메뉴 건너뛰기




Volumn 10, Issue 5, 2003, Pages 548-557

Apoptosis induced by Na+/H+ antiport inhibition activates the LEI/L-DNase II pathway

Author keywords

Amiloride; Apoptosis; Caspase independent pathway; Dnase II; Serpin

Indexed keywords

AMILORIDE DERIVATIVE; CYCLOHEXANE DERIVATIVE; DEOXYRIBONUCLEASE II; ETOPOSIDE; LEUKOCYTE ELASTASE; SODIUM PROTON EXCHANGE PROTEIN;

EID: 0038823547     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401195     Document Type: Article
Times cited : (46)

References (71)
  • 1
    • 0028891783 scopus 로고
    • Apoptosis, oncosis, and necrosis. An overview of cell death
    • Majno G and Joris I (1995) Apoptosis, oncosis, and necrosis. An overview of cell death. Am. J. Pathol. 146: 3-15
    • (1995) Am. J. Pathol. , vol.146 , pp. 3-15
    • Majno, G.1    Joris, I.2
  • 2
    • 0028242351 scopus 로고
    • A calcium-dependent nuclease from apoptotic rat thymocytes is homologous with cyclophilin. Recombinant cyclophilins A, B, and C have nuclease activity
    • Montague JW, Gaido ML, Frye C and Cidlowski JA (1994) A calcium-dependent nuclease from apoptotic rat thymocytes is homologous with cyclophilin. Recombinant cyclophilins A, B, and C have nuclease activity. J. Biol. Chem. 269: 18877-18880
    • (1994) J. Biol. Chem. , vol.269 , pp. 18877-18880
    • Montague, J.W.1    Gaido, M.L.2    Frye, C.3    Cidlowski, J.A.4
  • 3
    • 0027458695 scopus 로고
    • Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death)
    • Peitsch MC, Polzar B, Stephan H, Crompton T, MacDonald HR, Mannherz HG and Tschopp J (1993) Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death). EMBO J. 12: 371-377
    • (1993) EMBO J. , vol.12 , pp. 371-377
    • Peitsch, M.C.1    Polzar, B.2    Stephan, H.3    Crompton, T.4    MacDonald, H.R.5    Mannherz, H.G.6    Tschopp, J.7
  • 4
    • 0032526193 scopus 로고    scopus 로고
    • Molecular cloning and expression of a cDNA encoding an apoptotic endonuclease DNase gamma
    • Shiokawa D and Tanuma S (1998) Molecular cloning and expression of a cDNA encoding an apoptotic endonuclease DNase gamma. Biochem. J. 332: 713-720
    • (1998) Biochem. J. , vol.332 , pp. 713-720
    • Shiokawa, D.1    Tanuma, S.2
  • 5
    • 0031046748 scopus 로고    scopus 로고
    • Identification of a novel 97 kDa endonuclease capable of internucleosomal DNA cleavage
    • Pandey S, Walker PR and Sikorska M (1997) Identification of a novel 97 kDa endonuclease capable of internucleosomal DNA cleavage. Biochemistry 36: 711-720
    • (1997) Biochemistry , vol.36 , pp. 711-720
    • Pandey, S.1    Walker, P.R.2    Sikorska, M.3
  • 6
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A and Nagata S (1998) A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391: 43-50
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 7
    • 0027164993 scopus 로고
    • Identification of deoxyribonuclease II as an endonuclease involved in apoptosis
    • Barry MA and Eastman A (1993) Identification of deoxyribonuclease II as an endonuclease involved in apoptosis. Arch. Biochem. Biophys. 300: 440-450
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 440-450
    • Barry, M.A.1    Eastman, A.2
  • 8
    • 0029133608 scopus 로고
    • The acid deoxyribonuclease of neutrophils: A possible participant in apoptosis-associated genome destruction
    • Gottlieb RA, Giesing HA, Engler RL and Babior BM (1995) The acid deoxyribonuclease of neutrophils: a possible participant in apoptosis-associated genome destruction. Blood 86: 2414-2418
