophys. J. , vol.73 , pp. 3182-3191
    • Melia Jr., T.J.1
  • 22
    • 0020571486 scopus 로고
    • Rhodopsin chromophore exchanges among opsin molecules in the dark
    • Defoe D.M., Bok D. Rhodopsin chromophore exchanges among opsin molecules in the dark. Invest. Ophthalmol. Vis. Sci. 24:1983;1211-1226.
    • (1983) Invest. Ophthalmol. Vis. Sci. , vol.24 , pp. 1211-1226
    • Defoe, D.M.1    Bok, D.2
  • 23
    • 0026661978 scopus 로고
    • Constitutively active mutants of rhodopsin
    • Robinson P.R., et al. Constitutively active mutants of rhodopsin. Neuron. 9:1992;719-725.
    • (1992) Neuron , vol.9 , pp. 719-725
    • Robinson, P.R.1
  • 24
    • 0028947938 scopus 로고
    • Constitutive activation of phototransduction by K296E opsin is not a cause of photoreceptor degeneration
    • Li T., et al. Constitutive activation of phototransduction by K296E opsin is not a cause of photoreceptor degeneration. Proc. Natl. Acad. Sci. U. S. A. 92:1995;3551-3555.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3551-3555
    • Li, T.1
  • 25
    • 0025944670 scopus 로고
    • Autosomal dominant retinitis pigmentosa: Four new mutations in rhodopsin, one of them in the retinal attachment site
    • Keen T.J., et al. Autosomal dominant retinitis pigmentosa: four new mutations in rhodopsin, one of them in the retinal attachment site. Genomics. 11:1991;199-205.
    • (1991) Genomics , vol.11 , pp. 199-205
    • Keen, T.J.1
  • 28
    • 0036787618 scopus 로고    scopus 로고
    • Evidence for two apoptotic pathways in light-induced retinal degeneration
    • Hao W., et al. Evidence for two apoptotic pathways in light-induced retinal degeneration. Nat. Genet. 32:2002;254-260.
    • (2002) Nat. Genet. , vol.32 , pp. 254-260
    • Hao, W.1
  • 29
    • 0031038950 scopus 로고    scopus 로고
    • Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness
    • Yamamoto S., et al. Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness. Nat. Genet. 15:1997;175-178.
    • (1997) Nat. Genet. , vol.15 , pp. 175-178
    • Yamamoto, S.1
  • 30
    • 0031892644 scopus 로고    scopus 로고
    • Null mutation in the rhodopsin kinase gene slows recovery kinetics of rod and cone phototransduction in man
    • Cideciyan A.V., et al. Null mutation in the rhodopsin kinase gene slows recovery kinetics of rod and cone phototransduction in man. Proc. Natl. Acad. Sci. U. S. A. 95:1998;328-333.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 328-333
    • Cideciyan, A.V.1
  • 31
    • 0029067542 scopus 로고
    • A homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese
    • Fuchs S., et al. A homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese. Nat. Genet. 10:1995;360-362.
    • (1995) Nat. Genet. , vol.10 , pp. 360-362
    • Fuchs, S.1
  • 32
    • 0031894886 scopus 로고    scopus 로고
    • Arrestin gene mutations in autosomal recessive retinitis pigmentosa
    • Nakazawa M., et al. Arrestin gene mutations in autosomal recessive retinitis pigmentosa. Arch. Ophthalmol. 116:1998;498-501.
    • (1998) Arch. Ophthalmol. , vol.116 , pp. 498-501
    • Nakazawa, M.1
  • 33
    • 0034682551 scopus 로고    scopus 로고
    • Rapid restoration of visual pigment and function with oral retinoid in a mouse model of childhood blindness
    • Van Hooser J.P., et al. Rapid restoration of visual pigment and function with oral retinoid in a mouse model of childhood blindness. Proc. Natl. Acad. Sci. U. S. A. 97:2000;8623-8628.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8623-8628
    • Van Hooser, J.P.1
  • 34
    • 0028820045 scopus 로고
    • Mutations in the gene encoding the α subunit of the rod cGMP-gated channel in autosomal recessive retinitis pigmentosa
    • Dryja T.P., et al. Mutations in the gene encoding the α subunit of the rod cGMP-gated channel in autosomal recessive retinitis pigmentosa. Proc. Natl. Acad. Sci. U. S. A. 92:1995;10177-10181.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 10177-10181
    • Dryja, T.P.1
  • 35
    • 0028892944 scopus 로고
    • Support for the equivalent light hypothesis for RP
    • Lisman J., Fain G. Support for the equivalent light hypothesis for RP. Nat. Med. 1:1995;1254-1255.
