메뉴 건너뛰기




Volumn 107, Issue 1, 1996, Pages 19-34

The kinetics of inactivation of the rod phototransduction cascade with constant Ca2+i

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM ION; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; GUANYLATE CYCLASE; PHOSPHODIESTERASE; PHOSPHOTRANSFERASE; RECOVERIN; RETINA S ANTIGEN; RHODOPSIN;

EID: 0030068240     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.107.1.19     Document Type: Article
Times cited : (70)

References (51)
  • 1
    • 0028340572 scopus 로고
    • Enhancement of rod outer segment GTPase accelerating protein activity by the inhibitory subunit of cGMP phosphodiesterase
    • Angleson, J. K., and T. G. Wensel. 1994. Enhancement of rod outer segment GTPase accelerating protein activity by the inhibitory subunit of cGMP phosphodiesterase. J. Biol. Chem. 269:16290-16296.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16290-16296
    • Angleson, J.K.1    Wensel, T.G.2
  • 2
    • 0026742007 scopus 로고
    • Regulation of deactivation of photoreceptor G protein by its target enzyme and cGMP
    • Arshavsky, V. Y., and M. D. Bownds. 1992. Regulation of deactivation of photoreceptor G protein by its target enzyme and cGMP. Nature (Lond.). 357:416-417.
    • (1992) Nature (Lond.) , vol.357 , pp. 416-417
    • Arshavsky, V.Y.1    Bownds, M.D.2
  • 3
    • 0026489531 scopus 로고
    • Non-catalytic cGMP binding sites of amphibian rod cGMP phosphodiesterase control interaction with its inhibitory γ-subunits. A putative regulatory mechanism of the rod photoresponse
    • Arshavsky, V. Y., C. L. Dumke, and M. D. Bownds. 1992. Non-catalytic cGMP binding sites of amphibian rod cGMP phosphodiesterase control interaction with its inhibitory γ-subunits. A putative regulatory mechanism of the rod photoresponse. J. Biol. Chem., 267:24001-24507.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24001-24507
    • Arshavsky, V.Y.1    Dumke, C.L.2    Bownds, M.D.3
  • 5
    • 0018536273 scopus 로고
    • A voltageclamp study of the light response in solitary rods of the tiger salamander
    • Bader, D. R., P. R. MacLeish, and E. A. Schwartz. 1979. A voltageclamp study of the light response in solitary rods of the tiger salamander. J Physiol. (Lond.). 296:1-26.
    • (1979) J Physiol. (Lond.) , vol.296 , pp. 1-26
    • Bader, D.R.1    MacLeish, P.R.2    Schwartz, E.A.3
  • 6
    • 0016231987 scopus 로고
    • The electrical response of turtle cones to flashes and steps of light
    • Baylor, D. A., A. L. Hodgkin, and T. D. Lamb. 1974. The electrical response of turtle cones to flashes and steps of light. J. Physiol. (Lond.). 242:685-727.
    • (1974) J. Physiol. (Lond.) , vol.242 , pp. 685-727
    • Baylor, D.A.1    Hodgkin, A.L.2    Lamb, T.D.3
  • 7
    • 0022560529 scopus 로고
    • Electrical properties of the light-sensitive conductance of rods of the salamander Ambystoma tigrinum
    • Baylor, D. A., and B. J. Nunn. 1986. Electrical properties of the light-sensitive conductance of rods of the salamander Ambystoma tigrinum. J. Physiol. (Lond.). 371:115-145.
    • (1986) J. Physiol. (Lond.) , vol.371 , pp. 115-145
    • Baylor, D.A.1    Nunn, B.J.2
  • 8
    • 0023841528 scopus 로고
    • Inactivation of photoexcited rhodopsin in retinal rods: The roles of rhodopsin kinase and 48-dDa protein (Arrestin)
    • Bennett, N., and A. Sitaramayya. 1988. Inactivation of photoexcited rhodopsin in retinal rods: the roles of rhodopsin kinase and 48-dDa protein (Arrestin). Biochemistry. 27:1710-1715.
    • (1988) Biochemistry , vol.27 , pp. 1710-1715
    • Bennett, N.1    Sitaramayya, A.2
  • 9
    • 0028158701 scopus 로고
    • Analysis of ERG α-wave amplification and kinetics in terms of the G-protein cascade of phototransduction
    • Breton, M. E., A. W. Schueller, T. D. Lamb, and E. N. Pugh, Jr. 1994. Analysis of ERG α-wave amplification and kinetics in terms of the G-protein cascade of phototransduction. Invest. Ophthalmol. Vis. Sci. 35:295-309.
