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Volumn 49, Issue 1, 2010, Pages 505-512

Quantification of DNase type I ends, DNase type II ends, and modified bases using fluorescently labeled ddUTP, terminal deoxynucleotidyl transferase, and formamidopyrimidine-DNA glycosylase

Author keywords

Apoptosis; Chemotherapy; ddUTP; DNase; Formamidopyrimidine DNA glycosylase; Mammary gland; TUNEL; U87

Indexed keywords

ANTINEOPLASTIC AGENT; CARMUSTINE; DEOXYRIBONUCLEASE I; DEOXYRIBONUCLEASE II; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; DNA BASE; DNA FORMAMIDOPYRIMIDINE GLYCOSYLASE; DNA NUCLEOTIDYLEXOTRANSFERASE; IRINOTECAN; PARAQUAT; REACTIVE OXYGEN METABOLITE; TEMOZOLOMIDE; DNA; FLUORESCENT DYE; URIDINE TRIPHOSPHATE;

EID: 77957960606     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/000113439     Document Type: Article
Times cited : (10)

References (38)
  • 1
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli, Y., Y. Sherman, and S.A. Ben-Sasson. 1992. Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J. Cell Biol. 119:493-501.
    • (1992) J. Cell Biol. , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 2
    • 0037405816 scopus 로고    scopus 로고
    • A novel method to determine specificity and sensitivity of the TUNEL reaction in the quantitation of apoptosis
    • Kelly, K.J., R.M. Sandoval, K.W. Dunn, B.A. Molitoris, and P.C. Dagher. 2003. A novel method to determine specificity and sensitivity of the TUNEL reaction in the quantitation of apoptosis. Am. J. Physiol. Cell Physiol. 284:C1309-C1318.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Kelly, K.J.1    Sandoval, R.M.2    Dunn, K.W.3    Molitoris, B.A.4    Dagher, P.C.5
  • 4
    • 33744725190 scopus 로고    scopus 로고
    • Detection of DNA strand breaks by flow and laser scanning cytometry in studies of apoptosis and cell proliferation (DNA replication)
    • Darzynkiewicz, Z., X. Huang, and M. Okafuji. 2006. Detection of DNA strand breaks by flow and laser scanning cytometry in studies of apoptosis and cell proliferation (DNA replication). Methods Mol. Biol. 314:81-93.
    • (2006) Methods Mol. Biol. , vol.314 , pp. 81-93
    • Darzynkiewicz, Z.1    Huang, X.2    Okafuji, M.3
  • 5
    • 77954460238 scopus 로고    scopus 로고
    • Quantification and calibration of images in fluorescence microscopy
    • May 28. [Epub ahead of print]
    • Sharpe, M.A., M.A. Widmayer, and D.S. Baskin. 2010. Quantification and calibration of images in fluorescence microscopy. Anal. Biochem. May 28. [Epub ahead of print].
    • (2010) Anal. Biochem.
    • Sharpe, M.A.1    Widmayer, M.A.2    Baskin, D.S.3
  • 6
    • 33644821892 scopus 로고    scopus 로고
    • Rapid and preferential distribution of blood-borne CD3-ε to the liver is followed by local stimulation of T cells and natural killer T cells
    • Wingender, G., B. Schumak, A. Schurich, J.E. Gessner, E. Endl, A. Limmer, and P.A. Knolle. 2006. Rapid and preferential distribution of blood-borne CD3-ε to the liver is followed by local stimulation of T cells and natural killer T cells. Immunology 117:117-126.
    • (2006) Immunology , vol.117 , pp. 117-126
    • Wingender, G.1    Schumak, B.2    Schurich, A.3    Gessner, J.E.4    Endl, E.5    Limmer, A.6    Knolle, P.A.7
  • 7
    • 67651239268 scopus 로고    scopus 로고
    • Cell turnover and gene activities in sheep mammary glands prior to lambing to involution
    • Colitti, M. and M. Farinacci. 2009. Cell turnover and gene activities in sheep mammary glands prior to lambing to involution. Tissue Cell 41:326-333.
