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Volumn 414, Issue , 2007, Pages 109-135

In vitro and in vivo apoptosis detection using membrane permeant fluorescent-labeled inhibitors of caspases

Author keywords

Apoptosis; Caspase; Cytotoxicity assay; Detection; FLICA; In vitro; In vivo; Tumor imaging

Indexed keywords

CASPASE; CYTOTOXIN; DIAGNOSTIC AGENT; FLUORESCENT DYE;

EID: 37849005392     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Article
Times cited : (25)

References (56)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J.F.R., Wyllie, A.H., and Currie, A.R. (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26, 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 2
    • 0019225636 scopus 로고
    • Cell death: The significance of apoptosis
    • Wyllie, A.H., Kerr, J.F.R., and Currie, A.R. (1981) Cell death: the significance of apoptosis. Int. Rev. Cytol. 68, 251-306.
    • (1981) Int. Rev. Cytol , vol.68 , pp. 251-306
    • Wyllie, A.H.1    Kerr, J.F.R.2    Currie, A.R.3
  • 3
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw, W.C., Martins, L.M., and Kaufmann, S.H. (1999) Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 68, 383-424.
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 4
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson, D.W. (1999) Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6, 1028-1042.
    • (1999) Cell Death Differ , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 5
    • 33748464621 scopus 로고    scopus 로고
    • Nature insight apoptosis
    • Heemels, M.T, ed
    • Heemels, M.T. (ed.) (2000) Nature insight apoptosis. Nature 407, 770-816.
    • (2000) Nature , vol.407 , pp. 770-816
  • 6
    • 0347601880 scopus 로고    scopus 로고
    • A decade of caspases
    • Degterev, A., Boyce, M., and Yuan, J. (2003) A decade of caspases. Oncogene 22, 8543-8567.
    • (2003) Oncogene , vol.22 , pp. 8543-8567
    • Degterev, A.1    Boyce, M.2    Yuan, J.3
  • 7
    • 16244362671 scopus 로고    scopus 로고
    • Apoptosis, pyroptosis, and necrosis: Mechanistic description of dead and dying eukaryotic cells
    • Fink, S.L. and Cookson, B.T. (2005) Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Infect. Immun. 73, 1907-1916.
    • (2005) Infect. Immun , vol.73 , pp. 1907-1916
    • Fink, S.L.1    Cookson, B.T.2
  • 8
    • 26444560960 scopus 로고    scopus 로고
    • Caspases: Pharmacological manipulation of cell death
    • Lavrik, I.N., Golks, A., and Krammer, P.H. (2005) Caspases: pharmacological manipulation of cell death. J. Clin. Invest. 115, 2665-2672.
    • (2005) J. Clin. Invest , vol.115 , pp. 2665-2672
    • Lavrik, I.N.1    Golks, A.2    Krammer, P.H.3
  • 9
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry, N.A. and Lazebnik, Y. (1998) Caspases: enemies within. Science 281, 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 10
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1ß processing in monocytes
    • Thornberry, N.A. et al. (1992) A novel heterodimeric cysteine protease is required for interleukin-1ß processing in monocytes. Nature 356, 768-774.
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1
  • 11
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B
    • Thornberry, N.A. et al. (1997) A combinatorial approach defines specificities of members of the caspase family and granzyme B. J. Biol. Chem. 272, 17907-17911.
    • (1997) J. Biol. Chem , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1
  • 12
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • Fuentes-Prior, P. and Salvesen, G.S. (2004) The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384, 201-232.
    • (2004) Biochem. J , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 13
    • 0030472889 scopus 로고    scopus 로고
    • Different interleukin-1ß converting enzyme (ICE) family protease requirements for the apoptotic death of T lymphocytes triggered by diverse stimuli
    • Sarin, A., Wu, M.L., and Henkart, P.A. (1996) Different interleukin-1ß converting enzyme (ICE) family protease requirements for the apoptotic death of T lymphocytes triggered by diverse stimuli. J. Exp. Med. 184, 2445-2450.
    • (1996) J. Exp. Med , vol.184 , pp. 2445-2450
    • Sarin, A.1    Wu, M.L.2    Henkart, P.A.3
  • 14
    • 8944230656 scopus 로고    scopus 로고
    • Fas-induced activation of the cell death-related protease CPP32 is inhibited by Bcl-2 and by ICE family protease inhibitors
    • Armstrong, R.C. et al. (1996) Fas-induced activation of the cell death-related protease CPP32 is inhibited by Bcl-2 and by ICE family protease inhibitors. J. Biol. Chem. 211, 16850-16855.