    • (1995) Blood , vol.86 , pp. 2414-2418
    • Gottlieb, R.A.1    Giesing, H.A.2    Engler, R.L.3    Babior, B.M.4
  • 12
    • 0034627773 scopus 로고    scopus 로고
    • Nuclear translocation of a leukocyte elastase inhibitor/elastase complex during staurosporine-induced apoptosis: Role in the generation of nuclear L-DNase II activity
    • Belmokhtar CA, Torriglia A, Counis MF, Courtois Y, Jacquemin-Sablon A and Segal-Bendirdjian E (2000) Nuclear translocation of a leukocyte elastase inhibitor/elastase complex during staurosporine-induced apoptosis: role in the generation of nuclear L-DNase II activity. Exp. Cell Res. 254: 99-109
    • (2000) Exp. Cell Res. , vol.254 , pp. 99-109
    • Belmokhtar, C.A.1    Torriglia, A.2    Counis, M.F.3    Courtois, Y.4    Jacquemin-Sablon, A.5    Segal-Bendirdjian, E.6
  • 15
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist M and Jaattela M (2001) Four deaths and a funeral: from caspases to alternative mechanisms. Nat. Rev. Mol. Cell Biol. 2: 589-598
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 16
    • 0031813791 scopus 로고    scopus 로고
    • L-DNase II, a molecule that links proteases and endonucleases in apoptosis, derives from the ubiquitous serpin leukocyte elastase inhibitor
    • Torriglia A, Perani P, Brossas JY, Chaudun E, Treton J, Courtois Y and Counis MF (1998) L-DNase II, a molecule that links proteases and endonucleases in apoptosis, derives from the ubiquitous serpin leukocyte elastase inhibitor. Mol. Cell Biol. 18: 3612-3619
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3612-3619
    • Torriglia, A.1    Perani, P.2    Brossas, J.Y.3    Chaudun, E.4    Treton, J.5    Courtois, Y.6    Counis, M.F.7
  • 17
    • 0033026169 scopus 로고    scopus 로고
    • Regulation of pro-apoptotic leucocyte granule serine proteinases by intracellular serpins
    • Bird PI (1999) Regulation of pro-apoptotic leucocyte granule serine proteinases by intracellular serpins. Immunol. Cell Biol. 77: 47-57
    • (1999) Immunol. Cell Biol. , vol.77 , pp. 47-57
    • Bird, P.I.1
  • 18
    • 0035049240 scopus 로고    scopus 로고
    • Endogenous angiogenesis inhibitors and their therapeutic implications
    • Cao Y (2001) Endogenous angiogenesis inhibitors and their therapeutic implications. Int. J. Biochem. Cell Biol. 33: 357-369
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 357-369
    • Cao, Y.1
  • 19
    • 0029022365 scopus 로고
    • Involvement of an ICE-like protease in Fas-mediated apoptosis
    • Enari M, Hug H and Nagata S (1995) Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature 375: 78-81
    • (1995) Nature , vol.375 , pp. 78-81
    • Enari, M.1    Hug, H.2    Nagata, S.3
  • 20
    • 0030985808 scopus 로고    scopus 로고
    • Intracellular acidification induces apoptosis by stimulating ICE-like protease activity
    • Furlong IJ, Ascaso R, Lopez Rivas A and Collins MK (1997) Intracellular acidification induces apoptosis by stimulating ICE-like protease activity. J. Cell Sci. 110: 653-661
    • (1997) J. Cell Sci. , vol.110 , pp. 653-661
    • Furlong, I.J.1    Ascaso, R.2    Lopez Rivas, A.3    Collins, M.K.4
  • 21
    • 0031792776 scopus 로고    scopus 로고
    • Selective regulation of apoptosis: The cytotoxic lymphocyte serpin proteinase inhibitor 9 protects against granzyme B-mediated apoptosis without perturbing the Fas cell death pathway
