메뉴 건너뛰기




Volumn 7, Issue 4, 2002, Pages 555-560

Excitation ratiometric fluorescent biosensor for zinc ion at picomolar levels

Author keywords

Carbonic anhydrase; Fluorescence resonance energy transfer; Fluorescent indicator; FRET; Ratiometric; Zinc

Indexed keywords

APPROXIMATION THEORY; BIOMEDICAL ENGINEERING; ENERGY TRANSFER; FLUORESCENCE; MICROSCOPIC EXAMINATION; RESONANCE; ZINC;

EID: 0036816740     PISSN: 10833668     EISSN: None     Source Type: Journal    
DOI: 10.1117/1.1501886     Document Type: Article
Times cited : (36)

References (43)
  • 3
    • 0034306057 scopus 로고    scopus 로고
    • Zn(II): A novel ionic mediator of neural injury in brain disease
    • J.H. Weiss, S.L. Sensi, and J.-Y. Koh, "Zn(II): a novel ionic mediator of neural injury in brain disease," Trends Pharmacol. Sci. 21, 395-401 (2000).
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 395-401
    • Weiss, J.H.1    Sensi, S.L.2    Koh, J.-Y.3
  • 4
    • 0035696287 scopus 로고    scopus 로고
    • Synaptically released zinc: Physiological functions and pathological effects
    • C.J. Frederickson and A.I. Bush, "Synaptically released zinc: Physiological functions and pathological effects," BioMetals 14, 353-366 (2001).
    • (2001) BioMetals , vol.14 , pp. 353-366
    • Frederickson, C.J.1    Bush, A.I.2
  • 5
    • 0035887735 scopus 로고    scopus 로고
    • Induction of mossy fiber-CA3 long term potentiation requires translocation of synaptically released zinc
    • Y. Li, C.J. Hough, C.J. Frederickson, and J.M. Sarvey, "Induction of mossy fiber-CA3 long term potentiation requires translocation of synaptically released zinc," J. Neurosci. 21, 8015-8025 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 8015-8025
    • Li, Y.1    Hough, C.J.2    Frederickson, C.J.3    Sarvey, J.M.4
  • 6
    • 0030907004 scopus 로고    scopus 로고
    • A reappraisal of the role of zinc in life and death decisions of cells
    • P.J. Fraker and W.G. Telford, "A reappraisal of the role of zinc in life and death decisions of cells," Proc. Soc. Exp. Biol. Med. 215, 229-236 (1997).
    • (1997) Proc. Soc. Exp. Biol. Med. , vol.215 , pp. 229-236
    • Fraker, P.J.1    Telford, W.G.2
  • 7
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • B.L. Vallee and K.H. Falchuk, "The biochemical basis of zinc physiology," Physiol. Rev. 73, 79-118 (1993).
    • (1993) Physiol. Rev. , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 8
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • J.M. Berg and Y. Shi, "The galvanization of biology: a growing appreciation for the roles of zinc," Science 271, 1081-1085 (1996).
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 9
    • 0027501386 scopus 로고
    • Correlation of apoptosis with change in intracellular labile Zn(II) using Zinquin [(2-methyl-8-p-toluenesulphonamido-6-quinolyloxy)acetic acid], a new specific fluorescent probe for Zn(II)
    • P.D. Zalewski, I.J. Forbes, and W.H. Betts, "Correlation of apoptosis with change in intracellular labile Zn(II) using Zinquin [(2-methyl-8-p-toluenesulphonamido-6-quinolyloxy)acetic acid], a new specific fluorescent probe for Zn(II)," Biochem. J. 296, 403-408 (1993).
    • (1993) Biochem. J. , vol.296 , pp. 403-408
    • Zalewski, P.D.1    Forbes, I.J.2    Betts, W.H.3
  • 10
    • 0021895138 scopus 로고
    • A new generation of calcium indicators with greatly improved fluorescence properties
    • G. Grynkiewicz, M. Poenie, and R.Y. Tsien, "A new generation of calcium indicators with greatly improved fluorescence properties," J. Biol. Chem. 260, 3440-3450 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 11
    • 0023214741 scopus 로고
    • A quinoline fluorescence method for visualizing and assaying histochemicaily reactive zinc (bouton zinc) in the brain
    • C.J. Frederickson, E.J. Kasarskis, D. Ringo, and R.E. Frederickson, "A quinoline fluorescence method for visualizing and assaying histochemicaily reactive zinc (bouton zinc) in the brain," J. Neurosci. Methods 20, 91-103 (1987).