    • (1995) Nat. Med. , vol.1 , pp. 1254-1255
    • Lisman, J.1    Fain, G.2
  • 36
    • 0032477872 scopus 로고    scopus 로고
    • A null mutation in the photoreceptor guanylate cyclase gene causes the retinal degeneration chicken phenotype
    • Semple-Rowland S.L., et al. A null mutation in the photoreceptor guanylate cyclase gene causes the retinal degeneration chicken phenotype. Proc. Natl. Acad. Sci. U. S. A. 95:1998;1271-1276.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1271-1276
    • Semple-Rowland, S.L.1
  • 37
    • 0842264403 scopus 로고    scopus 로고
    • Lecithin:retinol acyltransferase (LRAT) is essential for retention of retinyl esters in the eye and in the liver
    • 10.1074/jbc.M132410200
    • Batten, M.L. et al. (2003) Lecithin:retinol acyltransferase (LRAT) is essential for retention of retinyl esters in the eye and in the liver. J. Biol. Chem. 10.1074/jbc.M132410200 (www.jbc.org).
    • (2003) J. Biol. Chem.
    • Batten, M.L.1
  • 38
    • 0034973574 scopus 로고    scopus 로고
    • Mutations in the gene encoding lecithin retinol acyltransferase are associated with early-onset severe retinal dystrophy
    • Thompson D.A., et al. Mutations in the gene encoding lecithin retinol acyltransferase are associated with early-onset severe retinal dystrophy. Nat. Genet. 28:2001;123-124.
    • (2001) Nat. Genet. , vol.28 , pp. 123-124
    • Thompson, D.A.1
  • 39
    • 0021358230 scopus 로고
    • Cation selectivity of light-sensitive conductance in retinal rods
    • Yau K.W., Nakatani K. Cation selectivity of light-sensitive conductance in retinal rods. Nature. 309:1984;352-354.
    • (1984) Nature , vol.309 , pp. 352-354
    • Yau, K.W.1    Nakatani, K.2
  • 40
    • 0021909037 scopus 로고
    • The ionic selectivity and calcium dependence of the light-sensitive pathway in toad rods
    • Hodgkin A.L., et al. The ionic selectivity and calcium dependence of the light-sensitive pathway in toad rods. J. Physiol. 358:1985;447-468.
    • (1985) J. Physiol. , vol.358 , pp. 447-468
    • Hodgkin, A.L.1
  • 41
    • 0242558891 scopus 로고    scopus 로고
    • The effect of light on outer segment calcium in salamander rods
    • Matthews H.R., Fain G.L. The effect of light on outer segment calcium in salamander rods. J. Physiol. 552:2003;763-776.
    • (2003) J. Physiol. , vol.552 , pp. 763-776
    • Matthews, H.R.1    Fain, G.L.2
  • 42
    • 0028018086 scopus 로고
    • Calcium chelators induce apoptosis-evidence that raised intracellular ionized calcium is not essential for apoptosis
    • Kluck R.M., et al. Calcium chelators induce apoptosis-evidence that raised intracellular ionized calcium is not essential for apoptosis. Biochim. Biophys. Acta. 1223:1994;247-254.
    • (1994) Biochim. Biophys. Acta , vol.1223 , pp. 247-254
    • Kluck, R.M.1
  • 43
    • 0014767671 scopus 로고
    • Potassium concentration and number of neurons in cultures of dissociated ganglia
    • Scott B.S., Fisher K.C. Potassium concentration and number of neurons in cultures of dissociated ganglia. Exp. Neurol. 27:1970;16-22.
    • (1970) Exp. Neurol. , vol.27 , pp. 16-22
    • Scott, B.S.1    Fisher, K.C.2
  • 44
    • 0023244774 scopus 로고
    • The role of depolarization in the survival and differentiation of cerebellar granule cells in culture
    • Gallo V., et al. The role of depolarization in the survival and differentiation of cerebellar granule cells in culture. J. Neurosci. 7:1987;2203-2213.