    • (1994) Invest. Ophthalmol. Vis. Sci. , vol.35 , pp. 295-309
    • Breton, M.E.1    Schueller, A.W.2    Lamb, T.D.3    Pugh Jr., E.N.4
  • 11
    • 0023623304 scopus 로고
    • Kinetics and components of the flash photocurrent of isolated retinal rods of the larval salamander Ambystona tigrinum
    • Cobbs, W. H., and E. N. Pugh, Jr. 1987. Kinetics and components of the flash photocurrent of isolated retinal rods of the larval salamander Ambystona tigrinum. J. Physiol. (Lond.). 394:529-572.
    • (1987) J. Physiol. (Lond.) , vol.394 , pp. 529-572
    • Cobbs, W.H.1    Pugh Jr., E.N.2
  • 12
    • 0001908198 scopus 로고
    • Fitting and statistical analysis of single-channel records
    • B. Sakmann and E. Neher, editors. Plenum Publishing Corp., New York
    • Colquhoun, D., and F. J. Sigworth. 1983. Fitting and statistical analysis of single-channel records. In Single-Channel Recording. B. Sakmann and E. Neher, editors. Plenum Publishing Corp., New York.
    • (1983) Single-Channel Recording
    • Colquhoun, D.1    Sigworth, F.J.2
  • 13
    • 0028240943 scopus 로고
    • Rod outer segment structure influences the apparent kinetic parameters of cyclic GMP phosphodiesterase
    • Dumke, C. L., V. Y. Arshavsky, P. D. Calvert, M. D. Bownds, and E. N. Pugh, Jr. 1994. Rod outer segment structure influences the apparent kinetic parameters of cyclic GMP phosphodiesterase. J. Gen. Physiol. 103:1071-1098.
    • (1994) J. Gen. Physiol. , vol.103 , pp. 1071-1098
    • Dumke, C.L.1    Arshavsky, V.Y.2    Calvert, P.D.3    Bownds, M.D.4    Pugh Jr., E.N.5
  • 14
    • 0020581198 scopus 로고
    • A survey of readily available chelators for buffering calcium ion concentrations in physiological solutions
    • Durham, A. C. H. 1983. A survey of readily available chelators for buffering calcium ion concentrations in physiological solutions. Cell Calcium. 4:33-46.
    • (1983) Cell Calcium , vol.4 , pp. 33-46
    • Durham, A.C.H.1
  • 15
    • 0024429983 scopus 로고
    • Cytoplasmic calcium as the messenger for light adaptation in salamander rods
    • Fain, G. L., T. D. Lamb, H. R. Matthews, and R. L. W. Murphy. 1989. Cytoplasmic calcium as the messenger for light adaptation in salamander rods. J. Physiol. (Lond.). 416:215-243.
    • (1989) J. Physiol. (Lond.) , vol.416 , pp. 215-243
    • Fain, G.L.1    Lamb, T.D.2    Matthews, H.R.3    Murphy, R.L.W.4
  • 16
    • 0028331799 scopus 로고
    • Purification and physiological evaluation of a guanylate cyclase activating protein from retinal rods
    • Gorczya, W. A., M. P. Gray-Keller, P. B. Detwiler, and K. Palczewski. 1994. Purification and physiological evaluation of a guanylate cyclase activating protein from retinal rods. Proc. Natl. Acad. Sci. USA. 91:4014-4018.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4014-4018
    • Gorczya, W.A.1    Gray-Keller, M.P.2    Detwiler, P.B.3    Palczewski, K.4
  • 17
    • 0028079834 scopus 로고
    • The calcium feedback signal in the phototransduction cascade of vertebrate rods
    • Gray-Keller, M. P., and P. B. Detwiler. 1994. The calcium feedback signal in the phototransduction cascade of vertebrate rods. Neuron. 13:849-861.
    • (1994) Neuron , vol.13 , pp. 849-861
    • Gray-Keller, M.P.1    Detwiler, P.B.2
  • 18
    • 0014782201 scopus 로고
    • Dark current and photocurrent in retinal rods
    • Hagins, W. A., R. D. Penn, and S. Yoshikami. 1970. Dark current and photocurrent in retinal rods. Biophys. J. 10:380-412.
    • (1970) Biophys. J. , vol.10 , pp. 380-412
    • Hagins, W.A.1    Penn, R.D.2    Yoshikami, S.3
  • 19
    • 0003818389 scopus 로고
    • Holt, Rinehart and Winston, New York
    • Hays, W. L. 1963. Statistics. Holt, Rinehart and Winston, New York.
