메뉴 건너뛰기




Volumn 6, Issue 5, 2011, Pages

Red fluorescent protein-aequorin fusions as improved bioluminescent Ca2+ reporters in single cells and mice

Author keywords

[No Author keywords available]

Indexed keywords

AEQUORIN; CALCIUM ION; HYBRID PROTEIN; RED FLUORESCENT PROTEIN; ADENOSINE TRIPHOSPHATE; CALCIUM; PHOTOPROTEIN; PRIMER DNA;

EID: 79955907733     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019520     Document Type: Article
Times cited : (44)

References (43)
  • 2
    • 0028987937 scopus 로고
    • Calcium signaling in neurons: molecular mechanisms and cellular consequences
    • Ghosh A, Greenberg ME, (1995) Calcium signaling in neurons: molecular mechanisms and cellular consequences. Science 268: 239-247.
    • (1995) Science , vol.268 , pp. 239-247
    • Ghosh, A.1    Greenberg, M.E.2
  • 3
    • 0023515143 scopus 로고
    • Calcium regulation of muscle contraction: the molecular regulation mechanisms of contracility
    • Ruegg JC, (1987) Calcium regulation of muscle contraction: the molecular regulation mechanisms of contracility. Naturwissenschaften 74: 579-584.
    • (1987) Naturwissenschaften , vol.74 , pp. 579-584
    • Ruegg, J.C.1
  • 5
    • 0021895138 scopus 로고
    • A New Generation of Ca2+ Indicators with Greatly Improved Fluorescence Properties
    • Grynkiewicz G, Poenie M, Tsien RY, (1985) A New Generation of Ca2+ Indicators with Greatly Improved Fluorescence Properties. JBC pp. 3440-3450.
    • (1985) JBC , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 7
    • 0030610646 scopus 로고    scopus 로고
    • Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin
    • Miyawaki A, Llopis J, Heim R, McCaffery JM, Adams JA, et al. (1997) Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin. Nature 388: 882-887.
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1    Llopis, J.2    Heim, R.3    McCaffery, J.M.4    Adams, J.A.5
  • 8
    • 0030133674 scopus 로고    scopus 로고
    • Shining the light: the mechanism of the bioluminescence reaction of calcium-binding photoproteins
    • Ohmiya Y, Hirano T, (1996) Shining the light: the mechanism of the bioluminescence reaction of calcium-binding photoproteins. ChemBiol 3: 337-347.
    • (1996) ChemBiol , vol.3 , pp. 337-347
    • Ohmiya, Y.1    Hirano, T.2
  • 9
    • 0028939743 scopus 로고
    • Cause of spectral variation in the luminescence of semisynthetic aequorins
    • Shimomura O, (1995) Cause of spectral variation in the luminescence of semisynthetic aequorins. BiochemJ 306 (Pt 2): 537-543.
    • (1995) BiochemJ , vol.306 , Issue.Pt 2 , pp. 537-543
    • Shimomura, O.1
  • 10
    • 0028832662 scopus 로고
    • Monitoring dynamic changes in free Ca2+ concentration in the endoplasmic reticulum of intact cells
    • Montero M, Brini M, Marsault R, Alvarez J, Sitia R, et al. (1995) Monitoring dynamic changes in free Ca2+ concentration in the endoplasmic reticulum of intact cells. EMBO J 14: 5467-5475.
    • (1995) EMBO J , vol.14 , pp. 5467-5475
    • Montero, M.1    Brini, M.2    Marsault, R.3    Alvarez, J.4    Sitia, R.5
  • 11
    • 57449113416 scopus 로고    scopus 로고
    • Modulation of calcium signalling by intracellular organelles seen with targeted aequorins
    • Alonso MT, Manjarres IM, Garcia-Sancho J, (2009) Modulation of calcium signalling by intracellular organelles seen with targeted aequorins. Acta Physiol (Oxf) 195: 37-49.
    • (2009) Acta Physiol (Oxf) , vol.195 , pp. 37-49
    • Alonso, M.T.1    Manjarres, I.M.2    Garcia-Sancho, J.3
  • 13
    • 0034691150 scopus 로고    scopus 로고
    • Chimeric green fluorescent protein-aequorin as bioluminescent Ca2+ reporters at the single-cell level
    • Baubet V, Le MH, Campbell AK, Lucas-Meunier E, Fossier P, et al. (2000) Chimeric green fluorescent protein-aequorin as bioluminescent Ca2+ reporters at the single-cell level. ProcNatlAcadSciUSA 97: 7260-7265.
