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Volumn 509, Issue , 2016, Pages 33-40

Mono-sulfonated tetrazolium salt based NAD(P)H detection reagents suitable for dehydrogenase and real-time cell viability assays

Author keywords

Cell proliferation; Cell toxicity; Dehydrogenase; High through put screening; Mono sulfonated tetrazolium salt; NAD(P)H assay

Indexed keywords

AMINES; CELL PROLIFERATION; CELLS; SILICA; SILICA GEL; TOXICITY;

EID: 84978154018     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2016.06.026     Document Type: Article
Times cited : (25)

References (24)
  • 1
    • 37549068090 scopus 로고    scopus 로고
    • +/NADPH in cellular functions and cell Death: regulation and Biological Consequences
    • PMID: 18020963
    • +/NADPH in cellular functions and cell Death: regulation and Biological Consequences. Antioxid. Redox. Sign 10 (2007), 179–206, 10.1089/ars.2007.1672 PMID: 18020963.
    • (2007) Antioxid. Redox. Sign , vol.10 , pp. 179-206
    • Ying, W.1
  • 3
    • 0025940277 scopus 로고
    • Drug antioxidant effects. A basis for drug selection?
    • PMID: 1723362
    • [3] Halliwell, B., Drug antioxidant effects. A basis for drug selection?. Drugs 42 (1991), 569–605 PMID: 1723362.
    • (1991) Drugs , vol.42 , pp. 569-605
    • Halliwell, B.1
  • 4
    • 0021039516 scopus 로고
    • Studies on the phenazine methosulphate-tetrazolium salt capture reaction in NAD(P)+-dependent dehydrogenase cytochemistry. III. The role of superoxide in tetrazolium reduction
    • PMID: 6315642
    • [4] Raap, A.K., Studies on the phenazine methosulphate-tetrazolium salt capture reaction in NAD(P)+-dependent dehydrogenase cytochemistry. III. The role of superoxide in tetrazolium reduction. Histochem. J. 15 (1983), 977–986 PMID: 6315642.
    • (1983) Histochem. J. , vol.15 , pp. 977-986
    • Raap, A.K.1
  • 5
    • 84927133194 scopus 로고    scopus 로고
    • Targeting mitochondria metabolism for cancer therapy
    • PMID: 25517383
    • [5] Weinberg, S.E., Chandel, N.S., Targeting mitochondria metabolism for cancer therapy. Nat. Chem. Biol. 11 (2015), 9–15, 10.1038/nchembio.1712 PMID: 25517383.
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 9-15
    • Weinberg, S.E.1    Chandel, N.S.2
  • 6
    • 0024331467 scopus 로고
    • Characterization of glutamate dehydrogenase isoproteins purified from the cerebellum of normal subjects and patients with degenerative neurological disorders, and from human neoplastic cell lines
    • PMID: 2573605
    • [6] Hussain, M.M., Zannis, V., Plaitakis, A., Characterization of glutamate dehydrogenase isoproteins purified from the cerebellum of normal subjects and patients with degenerative neurological disorders, and from human neoplastic cell lines. J. Biol. Chem. 264 (1989), 20730–20735 PMID: 2573605.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20730-20735
    • Hussain, M.M.1    Zannis, V.2    Plaitakis, A.3
  • 7
    • 0025058979 scopus 로고
    • The inhibition of glutamate dehydrogenase by some antipsychotic drugs, Biochem
    • PMID: 2310408
    • [7] Couée, I., Tipton, K.F., The inhibition of glutamate dehydrogenase by some antipsychotic drugs, Biochem. Pharmacol 39 (1990), 827–832 PMID: 2310408.
    • (1990) Pharmacol , vol.39 , pp. 827-832
    • Couée, I.1    Tipton, K.F.2
  • 8
    • 84885998103 scopus 로고    scopus 로고
    • Inhibitors of glutamate dehydrogenase block sodium-dependent glutamate uptake in rat brain membranes
    • PMID: 24062726
    • [8] Whitelaw, B.S., Robinson, M.B., Inhibitors of glutamate dehydrogenase block sodium-dependent glutamate uptake in rat brain membranes. Front. Endocrinol. (Lausanne) 4 (2013), 123–131, 10.3389/fendo.2013.00123 PMID: 24062726.
    • (2013) Front. Endocrinol. (Lausanne) , vol.4 , pp. 123-131
    • Whitelaw, B.S.1    Robinson, M.B.2
  • 9
    • 0023695196 scopus 로고
    • Regulation of insulin release by factors that also modify glutamate dehydrogenase
    • PMID: 3047128
    • [9] Fahien, L.A., MacDonald, M.J., Kmiotek, E.H., Mertz, R.J., Fahien, C.M., Regulation of insulin release by factors that also modify glutamate dehydrogenase. J. Biol. Chem. 263 (1988), 13610–136144 PMID: 3047128.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13610-136144