    • (1963) Statistics
    • Hays, W.L.1
  • 20
    • 0023731353 scopus 로고
    • Control of light-sensitive current in salamander rods
    • Hodgkin, A. L., and B. J. Nunn. 1988. Control of light-sensitive current in salamander rods. J. Physiol. (Lond.). 403:439-471.
    • (1988) J. Physiol. (Lond.) , vol.403 , pp. 439-471
    • Hodgkin, A.L.1    Nunn, B.J.2
  • 22
    • 0021909037 scopus 로고
    • The ionic selectivity and calcium dependence of the light-sensitive pathway in toad rods
    • Hodgkin, A. L., P. A. McNaughton, and B. J. Nunn. 1985. The ionic selectivity and calcium dependence of the light-sensitive pathway in toad rods. J. Physiol. (Lond.). 358:447-468.
    • (1985) J. Physiol. (Lond.) , vol.358 , pp. 447-468
    • Hodgkin, A.L.1    McNaughton, P.A.2    Nunn, B.J.3
  • 23
    • 0023193163 scopus 로고
    • Measurement of sodium-calcium exchange in salamander rods
    • Hodgkin, A. L., P. A. McNaughton, and B. J. Nunn. 1987. Measurement of sodium-calcium exchange in salamander rods. J. Physiol. (Lond.). 391:347-370.
    • (1987) J. Physiol. (Lond.) , vol.391 , pp. 347-370
    • Hodgkin, A.L.1    McNaughton, P.A.2    Nunn, B.J.3
  • 24
    • 3643148051 scopus 로고
    • Light-induced protein-protein interactions on the rod photoreceptor disc membrane
    • Lee, editor. JAI Press
    • Hofmann, K. P., and M. Heck. 1995. Light-induced protein-protein interactions on the rod photoreceptor disc membrane. In Biomembranes II. Lee, editor. JAI Press.
    • (1995) Biomembranes II
    • Hofmann, K.P.1    Heck, M.2
  • 25
    • 0028229520 scopus 로고
    • Rod phototransduction in retinitis pigmentosa: Estimation and interpretation of parameters derived from the rod α-wave
    • Hood, D. C., and D. G. Birch. 1994. Rod phototransduction in retinitis pigmentosa: estimation and interpretation of parameters derived from the rod α-wave. Invest. Ophthalmol. Vis. Sci. 35:2948-2961.
    • (1994) Invest. Ophthalmol. Vis. Sci. , vol.35 , pp. 2948-2961
    • Hood, D.C.1    Birch, D.G.2
  • 26
    • 0025368905 scopus 로고
    • Effect of bleached rhodopsin on signal amplification in rod visual receptors
    • Kahlert, M., D. R. Pepperberg, and K. P. Hofmann. 1990. Effect of bleached rhodopsin on signal amplification in rod visual receptors. Nature (Lond.). 345:537-539.
    • (1990) Nature (Lond.) , vol.345 , pp. 537-539
    • Kahlert, M.1    Pepperberg, D.R.2    Hofmann, K.P.3
  • 27
    • 0006044440 scopus 로고
    • Gating kinetics of the cyclic GMP-activated channel of retinal rods: Flash photolysis and voltage clamp studies
    • Karpen, J. W., A. L. Zimmerman, L. Suyer, and D. A. Baylor. 1988. Gating kinetics of the cyclic GMP-activated channel of retinal rods: flash photolysis and voltage clamp studies. Proc. Natl Acad. Sci. USA. 85:1287-1291.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 1287-1291
    • Karpen, J.W.1    Zimmerman, A.L.2    Suyer, L.3    Baylor, D.A.4
  • 28
    • 0027264959 scopus 로고
    • Rhodopsin phosphorylation as a mechanism of cyclic GMP phosphodiesterase regulation by S-modulin
    • Kawamura, S. 1993. Rhodopsin phosphorylation as a mechanism of cyclic GMP phosphodiesterase regulation by S-modulin. Nature (Lond.). 362:855-857.
    • (1993) Nature (Lond.) , vol.362 , pp. 855-857
    • Kawamura, S.1
  • 29
    • 0029033531 scopus 로고
    • Inhibition of rhodopsin kinase by recoverin: Evidence for a negative feedback system in phototransduction
    • Klenchin, V. A., P. D. Calvert, and M. D. Bownds. 1995. Inhibition of rhodopsin kinase by recoverin: evidence for a negative feedback system in phototransduction. J. Biol. Chem. 270:16147-16152.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16147-16152
    • Klenchin, V.A.1    Calvert, P.D.2    Bownds, M.D.3
  • 31
    • 0028047175 scopus 로고
    • Calcium controls light-triggered formation of catalytically active rhodopsin
    • Lagnado, L., and D. A. Baylor. 1994. Calcium controls light-triggered formation of catalytically active rhodopsin. Nature (Lond.). 367:273-277.