    • Bird CH, Sutton VR, Sun J, Hirst CE, Novak A, Kumar S, Trapani JA and Bird PI (1998) Selective regulation of apoptosis: The cytotoxic lymphocyte serpin proteinase inhibitor 9 protects against granzyme B-mediated apoptosis without perturbing the Fas cell death pathway. Mol. Cell Biol. 18: 6387-6398
    • (1998) Mol. Cell Biol. , vol.18 , pp. 6387-6398
    • Bird, C.H.1    Sutton, V.R.2    Sun, J.3    Hirst, C.E.4    Novak, A.5    Kumar, S.6    Trapani, J.A.7    Bird, P.I.8
  • 22
    • 0040189824 scopus 로고    scopus 로고
    • Functional characterization of DNase X, a novel endonuclease expressed in muscle cells
    • Los M, Neubuser D, Coy JF, Mozoluk M, Poustka A and Schulze-Osthoff K (2000) Functional characterization of DNase X, a novel endonuclease expressed in muscle cells. Biochemistry 39: 7365-7373
    • (2000) Biochemistry , vol.39 , pp. 7365-7373
    • Los, M.1    Neubuser, D.2    Coy, J.F.3    Mozoluk, M.4    Poustka, A.5    Schulze-Osthoff, K.6
  • 24
    • 0035081830 scopus 로고    scopus 로고
    • DNase I mediates internucleosomal DNA degradation in human cells undergoing drug-induced apoptosis
    • Oliveri M, Daga A, Cantoni C, Lunardi C, Millo R and Puccetti A (2001) DNase I mediates internucleosomal DNA degradation in human cells undergoing drug-induced apoptosis. Eur. J. Immunol. 31: 743-751
    • (2001) Eur. J. Immunol. , vol.31 , pp. 743-751
    • Oliveri, M.1    Daga, A.2    Cantoni, C.3    Lunardi, C.4    Millo, R.5    Puccetti, A.6
  • 25
    • 0027745784 scopus 로고
    • Overexpression of deoxyribonuclease I (DNase I) transfected into COS-cells: Its distribution during apoptotic cell death
    • Polzar B, Peitsch MC, Loos R, Tschopp J and Mannherz HG (1993) Overexpression of deoxyribonuclease I (DNase I) transfected into COS-cells: its distribution during apoptotic cell death. Eur. J. Cell Biol. 62: 397-405
    • (1993) Eur. J. Cell Biol. , vol.62 , pp. 397-405
    • Polzar, B.1    Peitsch, M.C.2    Loos, R.3    Tschopp, J.4    Mannherz, H.G.5
  • 26
    • 0032553416 scopus 로고    scopus 로고
    • The cloning and expression of human deoxyribonuclease II, A possible role in apoptosis
    • Krieser RJ and Eastman A (1998) The cloning and expression of human deoxyribonuclease II, A possible role in apoptosis. J. Biol. Chem. 273: 30909-30914
    • (1998) J. Biol. Chem. , vol.273 , pp. 30909-30914
    • Krieser, R.J.1    Eastman, A.2
  • 27
    • 0032982478 scopus 로고    scopus 로고
    • L-DNase II: A new molecule in apoptosis pathways
    • Torriglia A, Perani P and Courtois Y (1999) L-DNase II: a new molecule in apoptosis pathways. Med. Sci. 15: 253-259
    • (1999) Med. Sci. , vol.15 , pp. 253-259
    • Torriglia, A.1    Perani, P.2    Courtois, Y.3
  • 28
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis
    • Matsuyama S, Llopis J, Deveraux QL, Tsien RY and Reed JC (2000) Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis. Nat. Cell Biol. 2: 318-325
    • (2000) Nat. Cell Biol. , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 29
    • 0034737646 scopus 로고    scopus 로고
    • Caspase-8-mediated intracellular acidification precedes mitochondrial dysfunction in somatostatin-induced apoptosis
    • Liu D, Martino G, Thangaraju M, Sharma M, Halwani F, Shen SH, Patel YC and Srikant CB (2000) Caspase-8-mediated intracellular acidification precedes mitochondrial dysfunction in somatostatin-induced apoptosis. J. Biol. Chem. 275: 9244-9250
    • (2000) J. Biol. Chem. , vol.275 , pp. 9244-9250
    • Liu, D.1    Martino, G.2    Thangaraju, M.3    Sharma, M.4    Halwani, F.5    Shen, S.H.6    Patel, Y.C.7    Srikant, C.B.8
  • 32
    • 0035863104 scopus 로고    scopus 로고
