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Volumn 319, Issue 2, 2003, Pages 234-238

Synthesis and evaluation of fluorescent probes for the detection of calpain activity

Author keywords

Calpain I; Fluorescence; FRET; Proteolytic activity

Indexed keywords

CHROMOPHORES; ENERGY TRANSFER; FLUORESCENCE; FORSTER RESONANCE ENERGY TRANSFER; SUBSTRATES;

EID: 0038505787     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-2697(03)00324-5     Document Type: Article
Times cited : (47)

References (25)
  • 1
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system - Structure, function, and regulation
    • Croall D.E., Demartino G.N. Calcium-activated neutral protease (calpain) system - structure, function, and regulation. Physiol. Rev. 71:1991;813-847.
    • (1991) Physiol. Rev. , vol.71 , pp. 813-847
    • Croall, D.E.1    Demartino, G.N.2
  • 2
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: A potential molecular basis for neuronal degeneration
    • Saito K., Elce J., Hamos J., Nixon R. Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Proc. Natl. Acad. Sci. USA. 90:1993;2628-2632.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2628-2632
    • Saito, K.1    Elce, J.2    Hamos, J.3    Nixon, R.4
  • 3
    • 0031568260 scopus 로고    scopus 로고
    • A continuous method for measuring calpain activity
    • Jiang S.T., Wang J.H., Chang T., Chen C.S. A continuous method for measuring calpain activity. Anal. Biochem. 244:1997;233-238.
    • (1997) Anal. Biochem. , vol.244 , pp. 233-238
    • Jiang, S.T.1    Wang, J.H.2    Chang, T.3    Chen, C.S.4
  • 5
    • 0034653992 scopus 로고    scopus 로고
    • A BODIPY fluorescent microplate assay for measuring activity of calpains and other proteases
    • Thompson V.F., Saldana S., Cong J.Y., Goll D.E. A BODIPY fluorescent microplate assay for measuring activity of calpains and other proteases. Anal. Biochem. 279:2000;170-178.
    • (2000) Anal. Biochem. , vol.279 , pp. 170-178
    • Thompson, V.F.1    Saldana, S.2    Cong, J.Y.3    Goll, D.E.4
  • 6
  • 7
    • 84986466988 scopus 로고
    • Improved calpain assay using fluorescein isothiocyanate-labeled casein
    • Lonergan S.M., Johnson M.H., Calkins C.R. Improved calpain assay using fluorescein isothiocyanate-labeled casein. J. Food Sci. 60:1995;72-73.
    • (1995) J. Food Sci. , vol.60 , pp. 72-73
    • Lonergan, S.M.1    Johnson, M.H.2    Calkins, C.R.3
  • 8
    • 0032971239 scopus 로고    scopus 로고
    • Calpain activation and inhibition in organotypic rat hippocampal slice cultures deprived of oxygen and glucose
    • Brana C., Benham C.D., Sundstrom L.E. Calpain activation and inhibition in organotypic rat hippocampal slice cultures deprived of oxygen and glucose. Eur. J. Neurosci. 11:1999;2375-2384.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 2375-2384
    • Brana, C.1    Benham, C.D.2    Sundstrom, L.E.3
  • 10
    • 0025770925 scopus 로고
    • Anthranilamide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases - Multicolumn peptide-synthesis of enzyme substrates for subtilisin carlsberg and pepsin
    • Meldal M., Breddam K. Anthranilamide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases - multicolumn peptide-synthesis of enzyme substrates for subtilisin carlsberg and pepsin. Anal. Biochem. 195:1991;141-147.
    • (1991) Anal. Biochem. , vol.195 , pp. 141-147
    • Meldal, M.1    Breddam, K.2
  • 11
    • 0028264809 scopus 로고
    • Portion-mixing peptide libraries of quenched fluorogenic substrates for complete subsite mapping of endoprotease specificity
    • Meldal M., Svendsen I., Breddam K., Auzanneau F.I. Portion-mixing peptide libraries of quenched fluorogenic substrates for complete subsite mapping of endoprotease specificity. Proc. Natl. Acad. Sci. USA. 91:1994;3314-3318.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3314-3318
    • Meldal, M.1    Svendsen, I.2    Breddam, K.3    Auzanneau, F.I.4
  • 12
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
    • Stennicke H.R., Renatus M., Meldal M., Salvesen G.S. Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem. J. 350:2000;563-568.
    • (2000) Biochem. J. , vol.350 , pp. 563-568
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 13
    • 0018388950 scopus 로고
    • Intramolecularly quenched fluorogenic substrates for hydrolytic enzymes
    • Yaron A., Carmel A., Katchalski-Katzir E. Intramolecularly quenched fluorogenic substrates for hydrolytic enzymes. Anal. Biochem. 95:1979;228-235.
    • (1979) Anal. Biochem. , vol.95 , pp. 228-235
    • Yaron, A.1    Carmel, A.2    Katchalski-Katzir, E.3
  • 14
    • 0028282502 scopus 로고