    • (2000) ProcNatlAcadSciUSA , vol.97 , pp. 7260-7265
    • Baubet, V.1    Le, M.H.2    Campbell, A.K.3    Lucas-Meunier, E.4    Fossier, P.5
  • 14
    • 0027765629 scopus 로고
    • The relative rate of aequorin regeneration from apoaequorin and coelenterazine analogues
    • Shimomura O, Kishi Y, Inouye S, (1993) The relative rate of aequorin regeneration from apoaequorin and coelenterazine analogues. Biochem J 296 (Pt 3): 549-551.
    • (1993) Biochem J , vol.296 , Issue.Pt 3 , pp. 549-551
    • Shimomura, O.1    Kishi, Y.2    Inouye, S.3
  • 15
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • Shimomura O, Johnson FH, Saiga Y, (1962) Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J Cell Comp Physiol 59: 223-239.
    • (1962) J Cell Comp Physiol , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 16
    • 0016156057 scopus 로고
    • Intermolecular energy transfer in the bioluminescent system of Aequorea
    • Morise H, Shimomura O, Johnson FH, Winant J, (1974) Intermolecular energy transfer in the bioluminescent system of Aequorea. Biochemistry 13: 2656-2662.
    • (1974) Biochemistry , vol.13 , pp. 2656-2662
    • Morise, H.1    Shimomura, O.2    Johnson, F.H.3    Winant, J.4
  • 17
    • 0035424506 scopus 로고    scopus 로고
    • Measurement of proteases using chemiluminescence-resonance-energy-transfer chimaeras between green fluorescent protein and aequorin
    • Waud JP, Bermudez Fajardo A, Sudhaharan T, Trimby AR, Jeffery J, et al. (2001) Measurement of proteases using chemiluminescence-resonance-energy-transfer chimaeras between green fluorescent protein and aequorin. Biochem J 357: 687-697.
    • (2001) Biochem J , vol.357 , pp. 687-697
    • Waud, J.P.1    Bermudez Fajardo, A.2    Sudhaharan, T.3    Trimby, A.R.4    Jeffery, J.5
  • 18
    • 37249071850 scopus 로고    scopus 로고
    • Red and green aequorins for simultaneous monitoring of Ca2+ signals from two different organelles
    • Manjarres IM, Chamero P, Domingo B, Molina F, Llopis J, et al. (2008) Red and green aequorins for simultaneous monitoring of Ca2+ signals from two different organelles. Pflugers Arch 455: 961-970.
    • (2008) Pflugers Arch , vol.455 , pp. 961-970
    • Manjarres, I.M.1    Chamero, P.2    Domingo, B.3    Molina, F.4    Llopis, J.5
  • 19
    • 34247368977 scopus 로고    scopus 로고
    • Red-shifted aequorin-based bioluminescent reporters for in vivo imaging of Ca2+ signaling
    • Curie T, Rogers KL, Colasante C, Brulet P, (2007) Red-shifted aequorin-based bioluminescent reporters for in vivo imaging of Ca2+ signaling. Mol Imaging 6: 30-42.
    • (2007) Mol Imaging , vol.6 , pp. 30-42
    • Curie, T.1    Rogers, K.L.2    Colasante, C.3    Brulet, P.4
  • 20
    • 0037236238 scopus 로고    scopus 로고
    • Shedding light onto live molecular targets
    • Weissleder R, Ntziachristos V, (2003) Shedding light onto live molecular targets. NatMed 9: 123-128.
    • (2003) NatMed , vol.9 , pp. 123-128
    • Weissleder, R.1    Ntziachristos, V.2
  • 21
    • 29144442848 scopus 로고    scopus 로고
    • Emission spectra of bioluminescent reporters and interaction with mammalian tissue determine the sensitivity of detection in vivo
    • Zhao H, Doyle TC, Coquoz O, Kalish F, Rice BW, et al. (2005) Emission spectra of bioluminescent reporters and interaction with mammalian tissue determine the sensitivity of detection in vivo. JBiomedOpt 10: 41210.
    • (2005) JBiomedOpt , vol.10 , pp. 41210
    • Zhao, H.1    Doyle, T.C.2    Coquoz, O.3    Kalish, F.4    Rice, B.W.5
  • 22
    • 34547659144 scopus 로고    scopus 로고
    • Bright monomeric red fluorescent protein with an extended fluorescence lifetime
    • Merzlyak EM, Goedhart J, Shcherbo D, Bulina ME, Shcheglov AS, et al. (2007) Bright monomeric red fluorescent protein with an extended fluorescence lifetime. NatMethods 4: 555-557.