    • (1994) Nature (Lond.) , vol.367 , pp. 273-277
    • Lagnado, L.1    Baylor, D.A.2
  • 32
    • 0026698863 scopus 로고
    • Calcium homeostasis in the outer segments of retinal rods from the tiger salamander
    • Lagnado, L., L. Cervetto, and P. A. McNaughton. 1992. Calcium homeostasis in the outer segments of retinal rods from the tiger salamander. J. Physiol. 455:111-142.
    • (1992) J. Physiol. , vol.455 , pp. 111-142
    • Lagnado, L.1    Cervetto, L.2    McNaughton, P.A.3
  • 33
    • 0028085969 scopus 로고
    • Stochastic simulation of activation in the G-protein cascade of phototransduction
    • Lamb, T. D. 1994. Stochastic simulation of activation in the G-protein cascade of phototransduction. Biophys. J. 67:1439-1454.
    • (1994) Biophys. J. , vol.67 , pp. 1439-1454
    • Lamb, T.D.1
  • 34
    • 0024245385 scopus 로고
    • Incorporation of analogues of GTP and GDP into rod photoreceptors isolated from the tiger salamander
    • Lamb, T. D., and H. R. Matthews. 1988. Incorporation of analogues of GTP and GDP into rod photoreceptors isolated from the tiger salamander. J. Physiol. (Lond.). 407:463-487.
    • (1988) J. Physiol. (Lond.) , vol.407 , pp. 463-487
    • Lamb, T.D.1    Matthews, H.R.2
  • 35
    • 0026505707 scopus 로고
    • A quantitative account of the activation steps involved in phototransduction in amphibian photoreceptors
    • Lamb, T. D., and Pugh, E. N., Jr. 1992. A quantitative account of the activation steps involved in phototransduction in amphibian photoreceptors. J. Physiol. (Lond.). 449:719-758.
    • (1992) J. Physiol. (Lond.) , vol.449 , pp. 719-758
    • Lamb, T.D.1    Pugh Jr., E.N.2
  • 36
    • 0028957288 scopus 로고
    • Effects of lowered cytoplasmic calcium concentration and light on the responses of salamander rod photoreceptors
    • Matthews, H. R. 1995. Effects of lowered cytoplasmic calcium concentration and light on the responses of salamander rod photoreceptors. J. Physiol. (Lond.) 484:267-286.
    • (1995) J. Physiol. (Lond.) , vol.484 , pp. 267-286
    • Matthews, H.R.1
  • 37
    • 0023919180 scopus 로고
    • Photoreceptor light adaptation is mediated by cytoplasmic calcium concentration
    • Matthews, H. R., R. I., W. Murphy, G. L. Fain, and T. D. Lamb. 1988. Photoreceptor light adaptation is mediated by cytoplasmic calcium concentration. Nature (Lond.). 334:67-69.
    • (1988) Nature (Lond.) , vol.334 , pp. 67-69
    • Matthews, H.R.1    Murphy, R.I.W.2    Fain, G.L.3    Lamb, T.D.4
  • 38
    • 0028113655 scopus 로고
    • Differences in calcium homeostasis between retinal rod and cone photoreceptors revealed by the effects of voltage on the cGMP-gated conductance in intact cells
    • Miller, J. L., and J. I. Korenbrot. 1994. Differences in calcium homeostasis between retinal rod and cone photoreceptors revealed by the effects of voltage on the cGMP-gated conductance in intact cells. J. Gen. Physiol. 104:909-940.
    • (1994) J. Gen. Physiol. , vol.104 , pp. 909-940
    • Miller, J.L.1    Korenbrot, J.I.2
  • 39
    • 0023941670 scopus 로고
    • Calcium and light adaptation in retinal rods and cones
    • Nakatani, K., and K.-W. Yau. 1988. Calcium and light adaptation in retinal rods and cones. Nature (Lond.). 334:69-71.