    • (2009) Tissue Cell , vol.41 , pp. 326-333
    • Colitti, M.1    Farinacci, M.2
  • 8
    • 0038607918 scopus 로고    scopus 로고
    • Activating transcription factor 4 overexpression inhibits proliferation and differentiation of mammary epithelium resulting in impaired lactation and accelerated involution
    • Bagheri-Yarmand, R., R.K. Vadlamudi, and R. Kumar. 2003. Activating transcription factor 4 overexpression inhibits proliferation and differentiation of mammary epithelium resulting in impaired lactation and accelerated involution. J. Biol. Chem. 278:17421-17429.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17421-17429
    • Bagheri-Yarmand, R.1    Vadlamudi, R.K.2    Kumar, R.3
  • 9
    • 0038146874 scopus 로고    scopus 로고
    • Role of DDC-4/sFRP-4, a secreted frizzled-related protein, at the onset of apoptosis in mammary involution
    • Lacher, M.D., A. Siegenthaler, R. Jager, X. Yan, S. Hett, L. Xuan, S. Saurer, R.R. Lareu, et al. 2003. Role of DDC-4/sFRP-4, a secreted frizzled-related protein, at the onset of apoptosis in mammary involution. Cell Death Differ. 10:528-538.
    • (2003) Cell Death Differ. , vol.10 , pp. 528-538
    • Lacher, M.D.1    Siegenthaler, A.2    Jager, R.3    Yan, X.4    Hett, S.5    Xuan, L.6    Saurer, S.7    Lareu, R.R.8
  • 10
    • 0032920274 scopus 로고    scopus 로고
    • Double immunolabeling of neuropeptides in the human hypothalamus as analyzed by confocal laser scanning fluorescence microscopy
    • Romijn, H.J., J.F.M. Van Uum, I. Breedijk, J. Emmering, I. Radu, and C.W. Pool. 1999. Double immunolabeling of neuropeptides in the human hypothalamus as analyzed by confocal laser scanning fluorescence microscopy. J. Histochem. Cytochem. 47:229-235.
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 229-235
    • Romijn, H.J.1    Van Uum, J.F.M.2    Breedijk, I.3    Emmering, J.4    Radu, I.5    Pool, C.W.6
  • 11
    • 33845334495 scopus 로고    scopus 로고
    • Acid DNases and their interest among apoptotic endonucleases
    • Counis, M.F. and A. Torriglia. 2006. Acid DNases and their interest among apoptotic endonucleases. Biochimie 88:1851-1858.
    • (2006) Biochimie , vol.88 , pp. 1851-1858
    • Counis, M.F.1    Torriglia, A.2
  • 13
    • 69149090478 scopus 로고    scopus 로고
    • LEI/L-DNase II: Interplay between caspase-dependent and independent pathways
    • Torriglia, A. and C. Lepretre. 2009. LEI/L-DNase II: interplay between caspase-dependent and independent pathways. Front. Biosci. 14:4836-4847.
    • (2009) Front. Biosci. , vol.14 , pp. 4836-4847
    • Torriglia, A.1    Lepretre, C.2
  • 14
    • 0029761401 scopus 로고    scopus 로고
    • Increased resistance to N,N′,N″-triethylenethiophosphoramide (thiotepa) in cells expressing the Escherichia coli formamidopyrimidine-DNA glycosylase
    • Gill, R.D., C. Cussac, R.L. Souhami, and F. Laval. 1996. Increased resistance to N,N′,N″-triethylenethiophosphoramide (thiotepa) in cells expressing the Escherichia coli formamidopyrimidine-DNA glycosylase. Cancer Res. 56:3721-3724.
    • (1996) Cancer Res. , vol.56 , pp. 3721-3724
    • Gill, R.D.1    Cussac, C.2    Souhami, R.L.3    Laval, F.4
  • 15
    • 0004370304 scopus 로고
    • Physical association of the 2,6-diamino-4-hydroxy-5N-formamidopyrimidine- DNA glycosylase of Escherichia coli and an activity nicking DNA at apurinic/apyrimidinic sites
    • O'Connor, T.R. and J. Laval. 1989. Physical association of the 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase of Escherichia coli and an activity nicking DNA at apurinic/apyrimidinic sites. Proc. Natl. Acad. Sci. USA 86:5222-5226.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5222-5226
    • O'Connor, T.R.1    Laval, J.2
  • 16
    • 33644848956 scopus 로고    scopus 로고
    • Accelerated repair and reduced mutagenicity of oxidative DNA damage in human bladder cells expressing the E. coli FPG protein
    • Ropolo, M., A. Geroldi, P. Degan, V. Andreotti, S. Zupo, A. Poggi, A. Reed, M.R. Kelley, and G. Frosina. 2006. Accelerated repair and reduced mutagenicity of oxidative DNA damage in human bladder cells expressing the E. coli FPG protein. Int. J. Cancer 118:1628-1634.