    • Immunolocalization of calpain I-mediated spectrin degradation to vulnerable neurons in the ischemic gerbil brain
    • Roberts-Lewis J.M., Savage M.J., Marcy V.R., Pinsker L.R., Siman R. Immunolocalization of calpain I-mediated spectrin degradation to vulnerable neurons in the ischemic gerbil brain. J. Neurosci. 14:1994;3934-3944.
    • (1994) J. Neurosci. , vol.14 , pp. 3934-3944
    • Roberts-Lewis, J.M.1    Savage, M.J.2    Marcy, V.R.3    Pinsker, L.R.4    Siman, R.5
  • 15
    • 0029100373 scopus 로고
    • Translational suppression of calpain-I reduces NMDA-induced spectrin proteolysis and pathophysiology in cultured hippocampal slices
    • Bednarski E., Vanderklish P., Gall C., Saido T.C., Bahr B.A., Lynch G. Translational suppression of calpain-I reduces NMDA-induced spectrin proteolysis and pathophysiology in cultured hippocampal slices. Brain Res. 694:1995;147-157.
    • (1995) Brain Res. , vol.694 , pp. 147-157
    • Bednarski, E.1    Vanderklish, P.2    Gall, C.3    Saido, T.C.4    Bahr, B.A.5    Lynch, G.6
  • 17
    • 0034524665 scopus 로고    scopus 로고
    • The pathogenic activation of calpain: A marker and mediator of cellular toxicity and disease states
    • Vanderklish P.W., Bahr B.A. The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states. Int. J. Exp. Pathol. 81:2000;323-339.
    • (2000) Int. J. Exp. Pathol. , vol.81 , pp. 323-339
    • Vanderklish, P.W.1    Bahr, B.A.2
  • 18
    • 0034130546 scopus 로고    scopus 로고
    • Synthesis of dye-labeled lysine derivatives
    • Shen Z.X., Zhang Y.W., Chen Y. Synthesis of dye-labeled lysine derivatives. Synth. Commun. 30:2000;2525-2532.
    • (2000) Synth. Commun. , vol.30 , pp. 2525-2532
    • Shen, Z.X.1    Zhang, Y.W.2    Chen, Y.3
  • 19
    • 0034426594 scopus 로고    scopus 로고
    • Fluorescent indicators of peptide cleavage in the trafficking compartments of living cells: Peptides site-specifically labeled with two dyes
    • Bark S.J., Hahn K.M. Fluorescent indicators of peptide cleavage in the trafficking compartments of living cells: peptides site-specifically labeled with two dyes. Methods. 20:2000;429-435.
    • (2000) Methods , vol.20 , pp. 429-435
    • Bark, S.J.1    Hahn, K.M.2
  • 20
    • 0025232814 scopus 로고
    • Solid-phase peptide-synthesis utilizing 9-fluorenylmethoxycarbonyl amino-acids
    • Fields G.B., Noble R.L. Solid-phase peptide-synthesis utilizing 9-fluorenylmethoxycarbonyl amino-acids. Int. J. Pept. Protein Res. 35:1990;161-214.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 21
    • 0019627519 scopus 로고
    • Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction
    • Sarin V.K., Kent S.B.H., Tam J.P., Merrifield R.B. Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction. Anal. Biochem. 117:1981;147-157.
    • (1981) Anal. Biochem. , vol.117 , pp. 147-157
    • Sarin, V.K.1    Kent, S.B.H.2    Tam, J.P.3    Merrifield, R.B.4
  • 22
    • 84981779372 scopus 로고
    • Intermolecular energy transference and fluorescence
    • Forster T. Intermolecular energy transference and fluorescence. Ann. Physik. 2:1948;55-75.
    • (1948) Ann. Physik , vol.2 , pp. 55-75
    • Forster, T.1
  • 23
    • 0026503894 scopus 로고
    • New intramolecularly quenched fluorogenic peptide-substrates for the study of the kinetic specificity of papain
    • Garciaecheverria C., Rich D.H. New intramolecularly quenched fluorogenic peptide-substrates for the study of the kinetic specificity of papain. FEBS Lett. 297:1992;100-102.
    • (1992) FEBS Lett. , vol.297 , pp. 100-102
    • Garciaecheverria, C.1    Rich, D.H.2
  • 24
    • 0025099455 scopus 로고
    • Novel fluorogenic substrates for assaying retroviral proteases by resonance energy-transfer
    • Matayoshi E.D., Wang G.T., Krafft G.A., Erickson J. Novel fluorogenic substrates for assaying retroviral proteases by resonance energy-transfer. Science. 247:1990;954-958.
    • (1990) Science , vol.247 , pp. 954-958
    • Matayoshi, E.D.1    Wang, G.T.2    Krafft, G.A.3    Erickson, J.4
  • 25
    • 0021683468 scopus 로고
    • Comparative specificity and kinetic-studies on porcine calpain-I and calpain-II with naturally-occurring peptides and synthetic fluorogenic substrates
    • Sasaki T., Kikuchi T., Yumoto N., Yoshimura N., Murachi T. Comparative specificity and kinetic-studies on porcine calpain-I and calpain-II with naturally-occurring peptides and synthetic fluorogenic substrates. J. Biol. Chem. 259:1984;2489-2494.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2489-2494
    • Sasaki, T.1    Kikuchi, T.2    Yumoto, N.3    Yoshimura, N.4    Murachi, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.