    • Oxidation of pyridine nucleotides during Fas-and ceramide-induced apoptosis in Jurkat cells: Correlation with changes in mitochondria, glutathione depletion, intracellular acidification and caspase 3 activation
    • Petit PX, Gendron MC, Schrantz N, Metivier D, Kroemer G, Maciorowska Z, Sureau F and Koester S (2001) Oxidation of pyridine nucleotides during Fas-and ceramide-induced apoptosis in Jurkat cells: correlation with changes in mitochondria, glutathione depletion, intracellular acidification and caspase 3 activation. Biochem. J. 353: 357-367
    • (2001) Biochem. J. , vol.353 , pp. 357-367
    • Petit, P.X.1    Gendron, M.C.2    Schrantz, N.3    Metivier, D.4    Kroemer, G.5    Maciorowska, Z.6    Sureau, F.7    Koester, S.8
  • 33
    • 0028917643 scopus 로고
    • Intracellular alkalinization suppresses lovastatin-induced apoptosis in HL-60 cells through the inactivation of a pH-dependent endonuclease
    • Perez-Sala D, Collado-Escobar D and Mollinedo F (1995) Intracellular alkalinization suppresses lovastatin-induced apoptosis in HL-60 cells through the inactivation of a pH-dependent endonuclease. J. Biol. Chem. 270: 6235-6242
    • (1995) J. Biol. Chem. , vol.270 , pp. 6235-6242
    • Perez-Sala, D.1    Collado-Escobar, D.2    Mollinedo, F.3
  • 34
    • 0032513507 scopus 로고    scopus 로고
    • Induction of wild-type p53, Bax, and acidic endonuclease during somatostatin-signaled apoptosis in MCF-7 human breast cancer cells
    • Sharma K and Srikant CB (1998) Induction of wild-type p53, Bax, and acidic endonuclease during somatostatin-signaled apoptosis in MCF-7 human breast cancer cells. Int. J. Cancer 76: 259-266
    • (1998) Int. J. Cancer , vol.76 , pp. 259-266
    • Sharma, K.1    Srikant, C.B.2
  • 37
    • 0035957838 scopus 로고    scopus 로고
    • Elastase is not required for L-DNase II activation during apoptosis in developing chicken neural retina
    • Altairac S, Chaudun E, Courtois Y and Torriglia A (2001) Elastase is not required for L-DNase II activation during apoptosis in developing chicken neural retina. Neurosci. Lett. 303: 41-44
    • (2001) Neurosci. Lett. , vol.303 , pp. 41-44
    • Altairac, S.1    Chaudun, E.2    Courtois, Y.3    Torriglia, A.4
  • 38
    • 0030984026 scopus 로고    scopus 로고
    • Na+/H+ exchangers of mammalian cells
    • Orlowski J and Grinstein S (1997) Na+/H+ exchangers of mammalian cells. J. Biol. Chem. 272: 22373-22376
    • (1997) J. Biol. Chem. , vol.272 , pp. 22373-22376
    • Orlowski, J.1    Grinstein, S.2
  • 39
    • 0027409830 scopus 로고
    • Nucleotide sequence of the Chinese hamster Na+/H+ exchanger NHE1
    • 1172
    • Counillon L and Pouyssegur J (1993) Nucleotide sequence of the Chinese hamster Na+/H+ exchanger NHE1. Biochim. Biophys. Acta 1172: 343-345
    • (1993) Biochim. Biophys. Acta , pp. 343-345
    • Counillon, L.1    Pouyssegur, J.2
  • 40
    • 0028830773 scopus 로고
    • RT-PCR analysis of Na+/H+ exchanger mRNAs in rat medullary thick ascending limb
    • Borensztein P, Froissart M, Laghmani K, Bichara M and Paillard M (1995) RT-PCR analysis of Na+/H+ exchanger mRNAs in rat medullary thick ascending limb. Am. J. Physiol. 268: F1224-F1228
    • (1995) Am. J. Physiol. , vol.268 , pp. F1224-F1228
    • Borensztein, P.1    Froissart, M.2    Laghmani, K.3    Bichara, M.4    Paillard, M.5
  • 41
    • 0028855712 scopus 로고
    • Activation of the Na+/H+ exchanger gene by the transcription factor AP-2
    • Dyck JR, Silva NL and Fliegel L (1995) Activation of the Na+/H+ exchanger gene by the transcription factor AP-2. J. Biol. Chem. 270: 1375-1381