    • (2006) Int. J. Cancer , vol.118 , pp. 1628-1634
    • Ropolo, M.1    Geroldi, A.2    Degan, P.3    Andreotti, V.4    Zupo, S.5    Poggi, A.6    Reed, A.7    Kelley, M.R.8    Frosina, G.9
  • 17
    • 0345276655 scopus 로고    scopus 로고
    • Sensitivity of the FPG protein towards alkylation damage in the comet assay
    • Speit, G., P. Schitz, I. Bonzheim, K. Trenz, and H. Hoffmann. 2004. Sensitivity of the FPG protein towards alkylation damage in the comet assay. Toxicol. Lett. 146:151-158.
    • (2004) Toxicol. Lett. , vol.146 , pp. 151-158
    • Speit, G.1    Schitz, P.2    Bonzheim, I.3    Trenz, K.4    Hoffmann, H.5
  • 18
    • 0037099404 scopus 로고    scopus 로고
    • Protection of human lung cells against hyperoxia using the DNA base excision repair genes hOgg1 and Fpg
    • Wu, M., Y.H. He, M. Kobune, Y. Xu, M.R. Kelley, and W.J. Martin II. 2002. Protection of human lung cells against hyperoxia using the DNA base excision repair genes hOgg1 and Fpg. Am. J. Respir. Crit. Care Med. 166:192-199.
    • (2002) Am. J. Respir. Crit. Care Med. , vol.166 , pp. 192-199
    • Wu, M.1    He, Y.H.2    Kobune, M.3    Xu, Y.4    Kelley, M.R.5    Martin II, W.J.6
  • 20
    • 0035122915 scopus 로고    scopus 로고
    • Protection of mammalian cells against chemotherapeutic agents thiotepa, 1,3-N,N-bis(2-chloroethyl)-N-nitrosourea, and mafosfamide using the DNA base excision repair genes Fpg and Ogg1: Implications for protective gene therapy applications
    • Xu, Y., W.K. Hansen, T.A. Rosenquist, D.A. Williams, M. Limp-Foster, and M.R. Kelley. 2001. Protection of mammalian cells against chemotherapeutic agents thiotepa, 1,3-N,N-bis(2-chloroethyl)-N-nitrosourea, and mafosfamide using the DNA base excision repair genes Fpg and Ogg1: implications for protective gene therapy applications. J. Pharmacol. Exp. Ther. 296:825-831.
    • (2001) J. Pharmacol. Exp. Ther. , vol.296 , pp. 825-831
    • Xu, Y.1    Hansen, W.K.2    Rosenquist, T.A.3    Williams, D.A.4    Limp-Foster, M.5    Kelley, M.R.6
  • 21
    • 0031984807 scopus 로고    scopus 로고
    • Highly sensitive apurinic/apyrimidinic site assay can detect spontaneous and chemically induced depurination under physiological conditions
    • Nakamura, J., V.E. Walker, P.B. Upton, S.Y. Chiang, Y.W. Kow, and J.A. Swenberg. 1998. Highly sensitive apurinic/apyrimidinic site assay can detect spontaneous and chemically induced depurination under physiological conditions. Cancer Res. 58:222-225. (Pubitemid 28047058)
    • (1998) Cancer Research , vol.58 , Issue.2 , pp. 222-225
    • Nakamura, J.1    Walker, V.E.2    Upton, P.B.3    Chiang, S.-Y.4    Kow, Y.W.5    Swenberg, J.A.6
  • 22
    • 70350075002 scopus 로고    scopus 로고
    • Investigating the biochemical impact of DNA damage with structure-based probes: A basic sites, photodimers, alkylation adducts, and oxidative lesions
    • Dahlmann, H.A., V.G. Vaidyanathan, and S.J. Sturla. 2009. Investigating the biochemical impact of DNA damage with structure-based probes: a basic sites, photodimers, alkylation adducts, and oxidative lesions. Biochemistry 48:9347-9359.