    • (1987) J. Neurosci. , vol.7 , pp. 2203-2213
    • Gallo, V.1
  • 45
    • 0024711746 scopus 로고
    • 2+ determine nerve growth factor dependence of sympathetic ganglion cells
    • 2+ determine nerve growth factor dependence of sympathetic ganglion cells. Proc. Natl. Acad. Sci. U. S. A. 86:1989;6421-6425.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 6421-6425
    • Koike, T.1
  • 46
    • 0028644132 scopus 로고
    • Elevated intracellular calcium blocks programmed neuronal death
    • Franklin J.L., Johnson E.M. Jr. Elevated intracellular calcium blocks programmed neuronal death. Ann. N. Y. Acad. Sci. 747:1994;195-204.
    • (1994) Ann. N. Y. Acad. Sci. , vol.747 , pp. 195-204
    • Franklin, J.L.1    Johnson Jr., E.M.2
  • 47
    • 0028831283 scopus 로고
    • 2+ influx but not Trk activation
    • 2+ influx but not Trk activation. J. Neurosci. 15:1995;643-664.
    • (1995) J. Neurosci. , vol.15 , pp. 643-664
    • Franklin, J.L.1
  • 48
    • 0032519650 scopus 로고    scopus 로고
    • Calmodulin is involved in membrane depolarization-mediated survival of motoneurons by phosphatidylinositol-3 kinase and MAPK independent pathways
    • Soler R.M., et al. Calmodulin is involved in membrane depolarization-mediated survival of motoneurons by phosphatidylinositol-3 kinase and MAPK independent pathways. J. Neurosci. 18:1998;1230-1239.
    • (1998) J. Neurosci. , vol.18 , pp. 1230-1239
    • Soler, R.M.1
  • 50
    • 0141884305 scopus 로고    scopus 로고
    • Diversity in the mechanisms of neuronal cell death
    • Yuan J., et al. Diversity in the mechanisms of neuronal cell death. Neuron. 40:2003;401-413.
    • (2003) Neuron , vol.40 , pp. 401-413
    • Yuan, J.1
  • 51
    • 0024392837 scopus 로고
    • Neurotransmitter regulation of neuronal outgrowth, plasticity and survival
    • Lipton S.A., Kater S.B. Neurotransmitter regulation of neuronal outgrowth, plasticity and survival. Trends Neurosci. 12:1989;265-270.
    • (1989) Trends Neurosci. , vol.12 , pp. 265-270
    • Lipton, S.A.1    Kater, S.B.2
  • 52
    • 0036687344 scopus 로고    scopus 로고
    • Measurement of cytoplasmic calcium concentration in the rods of wild-type and transducin knock-out mice
    • Woodruff M.L., et al. Measurement of cytoplasmic calcium concentration in the rods of wild-type and transducin knock-out mice. J. Physiol. 542:2002;843-854.
    • (2002) J. Physiol. , vol.542 , pp. 843-854
    • Woodruff, M.L.1
  • 53
    • 0034955572 scopus 로고    scopus 로고
    • Fundus albipunctatus and retinitis punctata albescens in a pedigree with an R150Q mutation in RLBP1
    • Katsanis N., et al. Fundus albipunctatus and retinitis punctata albescens in a pedigree with an R150Q mutation in RLBP1. Clin. Genet. 59:2001;424-429.
    • (2001) Clin. Genet. , vol.59 , pp. 424-429
    • Katsanis, N.1
  • 54
    • 0035046365 scopus 로고    scopus 로고
    • Visual cycle impairment in cellular retinaldehyde binding protein (CRALBP) knockout mice results in delayed dark adaptation
    • Saari J.C., et al. Visual cycle impairment in cellular retinaldehyde binding protein (CRALBP) knockout mice results in delayed dark adaptation. Neuron. 29:2001;739-748.
    • (2001) Neuron , vol.29 , pp. 739-748
    • Saari, J.C.1
  • 55
    • 0033033364 scopus 로고    scopus 로고
    • Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus
    • Yamamoto H., et al. Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus. Nat. Genet. 22:1999;188-191.
    • (1999) Nat. Genet. , vol.22 , pp. 188-191
    • Yamamoto, H.1
  • 56
    • 0025860857 scopus 로고
    • Elevated level of protein phosphatase 2A activity in retinas of rd mice
    • Palczewski K., et al. Elevated level of protein phosphatase 2A activity in retinas of rd mice. Exp. Eye Res. 53:1991;101-105.
    • (1991) Exp. Eye Res. , vol.53 , pp. 101-105
    • Palczewski, K.1


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