    • (1995) J. Biol. Chem. , vol.270 , pp. 1375-1381
    • Dyck, J.R.1    Silva, N.L.2    Fliegel, L.3
  • 42
  • 43
    • 0029989610 scopus 로고    scopus 로고
    • Effect of intracellular acidity and ionomycin on apoptosis in HL-60 cells
    • Park HJ, Makepeace CM, Lyons JC and Song CW (1996) Effect of intracellular acidity and ionomycin on apoptosis in HL-60 cells. Eur. J. Cancer 32A: 540-546
    • (1996) Eur. J. Cancer , vol.32 A , pp. 540-546
    • Park, H.J.1    Makepeace, C.M.2    Lyons, J.C.3    Song, C.W.4
  • 44
    • 0034652007 scopus 로고    scopus 로고
    • Apoptosis of leukemic cells accompanies reduction in intracellular pH after targeted inhibition of the Na(+)/H(+) exchanger
    • Rich IN, Worthington-White D, Garden OA and Musk P (2000) Apoptosis of leukemic cells accompanies reduction in intracellular pH after targeted inhibition of the Na(+)/H(+) exchanger. Blood 95: 1427-1434
    • (2000) Blood , vol.95 , pp. 1427-1434
    • Rich, I.N.1    Worthington-White, D.2    Garden, O.A.3    Musk, P.4
  • 45
    • 0030954791 scopus 로고    scopus 로고
    • Apoptosis in C3H-10T1/2 cells: Roles of intracellular pH, protein kinase C, and the Na+/H+ antiporter
    • Boyle KM, Irwin JP, Humes BR and Runge SW (1997) Apoptosis in C3H-10T1/2 cells: roles of intracellular pH, protein kinase C, and the Na+/H+ antiporter. J. Cell Biochem. 67: 231-240
    • (1997) J. Cell Biochem. , vol.67 , pp. 231-240
    • Boyle, K.M.1    Irwin, J.P.2    Humes, B.R.3    Runge, S.W.4
  • 47
    • 0030023438 scopus 로고    scopus 로고
    • Topoisomerase II inhibitors affect entry into mitosis and chromosome condensation in BHK cells
    • Anderson H and Roberge M (1996) Topoisomerase II inhibitors affect entry into mitosis and chromosome condensation in BHK cells. Cell Growth Diff. 7: 83-90
    • (1996) Cell Growth Diff. , vol.7 , pp. 83-90
    • Anderson, H.1    Roberge, M.2
  • 49
    • 0024296721 scopus 로고
    • An elastase inhibitor from equine leukocyte cytosol belongs to the serpin superfamily. Further characterization and amino acid sequence of the reactive center
    • Potempa J, Dubin A, Watorek W and Travis J (1988) An elastase inhibitor from equine leukocyte cytosol belongs to the serpin superfamily. Further characterization and amino acid sequence of the reactive center. J. Biol. Chem. 263: 7364-7369
    • (1988) J. Biol. Chem. , vol.263 , pp. 7364-7369
    • Potempa, J.1    Dubin, A.2    Watorek, W.3    Travis, J.4
  • 50
    • 0026806528 scopus 로고
    • Molecular cloning of putative members of the Na/H exchanger gene family. cDNA cloning, deduced amino acid sequence, and mRNA tissue expression of the rat Na/H exchanger NHE-1 and two structurally related proteins
    • Orlowski J, Kandasamy RA and Shull GE (1992) Molecular cloning of putative members of the Na/H exchanger gene family. cDNA cloning, deduced amino acid sequence, and mRNA tissue expression of the rat Na/H exchanger NHE-1 and two structurally related proteins. J. Biol. Chem. 267: 9331-9339
    • (1992) J. Biol. Chem. , vol.267 , pp. 9331-9339
    • Orlowski, J.1    Kandasamy, R.A.2    Shull, G.E.3
  • 51
    • 0026602867 scopus 로고
    • Heterogeneity of the Na(+)-H+ antiport systems in renal cells
    • 1106
    • Viniegra S, Cragoe EJ and Rabito CA (1992) Heterogeneity of the Na(+)-H+ antiport systems in renal cells. Biochim. Biophys. Acta 1106: 99-109
    • (1992) Biochim. Biophys. Acta , pp. 99-109
    • Viniegra, S.1    Cragoe, E.J.2    Rabito, C.A.3