    • (2007) NatMethods , vol.4 , pp. 555-557
    • Merzlyak, E.M.1    Goedhart, J.2    Shcherbo, D.3    Bulina, M.E.4    Shcheglov, A.S.5
  • 23
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner NC, Campbell RE, Steinbach PA, Giepmans BN, Palmer AE, et al. (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. NatBiotechnol 22: 1567-1572.
    • (2004) NatBiotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5
  • 24
    • 0035800773 scopus 로고    scopus 로고
    • Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications
    • Griesbeck O, Baird GS, Campbell RE, Zacharias DA, Tsien RY, (2001) Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications. J Biol Chem 276: 29188-29194.
    • (2001) J Biol Chem , vol.276 , pp. 29188-29194
    • Griesbeck, O.1    Baird, G.S.2    Campbell, R.E.3    Zacharias, D.A.4    Tsien, R.Y.5
  • 25
    • 0026344311 scopus 로고
    • A C-terminal proline is required for bioluminescence of the Ca(2+)-binding photoprotein, aequorin
    • Nomura M, Inouye S, Ohmiya Y, Tsuji FI, (1991) A C-terminal proline is required for bioluminescence of the Ca(2+)-binding photoprotein, aequorin. FEBS Lett 295: 63-66.
    • (1991) FEBS Lett , vol.295 , pp. 63-66
    • Nomura, M.1    Inouye, S.2    Ohmiya, Y.3    Tsuji, F.I.4
  • 29
    • 77950951096 scopus 로고    scopus 로고
    • Structural characterization of acylimine-containing blue and red chromophores in mTagBFP and TagRFP fluorescent proteins
    • Subach OM, Malashkevich VN, Zencheck WD, Morozova KS, Piatkevich KD, et al. (2010) Structural characterization of acylimine-containing blue and red chromophores in mTagBFP and TagRFP fluorescent proteins. Chem Biol 17: 333-341.
    • (2010) Chem Biol , vol.17 , pp. 333-341
    • Subach, O.M.1    Malashkevich, V.N.2    Zencheck, W.D.3    Morozova, K.S.4    Piatkevich, K.D.5
  • 30
    • 77956152936 scopus 로고    scopus 로고
    • Mechanistic diversity of red fluorescence acquisition by GFP-like proteins
    • Wachter RM, Watkins JL, Kim H, (2010) Mechanistic diversity of red fluorescence acquisition by GFP-like proteins. Biochemistry 49: 7417-7427.
    • (2010) Biochemistry , vol.49 , pp. 7417-7427
    • Wachter, R.M.1    Watkins, J.L.2    Kim, H.3
  • 32
    • 33645217326 scopus 로고    scopus 로고
    • Blue fluorescent protein from the calcium-sensitive photoprotein aequorin: catalytic properties for the oxidation of coelenterazine as an oxygenase
    • Inouye S, Sasaki S, (2006) Blue fluorescent protein from the calcium-sensitive photoprotein aequorin: catalytic properties for the oxidation of coelenterazine as an oxygenase. FEBS Lett 580: 1977-1982.
    • (2006) FEBS Lett , vol.580 , pp. 1977-1982
    • Inouye, S.1    Sasaki, S.2
  • 33
    • 0025245420 scopus 로고
    • Calcium channels, stores, and oscillations
    • Tsien RW, Tsien RY, (1990) Calcium channels, stores, and oscillations. AnnuRevCell Biol 6: 715-760.
    • (1990) AnnuRevCell Biol , vol.6 , pp. 715-760
    • Tsien, R.W.1    Tsien, R.Y.2
  • 34
    • 0037370922 scopus 로고    scopus 로고
    • ATP-induced calcium oscillations and change of P2Y subtypes with culture conditions in HeLa cells
    • Okuda A, Furuya K, Kiyohara T, (2003) ATP-induced calcium oscillations and change of P2Y subtypes with culture conditions in HeLa cells. Cell BiochemFunct 21: 61-68.
    • (2003) Cell BiochemFunct , vol.21 , pp. 61-68
    • Okuda, A.1    Furuya, K.2    Kiyohara, T.3
  • 35
    • 58149354373 scopus 로고    scopus 로고
    • A redshifted codon-optimized firefly luciferase is a sensitive reporter for bioluminescence imaging
    • Caysa H, Jacob R, Muther N, Branchini B, Messerle M, et al. (2009) A redshifted codon-optimized firefly luciferase is a sensitive reporter for bioluminescence imaging. Photochem Photobiol Sci 8: 52-56.
    • (2009) Photochem Photobiol Sci , vol.8 , pp. 52-56