    • (1996) J. Biol. Chem , vol.211 , pp. 16850-16855
    • Armstrong, R.C.1
  • 16
    • 0033582526 scopus 로고    scopus 로고
    • Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis
    • Sun, X.M., MacFarlane, M., Zhuang, J., Wolf, B.B., Green, D.R., and Cohen, G.M. (1999) Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis. J. Biol. Chem. 274, 5053-5060.
    • (1999) J. Biol. Chem , vol.274 , pp. 5053-5060
    • Sun, X.M.1    MacFarlane, M.2    Zhuang, J.3    Wolf, B.B.4    Green, D.R.5    Cohen, G.M.6
  • 18
    • 0942265462 scopus 로고    scopus 로고
    • Rescue of defective branching nephrogenesis in renal coloboma syndrome by the caspase inhibitor, z-VAD-FMK
    • Clark, P., Dziarmaga, A., Eccles, M., and Goodyer, P. (2004) Rescue of defective branching nephrogenesis in renal coloboma syndrome by the caspase inhibitor, z-VAD-FMK. J. Am. Soc. Nephrol. 15, 299-305.
    • (2004) J. Am. Soc. Nephrol , vol.15 , pp. 299-305
    • Clark, P.1    Dziarmaga, A.2    Eccles, M.3    Goodyer, P.4
  • 19
    • 3242761599 scopus 로고    scopus 로고
    • Caspase-3 inhibitor prevents apoptosis of human islets immediately after isolation and improves islet graft function
    • Nakano, M. et al. (2004) Caspase-3 inhibitor prevents apoptosis of human islets immediately after isolation and improves islet graft function. Pancreas 29, 104-109.
    • (2004) Pancreas , vol.29 , pp. 104-109
    • Nakano, M.1
  • 20
    • 24644447930 scopus 로고    scopus 로고
    • Synthesis and evaluation of novel dipeptidyl benzoyloxymethyl ketones as caspase inhibitors
    • Nedev, H.N., Klaiman, G., LeBlanc, A., and Saragovi, H.U. (2005) Synthesis and evaluation of novel dipeptidyl benzoyloxymethyl ketones as caspase inhibitors. Biochem. Biophys. Res. Commun. 336, 397-400.
    • (2005) Biochem. Biophys. Res. Commun , vol.336 , pp. 397-400
    • Nedev, H.N.1    Klaiman, G.2    LeBlanc, A.3    Saragovi, H.U.4
  • 21
    • 0022856832 scopus 로고    scopus 로고
    • Rauber, P., Angliker, Walker, B., and Shaw, E. (1986) The synthesis of peptidylfluoromethanes and their properties as inhibitors of serine proteases and cysteine proteases. Biochem, J. 239, 633-640.
    • Rauber, P., Angliker, , Walker, B., and Shaw, E. (1986) The synthesis of peptidylfluoromethanes and their properties as inhibitors of serine proteases and cysteine proteases. Biochem, J. 239, 633-640.
  • 22
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • Powers, J.C., Asgian, J.L., Ekici, O.D., and James, K.E. (2002) Irreversible inhibitors of serine, cysteine, and threonine proteases. Chem. Rev. 102, 4639-4750.
    • (2002) Chem. Rev , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 23
    • 0032822084 scopus 로고    scopus 로고
    • Irreversible caspase inhibitors: Tools for studying apoptosis
    • Wu, J.C. and Fritz, L.C. (1999) Irreversible caspase inhibitors: tools for studying apoptosis. Methods 17, 320-328.
    • (1999) Methods , vol.17 , pp. 320-328
    • Wu, J.C.1    Fritz, L.C.2
  • 24
    • 0034714009 scopus 로고    scopus 로고
    • Activation of caspases measured in situ by binding of fluorochrome-labeled inhibitors of caspases (FLICA): Correlation with DNA fragmentation
    • Bedner, E., Smolewski, P., Amstad, P., and Darzynkiewicz, Z. (2000) Activation of caspases measured in situ by binding of fluorochrome-labeled inhibitors of caspases (FLICA): correlation with DNA fragmentation. Exp. Cell Res. 259, 308-313.