  • 52
    • 0035853137 scopus 로고    scopus 로고
    • A role for intracellular pH in membrane IgM-mediated cell death of human B lymphomas
    • Marches R, Vitetta ES and Uhr JW (2001) A role for intracellular pH in membrane IgM-mediated cell death of human B lymphomas. Proc. Natl. Acad. Sci. USA 98: 3434-3439
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3434-3439
    • Marches, R.1    Vitetta, E.S.2    Uhr, J.W.3
  • 53
    • 0031817915 scopus 로고    scopus 로고
    • The C-D interhelical domain of the serpin plasminogen activator inhibitor-type 2 is required for protection from TNF-alpha induced apoptosis
    • Dickinson JL, Norris BJ, Jensen PH and Antalis TM (1998) The C-D interhelical domain of the serpin plasminogen activator inhibitor-type 2 is required for protection from TNF-alpha induced apoptosis. Cell Death Diff. 5: 163-171
    • (1998) Cell Death Diff. , vol.5 , pp. 163-171
    • Dickinson, J.L.1    Norris, B.J.2    Jensen, P.H.3    Antalis, T.M.4
  • 54
    • 0034619771 scopus 로고    scopus 로고
    • Reduced mammary tumor progression in WAP-TAg/WAP-maspin bitransgenic mice
    • Zhang M, Shi Y, Magit D, Furth PA and Sager R (2000) Reduced mammary tumor progression in WAP-TAg/WAP-maspin bitransgenic mice. Oncogene 19: 6053-6058
    • (2000) Oncogene , vol.19 , pp. 6053-6058
    • Zhang, M.1    Shi, Y.2    Magit, D.3    Furth, P.A.4    Sager, R.5
  • 55
    • 0031755765 scopus 로고    scopus 로고
    • Structure-function relationships in serpins: Current concepts and controversies
    • Gils A and Declerck PJ (1998) Structure-function relationships in serpins: current concepts and controversies. Thromb. Haemostasis 80: 531-541
    • (1998) Thromb. Haemostasis , vol.80 , pp. 531-541
    • Gils, A.1    Declerck, P.J.2
  • 56
    • 0033538462 scopus 로고    scopus 로고
    • Inhibition of phosphatidylcholine biosynthesis following induction of apoptosis in HL-60 cells
    • Anthony ML, Zhao M and Brindle KM (1999) Inhibition of phosphatidylcholine biosynthesis following induction of apoptosis in HL-60 cells. J. Biol. Chem. 274: 19686-19692
    • (1999) J. Biol. Chem. , vol.274 , pp. 19686-19692
    • Anthony, M.L.1    Zhao, M.2    Brindle, K.M.3
  • 57
    • 0029905814 scopus 로고    scopus 로고
    • Detection of apoptosis by flow cytometry of cells simultaneously stained for intracellular pH (carboxy SNARF-1) and membrane permeability (Hoechst 33342)
    • Reynolds JE, Li J and Eastman A (1996) Detection of apoptosis by flow cytometry of cells simultaneously stained for intracellular pH (carboxy SNARF-1) and membrane permeability (Hoechst 33342). Cytometry 25: 349-357
    • (1996) Cytometry , vol.25 , pp. 349-357
    • Reynolds, J.E.1    Li, J.2    Eastman, A.3
  • 58
    • 0033020267 scopus 로고    scopus 로고
    • Cytoplasmic acidification is not an effector mechanism of VP16 or DEX-induced apoptosis in CEM T leukaemia cells
    • Benson RS, Dive C and Watson AJ (1999) Cytoplasmic acidification is not an effector mechanism of VP16 or DEX-induced apoptosis in CEM T leukaemia cells. J. Cell Sci. 112: 1755-1760
    • (1999) J. Cell Sci. , vol.112 , pp. 1755-1760
    • Benson, R.S.1    Dive, C.2    Watson, A.J.3
  • 59
    • 0030680151 scopus 로고    scopus 로고
    • Generation of anti-apoptotic presenilin-2 polypeptides by alternative transcription, proteolysis, and caspase-3 cleavage
    • Vito P, Ghayur T and D'Adamio L (1997) Generation of anti-apoptotic presenilin-2 polypeptides by alternative transcription, proteolysis, and caspase-3 cleavage. J. Biol. Chem. 272: 28315-28320