    • (2009) Biochemistry , vol.48 , pp. 9347-9359
    • Dahlmann, H.A.1    Vaidyanathan, V.G.2    Sturla, S.J.3
  • 23
    • 33845679785 scopus 로고    scopus 로고
    • Nonrandom AP site distribution in highly proliferative cells
    • Chastain 2nd, P.D., J. Nakamura, J. Swenberg, and D. Kaufman. 2006. Nonrandom AP site distribution in highly proliferative cells. FASEB J. 20:2612-2614.
    • (2006) FASEB J. , vol.20 , pp. 2612-2614
    • Chastain II, P.D.1    Nakamura, J.2    Swenberg, J.3    Kaufman, D.4
  • 25
    • 0031776586 scopus 로고    scopus 로고
    • Cytochemical demonstration of oxidative damage in Alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2,4- dinitrophenylhydrazine
    • Smith, M.A., L.M. Sayre, V.E. Anderson, P.L.R. Harris, M.F. Beal, N. Kowall, and G. Perry. 1998. Cytochemical demonstration of oxidative damage in Alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2,4-dinitrophenylhydrazine. J. Histochem. Cytochem. 46:731-735.
    • (1998) J. Histochem. Cytochem. , vol.46 , pp. 731-735
    • Smith, M.A.1    Sayre, L.M.2    Anderson, V.E.3    Harris, P.L.R.4    Beal, M.F.5    Kowall, N.6    Perry, G.7
  • 26
    • 0030933522 scopus 로고    scopus 로고
    • Involution of the sheep mammary gland
    • Tatarczuch, L., C. Philip, and C.S. Lee. 1997. Involution of the sheep mammary gland. J. Anat. 190:405-416.
    • (1997) J. Anat. , vol.190 , pp. 405-416
    • Tatarczuch, L.1    Philip, C.2    Lee, C.S.3
  • 27
    • 0028877356 scopus 로고
    • Degradation processes in different functional states of the mouse mammary gland
    • Kralj, M. and N. Pipan. 1995. Degradation processes in different functional states of the mouse mammary gland. Period. Biol. 97:201-206.
    • (1995) Period. Biol. , vol.97 , pp. 201-206
    • Kralj, M.1    Pipan, N.2
  • 28
    • 0024377789 scopus 로고
    • Cell death by apoptosis during involution of the lactating breast in mice and rats
    • Walker, N.I., R.E. Bennett, and J.F.R. Kerr. 1989. Cell death by apoptosis during involution of the lactating breast in mice and rats. Am. J. Anat. 185:19-32.
    • (1989) Am. J. Anat. , vol.185 , pp. 19-32
    • Walker, N.I.1    Bennett, R.E.2    Kerr, J.F.R.3
  • 29
    • 34047202713 scopus 로고    scopus 로고
    • Levels and distribution of BCNU in GBM tumors following intratumoral injection of DTI-015 (BCNU-ethanol)
    • Bodell, W.J., A.P. Bodell, and D.D. Giannini. 2007. Levels and distribution of BCNU in GBM tumors following intratumoral injection of DTI-015 (BCNU-ethanol). Neuro. Oncol. 9:12-19.
    • (2007) Neuro. Oncol. , vol.9 , pp. 12-19
    • Bodell, W.J.1    Bodell, A.P.2    Giannini, D.D.3
  • 31
    • 0028305721 scopus 로고
    • New substrates for old enzymes. 5-Hydroxy-2′-deoxycytidine and 5-hydroxy- 2′-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNA N-glycosylase
    • Hatahet, Z., Y.W. Kow, A.A. Purmal, R.P. Cunningham, and S.S. Wallace. 1994. New substrates for old enzymes. 5-Hydroxy-2′-deoxycytidine and 5-hydroxy- 2′-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNA N-glycosylase. J. Biol. Chem. 269:18814-18820.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18814-18820
    • Hatahet, Z.1    Kow, Y.W.2    Purmal, A.A.3    Cunningham, R.P.4    Wallace, S.S.5
  • 32
    • 0033574208 scopus 로고    scopus 로고
    • Excision of 5,6-dihydroxy-5,6-dihydrothymine, 5,6-dihydrothymine, and 5-hydroxycytosine from defined sequence oligonucleotides by Escherichia coli endonuclease III and Fpg proteins
    • D'Ham, C., A. Romieu, M. Jaquinod, D. Gasparutto, and J. Cadet. 1999. Excision of 5,6-dihydroxy-5,6-dihydrothymine, 5,6-dihydrothymine, and 5-hydroxycytosine from defined sequence oligonucleotides by Escherichia coli endonuclease III and Fpg proteins. Biochemistry 38:3335-3344.