    • (2000) Exp. Cell Res , vol.259 , pp. 308-313
    • Bedner, E.1    Smolewski, P.2    Amstad, P.3    Darzynkiewicz, Z.4
  • 25
    • 0034850207 scopus 로고    scopus 로고
    • Detection of caspase activation in situ by fluorochrome-labeled caspase inhibitors
    • Amstad, P.A., Yu, G.L., Johnson, G.L., Lee, B.L., Dhawan, S., and Phelps, D.J. (2001) Detection of caspase activation in situ by fluorochrome-labeled caspase inhibitors. Biotechniques 31, 608-616.
    • (2001) Biotechniques , vol.31 , pp. 608-616
    • Amstad, P.A.1    Yu, G.L.2    Johnson, G.L.3    Lee, B.L.4    Dhawan, S.5    Phelps, D.J.6
  • 26
    • 0035340652 scopus 로고    scopus 로고
    • Detection of caspase activation by fluorochrome-labeled inhibitors: Multiparameter analysis by laser scanning cytometry
    • Smolewski, P., Bedner, E., Du, L., Hsieh, T.C., Wu, J.M., Phelps, D.J., and Darzynkiewicz, Z. (2001) Detection of caspase activation by fluorochrome-labeled inhibitors: multiparameter analysis by laser scanning cytometry. Cytometry 44, 73-82.
    • (2001) Cytometry , vol.44 , pp. 73-82
    • Smolewski, P.1    Bedner, E.2    Du, L.3    Hsieh, T.C.4    Wu, J.M.5    Phelps, D.J.6    Darzynkiewicz, Z.7
  • 27
    • 0036644212 scopus 로고    scopus 로고
    • Assay of caspase activation in situ combined with probing plasma membrane integrity to detect three distinct stages of apoptosis
    • Smolewski, P., Grabarek, J., Halicka, H.D., and Darzynkiewicz, Z. (2002) Assay of caspase activation in situ combined with probing plasma membrane integrity to detect three distinct stages of apoptosis. J. Immunol. Methods 265, 111-121.
    • (2002) J. Immunol. Methods , vol.265 , pp. 111-121
    • Smolewski, P.1    Grabarek, J.2    Halicka, H.D.3    Darzynkiewicz, Z.4
  • 28
    • 0036490576 scopus 로고    scopus 로고
    • Kinetics of HL-60 cell entry to apoptosis during treatment with TNF-a or camptothecin assayed by the stathmo-apoptosis method
    • Smolewski, P., Grabarek, J., Lee, B.W., Johnson, G.L., and Darzynkiewicz, Z. (2002) Kinetics of HL-60 cell entry to apoptosis during treatment with TNF-a or camptothecin assayed by the stathmo-apoptosis method. Cytometry 47, 143-149.
    • (2002) Cytometry , vol.47 , pp. 143-149
    • Smolewski, P.1    Grabarek, J.2    Lee, B.W.3    Johnson, G.L.4    Darzynkiewicz, Z.5
  • 29
    • 3242795805 scopus 로고    scopus 로고
    • Apoptotic cell death kinetics in vitro depend on the cell types and the inducers used
    • Wolbers, F., Buijtenhuljs, P., Haanen, C., and Vermes, I. (2004) Apoptotic cell death kinetics in vitro depend on the cell types and the inducers used. Apoptosis 9, 385-392.
    • (2004) Apoptosis , vol.9 , pp. 385-392
    • Wolbers, F.1    Buijtenhuljs, P.2    Haanen, C.3    Vermes, I.4
  • 30
    • 17444364399 scopus 로고    scopus 로고
    • Caspase activation in human spermatozoa in response to physiological and pathological stimuli
    • Grunewald, S., Paasch, U., Said, T.M., Sharma, R.K., Glander, H.J., and Agarwal, A. (2004) Caspase activation in human spermatozoa in response to physiological and pathological stimuli. Fertil. Steril. 83, 1106-1112.
    • (2004) Fertil. Steril , vol.83 , pp. 1106-1112
    • Grunewald, S.1    Paasch, U.2    Said, T.M.3    Sharma, R.K.4    Glander, H.J.5    Agarwal, A.6
  • 32
    • 0032773297 scopus 로고    scopus 로고
    • Imaging of caspase-3 activation in HeLa cells stimulated with etoposide using a novel fluorescent, probe
    • Mizukami, S., Kikuchi, K., Higuchi, T., Urano, Y., Mashima, T., Tsuruo, T., and Nagano, T. (1999) Imaging of caspase-3 activation in HeLa cells stimulated with etoposide using a novel fluorescent, probe. FEBS Lett. 453, 356-360.