    • (1997) J. Biol. Chem. , vol.272 , pp. 28315-28320
    • Vito, P.1    Ghayur, T.2    D'Adamio, L.3
  • 61
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ and Yuan J (1998) Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94: 491-501
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 64
    • 0035843138 scopus 로고    scopus 로고
    • Modulation of apoptoss by procaspase-2 short isoform: Selective inhibition of chromatine condensation, apoptotic body formation and phosphatidylserine externalization
    • Droin N, Rebe C, Hammann A, Bertrand R and Solary E (2001) Modulation of apoptoss by procaspase-2 short isoform: selective inhibition of chromatine condensation, apoptotic body formation and phosphatidylserine externalization. Oncogene 20: 260-269
    • (2001) Oncogene , vol.20 , pp. 260-269
    • Droin, N.1    Rebe, C.2    Hammann, A.3    Bertrand, R.4    Solary, E.5
  • 65
    • 0031708849 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase (BTK) as a dual-function regulator of apoptosis
    • Uckun FM (1998) Bruton's tyrosine kinase (BTK) as a dual-function regulator of apoptosis. Biochem. Pharmacol. 56: 683-691
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 683-691
    • Uckun, F.M.1
  • 66
    • 0032740020 scopus 로고    scopus 로고
    • The phosphoprotein protein PEA-15 inhibits Fas- but increases TNF-R1-mediated caspase-8 activity and apoptosis
    • Estelles A, Charlton CA and Blau HM (1999) The phosphoprotein protein PEA-15 inhibits Fas- but increases TNF-R1-mediated caspase-8 activity and apoptosis. Dev. Biol. 216: 16-28
    • (1999) Dev. Biol. , vol.216 , pp. 16-28
    • Estelles, A.1    Charlton, C.A.2    Blau, H.M.3
  • 67
    • 0028813378 scopus 로고
    • Apoptosis in an interleukin-2-dependent cytotoxic T lymphocyte cell line is associated with intracellular acidification. Role of the Na(+)/H(+)-antiport
    • Li J and Eastman A (1995) Apoptosis in an interleukin-2-dependent cytotoxic T lymphocyte cell line is associated with intracellular acidification. Role of the Na(+)/H(+)-antiport. J. Biol. Chem. 270: 3203-3211
    • (1995) J. Biol. Chem. , vol.270 , pp. 3203-3211
    • Li, J.1    Eastman, A.2
  • 68
    • 0029185707 scopus 로고
    • Assays for DNA fragmentation, endonucleases, and intracellular pH and Ca2+ associated with apoptosis
    • Eastman A (1995) Assays for DNA fragmentation, endonucleases, and intracellular pH and Ca2+ associated with apoptosis. Methods Cell Biol. 46: 41-55
    • (1995) Methods Cell Biol. , vol.46 , pp. 41-55
    • Eastman, A.1
  • 69
    • 0031106826 scopus 로고    scopus 로고
    • An assay for DNA fragmentation in apoptosis without phenol/chloroform extraction and ethanol precipitation
    • Zhu N and Wang Z (1997) An assay for DNA fragmentation in apoptosis without phenol/chloroform extraction and ethanol precipitation. Anal. Biochem. 246: 155-158
    • (1997) Anal. Biochem. , vol.246 , pp. 155-158
    • Zhu, N.1    Wang, Z.2
  • 70
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T and Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 71
    • 0030852948 scopus 로고    scopus 로고
    • Mechanism of cellular 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) reduction
    • Liu Y, Peterson DA, Kimura H and Schubert D (1997) Mechanism of cellular 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) reduction. J. Neurochem. 69: 581-593
    • (1997) J. Neurochem. , vol.69 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.