    • Caysa, H.1    Jacob, R.2    Muther, N.3    Branchini, B.4    Messerle, M.5
  • 36
    • 33746147768 scopus 로고    scopus 로고
    • In vivo monitoring of cutaneous edema using spectral imaging in the visible and near infrared
    • Stamatas GN, Southall M, Kollias N, (2006) In vivo monitoring of cutaneous edema using spectral imaging in the visible and near infrared. J Invest Dermatol 126: 1753-1760.
    • (2006) J Invest Dermatol , vol.126 , pp. 1753-1760
    • Stamatas, G.N.1    Southall, M.2    Kollias, N.3
  • 37
    • 77953865084 scopus 로고    scopus 로고
    • Principles of Fluorescence Spectroscopy
    • Springer Science 3rd Edition
    • Lakowicz JR, (2006) Principles of Fluorescence Spectroscopy. Springer Science 3rd Edition pp. 443-450.
    • (2006) , pp. 443-450
    • Lakowicz, J.R.1
  • 38
    • 71049156731 scopus 로고    scopus 로고
    • Anomalous surplus energy transfer observed with multiple FRET acceptors
    • Koushik SV, Blank PS, Vogel SS, (2009) Anomalous surplus energy transfer observed with multiple FRET acceptors. PLoS One 4: e8031.
    • (2009) PLoS One , vol.4
    • Koushik, S.V.1    Blank, P.S.2    Vogel, S.S.3
  • 39
    • 0347720886 scopus 로고    scopus 로고
    • Practical use of corrected fluorescence excitation and emission spectra of fluorescent proteins in Förster Resonance Energy Transfer (FRET) studies
    • Hink MA, Visser NV, Borst JW, Hoek Av, Visser AJWG, (2004) Practical use of corrected fluorescence excitation and emission spectra of fluorescent proteins in Förster Resonance Energy Transfer (FRET) studies. J FLUORESC 13: 185-188.
    • (2004) J FLUORESC , vol.13 , pp. 185-188
    • Hink, M.A.1    Visser, N.V.2    Borst, J.W.3    Hoek, A.v.4    Visser, A.J.W.G.5
  • 40
    • 3042727962 scopus 로고    scopus 로고
    • Fusion of Aequorea victoria GFP and aequorin provides their Ca(2+)-induced interaction that results in red shift of GFP absorption and efficient bioluminescence energy transfer
    • Gorokhovatsky AY, Marchenkov VV, Rudenko NV, Ivashina TV, Ksenzenko VN, et al. (2004) Fusion of Aequorea victoria GFP and aequorin provides their Ca(2+)-induced interaction that results in red shift of GFP absorption and efficient bioluminescence energy transfer. Biochem Biophys Res Commun 320: 703-711.
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 703-711
    • Gorokhovatsky, A.Y.1    Marchenkov, V.V.2    Rudenko, N.V.3    Ivashina, T.V.4    Ksenzenko, V.N.5
  • 41
    • 72049085243 scopus 로고    scopus 로고
    • Autofluorescent proteins with excitation in the optical window for intravital imaging in mammals
    • Lin MZ, McKeown MR, Ng HL, Aguilera TA, Shaner NC, et al. (2009) Autofluorescent proteins with excitation in the optical window for intravital imaging in mammals. ChemBiol 16: 1169-1179.
    • (2009) ChemBiol , vol.16 , pp. 1169-1179
    • Lin, M.Z.1    McKeown, M.R.2    Ng, H.L.3    Aguilera, T.A.4    Shaner, N.C.5
  • 42
    • 0022425513 scopus 로고
    • Cloning and expression of the cDNA coding for aequorin, a bioluminescent calcium-binding protein
    • Prasher D, McCann RO, Cormier MJ, (1985) Cloning and expression of the cDNA coding for aequorin, a bioluminescent calcium-binding protein. BiochemBiophysResCommun 126: 1259-1268.
    • (1985) BiochemBiophysResCommun , vol.126 , pp. 1259-1268
    • Prasher, D.1    McCann, R.O.2    Cormier, M.J.3
  • 43
    • 0017334141 scopus 로고
    • Aequorin luminescence: relation of light emission to calcium concentration--a calcium-independent component
    • Allen DG, Blinks JR, Prendergast FG, (1977) Aequorin luminescence: relation of light emission to calcium concentration--a calcium-independent component. Science 195: 996-998.
    • (1977) Science , vol.195 , pp. 996-998
    • Allen, D.G.1    Blinks, J.R.2    Prendergast, F.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.