    • (1999) FEBS Lett , vol.453 , pp. 356-360
    • Mizukami, S.1    Kikuchi, K.2    Higuchi, T.3    Urano, Y.4    Mashima, T.5    Tsuruo, T.6    Nagano, T.7
  • 33
    • 0344564126 scopus 로고    scopus 로고
    • Rhodamine 110-linked amino acids and peptides as substrates to measure caspase activity upon apoptosis induction in intact cells
    • Hug, H., Los, M., Hirt, W., and Debatin, K.M. (1999) Rhodamine 110-linked amino acids and peptides as substrates to measure caspase activity upon apoptosis induction in intact cells. Biochemistry 38, 13906-13911.
    • (1999) Biochemistry , vol.38 , pp. 13906-13911
    • Hug, H.1    Los, M.2    Hirt, W.3    Debatin, K.M.4
  • 34
    • 0343526894 scopus 로고    scopus 로고
    • Detection of caspase-activation in intact lymphoid cells using standard caspase substrates and inhibitors
    • Mack, A., Purinarm, C., and Hacker, G. (2000) Detection of caspase-activation in intact lymphoid cells using standard caspase substrates and inhibitors. J. Immunol. Methods 241, 19-31.
    • (2000) J. Immunol. Methods , vol.241 , pp. 19-31
    • Mack, A.1    Purinarm, C.2    Hacker, G.3
  • 35
    • 0034608386 scopus 로고    scopus 로고
    • Assessment of caspase activities in intact apoptotic thymocytes using cell-permeable fluorogenic substrates
    • Komoriya, A., Packard, B.Z., Brown, M.J., Wu, M.L., and Henkart, P.A. (2000) Assessment of caspase activities in intact apoptotic thymocytes using cell-permeable fluorogenic substrates. J. Exp. Med. 191, 1819-1828.
    • (2000) J. Exp. Med , vol.191 , pp. 1819-1828
    • Komoriya, A.1    Packard, B.Z.2    Brown, M.J.3    Wu, M.L.4    Henkart, P.A.5
  • 36
    • 33748701019 scopus 로고    scopus 로고
    • Detection of localized caspase activity in early apoptotic cells by laser scanning cytometry
    • Telford, W.G., Komoriya, A., and Packard, B.Z. (2002) Detection of localized caspase activity in early apoptotic cells by laser scanning cytometry. Cytometry 47, 81-88.
    • (2002) Cytometry , vol.47 , pp. 81-88
    • Telford, W.G.1    Komoriya, A.2    Packard, B.Z.3
  • 37
    • 0242610958 scopus 로고    scopus 로고
    • DEVDase detection in intact apoptotic cells using the cell permeant fluorogenic substrate, (z-DEVD)2-cresyl violet
    • Lee, B.W., Johnson, G.L., Hed, S.A., Darzynkiewicz, Z., Talhouk, J.W., and Mehrotra, S. (2003) DEVDase detection in intact apoptotic cells using the cell permeant fluorogenic substrate, (z-DEVD)2-cresyl violet. Biotechniques 35, 1080-1085.
    • (2003) Biotechniques , vol.35 , pp. 1080-1085
    • Lee, B.W.1    Johnson, G.L.2    Hed, S.A.3    Darzynkiewicz, Z.4    Talhouk, J.W.5    Mehrotra, S.6
  • 38
    • 0034660612 scopus 로고    scopus 로고
    • During apoptosis of HL-60 and U-937 cells caspases are activated independently of dissipation of mitochondrial electrochemical potential
    • Li, X., Du, L., and Darzynkiewicz, Z. (2000) During apoptosis of HL-60 and U-937 cells caspases are activated independently of dissipation of mitochondrial electrochemical potential. Exp. Cell Res. 257, 290-297.
    • (2000) Exp. Cell Res , vol.257 , pp. 290-297
    • Li, X.1    Du, L.2    Darzynkiewicz, Z.3
  • 39
    • 0037314551 scopus 로고    scopus 로고
    • Comparison of immunohistochemistry for activated caspase-3 and cleaved cytokeratin 18 with TUNEL method for quantification of apoptosis in histological sections of PC-3 subcutaneous xenografts
    • Duan, R.W., Garner, D.S., Williams, S.D., Funckes-Shippy, C.L., Spath, I.S., and Blomme, E.A. (2003) Comparison of immunohistochemistry for activated caspase-3 and cleaved cytokeratin 18 with TUNEL method for quantification of apoptosis in histological sections of PC-3 subcutaneous xenografts. J. Pathol. 199, 221-228.