    • (1987) J. Neurosci. Methods , vol.20 , pp. 91-103
    • Frederickson, C.J.1    Kasarskis, E.J.2    Ringo, D.3    Frederickson, R.E.4
  • 12
    • 0031009848 scopus 로고    scopus 로고
    • Imaging free zinc in synaptic terminals in live hippocampal slices
    • T. Budde, A. Minta, J.A. White, and A.R. Kay, "Imaging free zinc in synaptic terminals in live hippocampal slices," Neuroscience 79, 347-358 (1997).
    • (1997) Neuroscience , vol.79 , pp. 347-358
    • Budde, T.1    Minta, A.2    White, J.A.3    Kay, A.R.4
  • 13
    • 0034808118 scopus 로고    scopus 로고
    • Fluorescent sensors for Zn2+ based on a fluorescein platform: Synthesis, properties, and intracellular distribution
    • S.C. Burdette, G.K. Walkup, B. Spingler, R.Y. Tsien, and S.J. Lippard, "Fluorescent Sensors for Zn2+ based on a fluorescein platform: synthesis, properties, and intracellular distribution," J. Am. Chem. Soc. 123, 7831-7841 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7831-7841
    • Burdette, S.C.1    Walkup, G.K.2    Spingler, B.3    Tsien, R.Y.4    Lippard, S.J.5
  • 15
    • 0034677695 scopus 로고    scopus 로고
    • Novel zinc fluorescent probes excitable with visible light for biological applications
    • T. Hirano, K. Kikuchi, Y. Urano, T. Higuchi, and T. Nagano, "Novel zinc fluorescent probes excitable with visible light for biological applications," Angew. Chem. Int. Ed. Engl. 39, 1052-1054 (2000).
    • (2000) Angew. Chem. Int. Ed. Engl. , vol.39 , pp. 1052-1054
    • Hirano, T.1    Kikuchi, K.2    Urano, Y.3    Higuchi, T.4    Nagano, T.5
  • 16
    • 0035693720 scopus 로고    scopus 로고
    • Chemistry of zinc(II) fluorophore sensors
    • E. Kimura and S. Aoki, "Chemistry of zinc(II) fluorophore sensors," BioMetals 14, 191-204 (2001).
    • (2001) BioMetals , vol.14 , pp. 191-204
    • Kimura, E.1    Aoki, S.2
  • 17
    • 0030746608 scopus 로고    scopus 로고
    • High-affinity zinc inhibition of NMDA NR1-NR2A receptors
    • P. Paoletti, P. Ascher, and J. Neyton, "High-affinity zinc inhibition of NMDA NR1-NR2A receptors," J. Neurosci. 17, 5711-5725 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 5711-5725
    • Paoletti, P.1    Ascher, P.2    Neyton, J.3
  • 18
    • 0029971595 scopus 로고    scopus 로고
    • Zinc transport in mammalian cells
    • J.G. Reyes, "Zinc transport in mammalian cells," Am. J. Physiol. 270, C401-410 (1996).
    • (1996) Am. J. Physiol. , vol.270
    • Reyes, J.G.1
  • 19
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • C.E. Outten and T.V. O'Halloran, "Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis," Science 292, 2488-2492 (2001).
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 20
    • 0035657358 scopus 로고    scopus 로고
    • Rapid translocation of Zn2+ from presynaptic terminals into postsynaptic hippocampal neurons after physiological stimulation
    • Y. Li, C. Hough, S.W. Suh, J.M. Sarvey, and C.J. Frederickson, "Rapid translocation of Zn2+ from presynaptic terminals into postsynaptic hippocampal neurons after physiological stimulation," J. Neurophysiol. 86, 2597-2604 (2001).
    • (2001) J. Neurophysiol. , vol.86 , pp. 2597-2604
    • Li, Y.1    Hough, C.2    Suh, S.W.3    Sarvey, J.M.4    Frederickson, C.J.5
  • 21
    • 0000750473 scopus 로고
    • Metal-binding properties of human erythrocyte carbonic anhydrases
    • S. Lindskog and P.O. Nyman, "Metal-binding properties of human erythrocyte carbonic anhydrases," Biochim. Biophys. Acta 85, 462-474 (1964).
    • (1964) Biochim. Biophys. Acta , vol.85 , pp. 462-474
    • Lindskog, S.1    Nyman, P.O.2
  • 22
    • 0033551442 scopus 로고    scopus 로고
    • Metal binding specificity in carbonic anhydrase is influenced by conserved hydrophobic amino acids