    • (1999) Biochemistry , vol.38 , pp. 3335-3344
    • D'Ham, C.1    Romieu, A.2    Jaquinod, M.3    Gasparutto, D.4    Cadet, J.5
  • 33
    • 0035394724 scopus 로고    scopus 로고
    • Retrovirus-mediated expression of the base excision repair proteins, formamidopyrimidine DNA glycosylase or human oxoguanine DNA glycosylase, protects hematopoietic cells from N,N′,N″- triethylenethiophosphoramide (thioTEPA)-induced toxicity in vitro and in vivo
    • Kobune, M., Y. Xu, C. Baum, M.R. Kelley, and D.A. Williams. 2001. Retrovirus-mediated expression of the base excision repair proteins, formamidopyrimidine DNA glycosylase or human oxoguanine DNA glycosylase, protects hematopoietic cells from N,N′,N″- triethylenethiophosphoramide (thioTEPA)-induced toxicity in vitro and in vivo. Cancer Res. 61:5116-5125. (Pubitemid 32681543)
    • (2001) Cancer Research , vol.61 , Issue.13 , pp. 5116-5125
    • Kobune, M.1    Xu, Y.2    Baum, C.3    Kelley, M.R.4    Williams, D.A.5
  • 34
    • 33646508777 scopus 로고    scopus 로고
    • Prophylaxis of oxidative DNA damage by formamidopyrimidine-DNA glycosylase
    • Frosina, G. 2006. Prophylaxis of oxidative DNA damage by formamidopyrimidine-DNA glycosylase. Int. J. Cancer 119:1-7.
    • (2006) Int. J. Cancer , vol.119 , pp. 1-7
    • Frosina, G.1
  • 35
    • 0030983740 scopus 로고    scopus 로고
    • Synthesis of fluorescent probes for the detection of abasic sites in DNA
    • DOI 10.1016/S0040-4020(97)00235-4, PII S0040402097002354
    • Boturyn, D., A. Boudali, J.-F. Constant, E. Defrancq, and J. Lhomme. 1997. Synthesis of fluorescent probes for the detection of abasic sites in DNA. Tetrahedron 53:5485-5492. (Pubitemid 27149942)
    • (1997) Tetrahedron , vol.53 , Issue.15 , pp. 5485-5492
    • Boturyn, D.1    Boudali, A.2    Constant, J.-F.3    Defrancq, E.4    Lhomme, J.5
  • 36
    • 0141918862 scopus 로고    scopus 로고
    • Nitric oxide and Fenton/Haber-Weiss chemistry: Nitric oxide is a potent antioxidant at physiological concentrations
    • DOI 10.1046/j.1471-4159.2003.02001.x
    • Sharpe, M.A., S.J. Robb, and J.B. Clark. 2003. Nitric oxide and Fenton/Haber-Weiss chemistry: nitric oxide is a potent antioxidant at physiological concentrations. J. Neurochem. 87:386-394. (Pubitemid 37255246)
    • (2003) Journal of Neurochemistry , vol.87 , Issue.2 , pp. 386-394
    • Sharpe, M.A.1    Robb, S.J.2    Clark, J.B.3
  • 37
    • 0029812580 scopus 로고    scopus 로고
    • Oxidative damage to DNA constituents by iron-mediated Fenton reactions
    • Henle, E.S., Y. Luo, W. Gassmann, and S. Linn. 1996. Oxidative damage to DNA constituents by iron-mediated Fenton reactions. J. Biol. Chem. 271:21167-21176.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21167-21176
    • Henle, E.S.1    Luo, Y.2    Gassmann, W.3    Linn, S.4
  • 38
    • 0037867770 scopus 로고    scopus 로고
    • Imidazole ring-opened DNA purines and their biological significance
    • Tudek, B. 2003. Imidazole ring-opened DNA purines and their biological significance. J. Biochem. Mol. Biol. 36:12-19.
    • (2003) J. Biochem. Mol. Biol. , vol.36 , pp. 12-19
    • Tudek, B.1


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