    • (2003) J. Pathol , vol.199 , pp. 221-228
    • Duan, R.W.1    Garner, D.S.2    Williams, S.D.3    Funckes-Shippy, C.L.4    Spath, I.S.5    Blomme, E.A.6
  • 40
    • 0030612749 scopus 로고    scopus 로고
    • JC-1 but not DiOC6(3) or rhodamine 123, is a reliable fluorescent probe to assess delta psi changes in intact cells: Implications for studies on mitochondrial functionality during apoptosis
    • Salvioli, S., Ardizzoni, A., Franceschi, C., and Cossarizza, A. (1997) JC-1 but not DiOC6(3) or rhodamine 123, is a reliable fluorescent probe to assess delta psi changes in intact cells: implications for studies on mitochondrial functionality during apoptosis. FEBS Lett. 411, 77-82.
    • (1997) FEBS Lett , vol.411 , pp. 77-82
    • Salvioli, S.1    Ardizzoni, A.2    Franceschi, C.3    Cossarizza, A.4
  • 42
    • 0014251127 scopus 로고
    • Quantitative assay of the lytic action of immune lymphoid cells on 51-Cr-labeled allogenic target cells in vitro; inhibition by isoantibody and by drugs
    • Brunner, K.T., Mauel, J., Cerottini, J.C., and Chapuis, B. (1968) Quantitative assay of the lytic action of immune lymphoid cells on 51-Cr-labeled allogenic target cells in vitro; inhibition by isoantibody and by drugs. Immunology 14, 181-196.
    • (1968) Immunology , vol.14 , pp. 181-196
    • Brunner, K.T.1    Mauel, J.2    Cerottini, J.C.3    Chapuis, B.4
  • 43
    • 4444276508 scopus 로고    scopus 로고
    • HLA-C and HLA-E reduce antibody-dependent natural killer cell-mediated cytotoxicity of HIV-infected primary T cell blasts
    • Ward, P.W., Bonaparte, M.I., and Barker, E. (2004) HLA-C and HLA-E reduce antibody-dependent natural killer cell-mediated cytotoxicity of HIV-infected primary T cell blasts. AIDS 18, 1769-1779.
    • (2004) AIDS , vol.18 , pp. 1769-1779
    • Ward, P.W.1    Bonaparte, M.I.2    Barker, E.3
  • 44
    • 0038128194 scopus 로고    scopus 로고
    • Cutting edge: Rapid in vivo killing by memory CD8 T cells
    • Barber, D.L., Wherry, E.J., and Ahmed, R. (2003) Cutting edge: rapid in vivo killing by memory CD8 T cells. J. Immunol. 171, 27-31.
    • (2003) J. Immunol , vol.171 , pp. 27-31
    • Barber, D.L.1    Wherry, E.J.2    Ahmed, R.3
  • 45
    • 1642418522 scopus 로고    scopus 로고
    • Treatment of melanoma with 5-fluorouracil or dacarbazine in vitro sensitizes cells to antigen-specific CTL lysis through perforin/granzyme- and Fas-mediated pathways
    • Yang, S. and Haluska, F.G. (2004) Treatment of melanoma with 5-fluorouracil or dacarbazine in vitro sensitizes cells to antigen-specific CTL lysis through perforin/granzyme- and Fas-mediated pathways. J. Immunol. 172, 4599-4608.
    • (2004) J. Immunol , vol.172 , pp. 4599-4608
    • Yang, S.1    Haluska, F.G.2
  • 47
    • 0036217977 scopus 로고    scopus 로고
    • Lymphocyte-mediated cytotoxicity
    • Russell, J.H. and Ley, T.J. (2002) Lymphocyte-mediated cytotoxicity. Annu. Rev. Immunol. 20, 323-370.
    • (2002) Annu. Rev. Immunol , vol.20 , pp. 323-370
    • Russell, J.H.1    Ley, T.J.2
  • 48
    • 37849001296 scopus 로고    scopus 로고
    • Pross, H., Callewaert, D., and Rubin, P. (1986) Assays for NK cell cytotoxicity-their values and pitfalls, in Immunobiology of Natural Killer Cells (E. Lotzova and R.B. Herberman eds.) I. CRC Press, Boca Raton, FL, pp. 1-16.