    • J.A. Hunt, M. Ahmed, and C.A. Fierke, "Metal binding specificity in carbonic anhydrase is influenced by conserved hydrophobic amino acids," Biochemistry 38, 9054-9060 (1999).
    • (1999) Biochemistry , vol.38 , pp. 9054-9060
    • Hunt, J.A.1    Ahmed, M.2    Fierke, C.A.3
  • 23
    • 0035693721 scopus 로고    scopus 로고
    • Fluorescence-based biosensing of zinc using carbonic anhydrase
    • C.A. Fierke and R.B. Thompson, "Fluorescence-based biosensing of zinc using carbonic anhydrase," BioMetals 14, 205-222 (2001).
    • (2001) BioMetals , vol.14 , pp. 205-222
    • Fierke, C.A.1    Thompson, R.B.2
  • 25
    • 0034002451 scopus 로고    scopus 로고
    • Fluorescence microscopy of stimulated Zn(II) release from organotypic cultures of mammalian hippocampus using a carbonic anhydrase-based biosensor system
    • R.B. Thompson, W.O. Whetsell, Jr., B.P. Maliwal, C.A. Fierke, and C.J. Frederickson, "Fluorescence microscopy of stimulated Zn(II) release from organotypic cultures of mammalian hippocampus using a carbonic anhydrase-based biosensor system," J. Neurosci. Methods 96, 35-45 (2000).
    • (2000) J. Neurosci. Methods , vol.96 , pp. 35-45
    • Thompson, R.B.1    Whetsell W.O., Jr.2    Maliwal, B.P.3    Fierke, C.A.4    Frederickson, C.J.5
  • 28
    • 0001356438 scopus 로고
    • Enzyme-based fiber optic zinc biosensor
    • R.B. Thompson and E.R. Jones, "Enzyme-based fiber optic zinc biosensor," Anal. Chem. 65, 730-734 (1993).
    • (1993) Anal. Chem. , vol.65 , pp. 730-734
    • Thompson, R.B.1    Jones, E.R.2
  • 29
    • 0029790057 scopus 로고    scopus 로고
    • Structure-based design of a sulfonamide probe for fluorescence anisotropy detection of zinc with a carbonic anhydrase-based biosensor
    • D. Elbaum, S.K. Nair, M.W. Patchan, R.B. Thompson, and D.W. Christianson, "Structure-based design of a sulfonamide probe for fluorescence anisotropy detection of zinc with a carbonic anhydrase-based biosensor," J. Am. Chem. Soc. 118, 8381-8387 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8381-8387
    • Elbaum, D.1    Nair, S.K.2    Patchan, M.W.3    Thompson, R.B.4    Christianson, D.W.5
  • 30
    • 0001606250 scopus 로고    scopus 로고
    • Expanded dynamic range of free zinc ion determination by fluorescence anisotropy
    • R.B. Thompson, B.P. Maliwal, and C.A. Fierke, "Expanded dynamic range of free zinc ion determination by fluorescence anisotropy," Anal. Chem. 70, 1749-1754 (1998).
    • (1998) Anal. Chem. , vol.70 , pp. 1749-1754
    • Thompson, R.B.1    Maliwal, B.P.2    Fierke, C.A.3
  • 31
    • 0033624438 scopus 로고    scopus 로고
    • Zinc biosensing with multiphoton excitation using carbonic anhydrase and improved fluorophores
    • R.B. Thompson, B.P. Maliwal, and H.H. Zeng, "Zinc biosensing with multiphoton excitation using carbonic anhydrase and improved fluorophores," J. Biomed. Opt. 5, 17-22 (2000).
    • (2000) J. Biomed. Opt. , vol.5 , pp. 17-22
    • Thompson, R.B.1    Maliwal, B.P.2    Zeng, H.H.3
  • 32
    • 0011993640 scopus 로고
    • Time-resolved fluorescence lifetime imaging
    • B. Herman and J.J. Lemasters, Eds., Academic, New York
    • M. vandeVen and E. Gratton, "Time-resolved fluorescence lifetime imaging," in Optical Microscopy: Emerging Methods and Applications, B. Herman and J.J. Lemasters, Eds., pp. 373-402, Academic, New York (1993).
    • (1993) Optical Microscopy: Emerging Methods and Applications , pp. 373-402
    • VandeVen, M.1    Gratton, E.2
  • 33
    • 0028673388 scopus 로고
    • Fluorescence lifetime imaging microscopy: Homodyne technique using high-speed gated image intensifier
    • M.L. Johnson and L. Brand, Eds., Academic, New York
    • H. Szmacinski, J.R. Lakowicz, and M.L. Johnson, "Fluorescence lifetime imaging microscopy: homodyne technique using high-speed gated image intensifier," in Numerical Computer Methods, Methods in Enzymology, M.L. Johnson and L. Brand, Eds., pp. 723-748, Academic, New York (1994).
    • (1994) Numerical Computer Methods, Methods in Enzymology , pp. 723-748