    • (1988) Nature (Lond.) , vol.334 , pp. 69-71
    • Nakatani, K.1    Yau, K.-W.2
  • 40
    • 0024502591 scopus 로고
    • Sodium-dependent calcium extrusion and sensitivity regulation in retinal cones of the salamander
    • Nakatani, K., and K.-W. Yau. 1989. Sodium-dependent calcium extrusion and sensitivity regulation in retinal cones of the salamander. J. Physiol. (Lond.). 409:525-548.
    • (1989) J. Physiol. (Lond.) , vol.409 , pp. 525-548
    • Nakatani, K.1    Yau, K.-W.2
  • 43
    • 0023813698 scopus 로고
    • Photic modulation of a highly sensitive, near-infrared light-scattering signal recorded from intact retinal photoreceptors
    • Pepperberg, D. R., M. Kahlert, A. Krause, and K. P. Hofmann. 1988. Photic modulation of a highly sensitive, near-infrared light-scattering signal recorded from intact retinal photoreceptors. Proc. Natl. Acad Sci. USA. 85:5531-5535.
    • (1988) Proc. Natl. Acad Sci. USA , vol.85 , pp. 5531-5535
    • Pepperberg, D.R.1    Kahlert, M.2    Krause, A.3    Hofmann, K.P.4
  • 44
    • 0027407602 scopus 로고
    • Amplification and kinetics of the activation steps in phototransduction
    • Pugh, E. N., Jr., and T. D. Lamb. 1993. Amplification and kinetics of the activation steps in phototransduction. Biochim. Biophys. Acta. 1141:111-149
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 111-149
    • Pugh Jr., E.N.1    Lamb, T.D.2
  • 45
    • 0023754070 scopus 로고
    • The concentration of cytosolic free calcium in vertebrate outer segments measured with fura-2
    • Ratto, G. M., R Payne, W. G. Owen, and R. Y. Tsien. 1988. The concentration of cytosolic free calcium in vertebrate outer segments measured with fura-2. J. Neurosci. 8:3240-3246.
    • (1988) J. Neurosci. , vol.8 , pp. 3240-3246
    • Ratto, G.M.1    Payne, R.2    Owen, W.G.3    Tsien, R.Y.4
  • 46
    • 0020694118 scopus 로고
    • Mechanism of ATP quench of phosphodiesterase activation in rod disc membranes
    • Sitaramayya, A., and P. A. Liebman. 1983. Mechanism of ATP quench of phosphodiesterase activation in rod disc membranes. J. Biol. Chem. 258:1205-1209.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1205-1209
    • Sitaramayya, A.1    Liebman, P.A.2
  • 47
    • 0025863686 scopus 로고
    • Calcium feedback and sensitivity regulation in primate rods
    • Tamura, T., K. Nakatani, and K.-W. Yau. 1991. Calcium feedback and sensitivity regulation in primate rods. J. Gen. Physiol. 98:95-130.
    • (1991) J. Gen. Physiol. , vol.98 , pp. 95-130
    • Tamura, T.1    Nakatani, K.2    Yau, K.-W.3
  • 48
    • 0022478829 scopus 로고
    • Role of calcium in regulating the cyclic nucleotide cascade of phototransduction in retinal rods
    • Torre, V., H. R Matthews, and T. D. Lamb. 1986. Role of calcium in regulating the cyclic nucleotide cascade of phototransduction in retinal rods. Proc. Natl. Acad. Sci. USA. 83:7109-7113.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7109-7113
    • Torre, V.1    Matthews, H.R.2    Lamb, T.D.3
  • 49
    • 0020972777 scopus 로고
    • Intracellular measurements of ion activities
    • Tsien, R. Y. 1983. Intracellular measurements of ion activities. Annu. Rev. Biophys. Bioeng. 12:91-116.
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 91-116
    • Tsien, R.Y.1
  • 50
    • 0000025689 scopus 로고
    • Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48 KDa protein of rod outer segments
    • Wilden, U., S. W. Hall, and H. Kuhn. 1986. Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48 KDa protein of rod outer segments. Proc Natl Acad. Sci. USA 83:1174-1178.
    • (1986) Proc Natl Acad. Sci. USA , vol.83 , pp. 1174-1178
    • Wilden, U.1    Hall, S.W.2    Kuhn, H.3
  • 51
    • 0024564964 scopus 로고
    • Cyclic GMP-activated conductance of retinal photoreceptor cells
    • Yau, K.-W., and D. A. Baylor. 1989. Cyclic GMP-activated conductance of retinal photoreceptor cells. Anuu. Rev. Neurosci. 12:289-327.
    • (1989) Anuu. Rev. Neurosci. , vol.12 , pp. 289-327
    • Yau, K.-W.1    Baylor, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.