    • Pross, H., Callewaert, D., and Rubin, P. (1986) Assays for NK cell cytotoxicity-their values and pitfalls, in Immunobiology of Natural Killer Cells (E. Lotzova and R.B. Herberman eds.) Vol, I. CRC Press, Boca Raton, FL, pp. 1-16.
  • 49
    • 0242636272 scopus 로고    scopus 로고
    • Measurement of CTL-induced cytotoxicity: The caspase 3 assay
    • Jerome, K.R., Sloan, D.D., and Aubert, M. (2003) Measurement of CTL-induced cytotoxicity: the caspase 3 assay. Apoptosis 8, 563-571.
    • (2003) Apoptosis , vol.8 , pp. 563-571
    • Jerome, K.R.1    Sloan, D.D.2    Aubert, M.3
  • 50
    • 0024477204 scopus 로고
    • Cell-mediated cytotoxicity: A highly sensitive and informative flow cytometric assay
    • Slezak, S.E. and Horan, P.K. (1989) Cell-mediated cytotoxicity: a highly sensitive and informative flow cytometric assay. J. Immunol. Methods 117, 205-214.
    • (1989) J. Immunol. Methods , vol.117 , pp. 205-214
    • Slezak, S.E.1    Horan, P.K.2
  • 51
    • 0025642387 scopus 로고
    • A simple and sensitive flow cytometric assay for the determination of the cytotoxic activity of human natural killer cells
    • Radosevic, K., Garritsen, H.S.P., Van Graft, M., De Grooth, B.G., and Greve, J. (1990) A simple and sensitive flow cytometric assay for the determination of the cytotoxic activity of human natural killer cells. J. Immunol. Methods 135, 81-89.
    • (1990) J. Immunol. Methods , vol.135 , pp. 81-89
    • Radosevic, K.1    Garritsen, H.S.P.2    Van Graft, M.3    De Grooth, B.G.4    Greve, J.5
  • 52
    • 0028241784 scopus 로고
    • Flow cytometric analysis of natural killer cell function as a clinical assay
    • Hatam, L., Schuval, S., and Bonagura, V.R. (1994) Flow cytometric analysis of natural killer cell function as a clinical assay. Cytometry 16, 59-68.
    • (1994) Cytometry , vol.16 , pp. 59-68
    • Hatam, L.1    Schuval, S.2    Bonagura, V.R.3
  • 54
    • 0037106009 scopus 로고    scopus 로고
    • A flow-cytometry based cytotoxicity assay using stained effector cells in combination with native target cells
    • Hoppner, M., Luhm, J., Schlenke, P., Koritke, P., and Frohn, C. (2002) A flow-cytometry based cytotoxicity assay using stained effector cells in combination with native target cells. J. Immunol. Methods 267, 157-163.
    • (2002) J. Immunol. Methods , vol.267 , pp. 157-163
    • Hoppner, M.1    Luhm, J.2    Schlenke, P.3    Koritke, P.4    Frohn, C.5
  • 55
    • 15244346296 scopus 로고    scopus 로고
    • γδ T-lymphocyte cytotoxic activity against Mycobacterium bovis analyzed by flow cytometry
    • Olin, M.R., Choi, K.H., Lee, J., and Molitor, T.W. (2005) γδ T-lymphocyte cytotoxic activity against Mycobacterium bovis analyzed by flow cytometry. J. Immunol. Methods 297, 1-11.
    • (2005) J. Immunol. Methods , vol.297 , pp. 1-11
    • Olin, M.R.1    Choi, K.H.2    Lee, J.3    Molitor, T.W.4
  • 56
    • 0037105972 scopus 로고    scopus 로고
    • The fluorolysis assay, a highly sensitive method for measuring the cytolytic activity of T cells at very low numbers
    • Kienzle, N., Oliver, S., Buttigieg, K., and Kelso, A. (2002) The fluorolysis assay, a highly sensitive method for measuring the cytolytic activity of T cells at very low numbers. J. Immunol. Methods 267, 98-108.
    • (2002) J. Immunol. Methods , vol.267 , pp. 98-108
    • Kienzle, N.1    Oliver, S.2    Buttigieg, K.3    Kelso, A.4


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