    • Szmacinski, H.1    Lakowicz, J.R.2    Johnson, M.L.3
  • 36
    • 0025174178 scopus 로고
    • Cell membrane fluidity in the intact kidney proximal tubule measured by orientation-independent fluorescence anisotropy imaging
    • K. Fushimi, J.A. Dix, and A.S. Verkman, "Cell membrane fluidity in the intact kidney proximal tubule measured by orientation-independent fluorescence anisotropy imaging," Biophys. J. 57, 241-254 (1990).
    • (1990) Biophys. J. , vol.57 , pp. 241-254
    • Fushimi, K.1    Dix, J.A.2    Verkman, A.S.3
  • 37
    • 84981779372 scopus 로고
    • Intermolecular energy migration and fluorescence (Ger.)
    • T. Forster, "Intermolecular energy migration and fluorescence (Ger.)," Ann. Phys. (Leipzig) 2, 55-75 (1948).
    • (1948) Ann. Phys. (Leipzig) , vol.2 , pp. 55-75
    • Forster, T.1
  • 38
    • 0000057588 scopus 로고    scopus 로고
    • Performance enhancement of fluorescence energy transfer-based biosensors by site-directed mutagenesis of the transducer
    • R.B. Thompson, Z. Ge, M.W. Patchan, and C.A. Fierke, "Performance enhancement of fluorescence energy transfer-based biosensors by site-directed mutagenesis of the transducer," J. Biomed. Opt. 1, 131-137 (1996).
    • (1996) J. Biomed. Opt. , vol.1 , pp. 131-137
    • Thompson, R.B.1    Ge, Z.2    Patchan, M.W.3    Fierke, C.A.4
  • 39
    • 0027439522 scopus 로고
    • Determinants of catalytic activity and stability of carbonic anhydrase II as revealed by random mutagenesis
    • J.E Krebs and C.A. Fierke, "Determinants of catalytic activity and stability of carbonic anhydrase II as revealed by random mutagenesis," J. Biol. Chem. 268, 948-954 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 948-954
    • Krebs, J.E.1    Fierke, C.A.2
  • 40
    • 0017393793 scopus 로고
    • A rapid and convenient preparation of apocarbonic anhydrase
    • J.B. Hunt, M.J. Rhee, and C.B. Storm, "A rapid and convenient preparation of apocarbonic anhydrase," Anal. Biochem. 79, 614-617 (1977).
    • (1977) Anal. Biochem. , vol.79 , pp. 614-617
    • Hunt, J.B.1    Rhee, M.J.2    Storm, C.B.3
  • 41
    • 0030050546 scopus 로고    scopus 로고
    • Unexpected binding mode of the sulfonamide fluorophore 5-dimethylamino-1-naphthalene sulfonamide to human carbonic anhydrase II: Implications for the development of a zinc biosensor
    • S.K. Nair, D. Elbaum, and D.W. Christianson, "Unexpected binding mode of the sulfonamide fluorophore 5-dimethylamino-1-naphthalene sulfonamide to human carbonic anhydrase II: Implications for the development of a zinc biosensor," J. Biol. Chem. 271, 1003-1007 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 1003-1007
    • Nair, S.K.1    Elbaum, D.2    Christianson, D.W.3
  • 42
    • 0030843294 scopus 로고    scopus 로고
    • Selection of carbonic anhydrase variants displayed on phage: Aromatic residues in zinc binding site enhance metal affinity and equilibration kinetics
    • J.A. Hunt and C.A. Fierke, "Selection of carbonic anhydrase variants displayed on phage: aromatic residues in zinc binding site enhance metal affinity and equilibration kinetics," J. Biol. Chem. 272, 20364-20372 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 20364-20372
    • Hunt, J.A.1    Fierke, C.A.2
  • 43
    • 0033231311 scopus 로고    scopus 로고
    • Optical nanosensors for chemical analysis inside single living cells. 1. Fabrication, characterization, and methods for intracellular delivery of PEBBLE sensors
    • H.A. Clark, M. Hoyer, M.A. Philbert, and R. Kopelman, "Optical nanosensors for chemical analysis inside single living cells. 1. Fabrication, characterization, and methods for intracellular delivery of PEBBLE sensors," Anal. Chem. 71, 4831-4836 (1999).
    • (1999) Anal. Chem. , vol.71 , pp. 4831-4836
    • Clark, H.A.1    Hoyer, M.2    Philbert, M.A.3    Kopelman, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.