    • Fahien, L.A.1    MacDonald, M.J.2    Kmiotek, E.H.3    Mertz, R.J.4    Fahien, C.M.5
  • 11
    • 84959142950 scopus 로고    scopus 로고
    • 2-Methylcitric Acid Impairs Glutamate Metabolism and Induces Permeability Transition in Brain Mitochondria
    • PMID: 26800654
    • [11] Amaral, A.U., Cecatto, C., Castilho, R.F., Wajner, M., 2-Methylcitric Acid Impairs Glutamate Metabolism and Induces Permeability Transition in Brain Mitochondria. J. Neurochem., 2016, 10.1111/jnc.13544 PMID: 26800654.
    • (2016) J. Neurochem.
    • Amaral, A.U.1    Cecatto, C.2    Castilho, R.F.3    Wajner, M.4
  • 12
    • 0034754714 scopus 로고    scopus 로고
    • Effects of ADP on different inhibitory properties of brain glutamate dehydrogenase isoproteins by perphenazine
    • PMID: 11698113
    • [12] Yoon, H.Y., Hwang, S.H., Lee, E.Y., Kim, T.U., Cho, E.H., Cho, S.W., Effects of ADP on different inhibitory properties of brain glutamate dehydrogenase isoproteins by perphenazine. Biochimie 83 (2001), 907–913 PMID: 11698113.
    • (2001) Biochimie , vol.83 , pp. 907-913
    • Yoon, H.Y.1    Hwang, S.H.2    Lee, E.Y.3    Kim, T.U.4    Cho, E.H.5    Cho, S.W.6
  • 13
    • 0025278026 scopus 로고
    • Inhibition of ox brain glutamate dehydrogenase by perphenazine
    • PMID: 2322301
    • [13] Couée, I., Tipton, K.F., Inhibition of ox brain glutamate dehydrogenase by perphenazine. Biochem. Pharmacol. 39 (1990), 1167–1173 PMID: 2322301.
    • (1990) Biochem. Pharmacol. , vol.39 , pp. 1167-1173
    • Couée, I.1    Tipton, K.F.2
  • 14
    • 0017247658 scopus 로고
    • Tetrazolium salts and formazans
    • PMID: 792958
    • [14] Altman, F.P., Tetrazolium salts and formazans. Prog. Histochem. Cytochem 9 (1976), 1–56 PMID: 792958.
    • (1976) Prog. Histochem. Cytochem , vol.9 , pp. 1-56
    • Altman, F.P.1
  • 15
    • 0026180079 scopus 로고
    • 2, 3, 5-Triphenyi Tetrazolium Chloride (TTC) reduction as exponential growth phase marker for mammalian cells in culture and for myeloma hybridization experiments
    • PMID: 1367407
    • [15] Otero, A.J., Rodríguez, I., Falero, G., 2, 3, 5-Triphenyi Tetrazolium Chloride (TTC) reduction as exponential growth phase marker for mammalian cells in culture and for myeloma hybridization experiments. Cytotechnology 6 (1991), 137–142 PMID: 1367407.
    • (1991) Cytotechnology , vol.6 , pp. 137-142
    • Otero, A.J.1    Rodríguez, I.2    Falero, G.3
  • 16
    • 0025738516 scopus 로고
    • Tetrazolium-based Assays for Cellular Viability: A Critical Examination of Selected Parameters Affecting Formazan Production
    • PMID: 2021931
    • [16] Vistica, D.T., Skehan, P., Scudiero, D., Monks, A., Pittman, A., Boyd, M.R., Tetrazolium-based Assays for Cellular Viability: A Critical Examination of Selected Parameters Affecting Formazan Production. Cancer Res. 51 (1991), 2515–2520 PMID: 2021931.
    • (1991) Cancer Res. , vol.51 , pp. 2515-2520
    • Vistica, D.T.1    Skehan, P.2    Scudiero, D.3    Monks, A.4    Pittman, A.5    Boyd, M.R.6
  • 18
    • 0030978319 scopus 로고    scopus 로고
    • A highly water-soluble disulfonated tetrazolium salt as a chromogenic indicator for NADH as well as cell viability
    • PMID: 18966866
    • [18] Ishiyama, M., Miyazono, Y., Sasamoto, K., Ohkura, Y., Ueno, K., A highly water-soluble disulfonated tetrazolium salt as a chromogenic indicator for NADH as well as cell viability. Talanta 44 (1997), 1299–1305 PMID: 18966866.
    • (1997) Talanta , vol.44 , pp. 1299-1305
    • Ishiyama, M.1    Miyazono, Y.2    Sasamoto, K.3    Ohkura, Y.4    Ueno, K.5
  • 19
    • 84978105544 scopus 로고
    • Method for preparing 2H-tetrazolium chloride and 2H-tetrazolium chloride hydrochloride
    • [19] Ostrovskaya, V.M., Lushina, O.T., Dziomko, V.M., Davydovskaya, J.A., Method for preparing 2H-tetrazolium chloride and 2H-tetrazolium chloride hydrochloride. United States Patent No. 4143049, 1979, 1–5 http://www.freepatentsonline.com/4143049.html.
    • (1979) United States Patent No. 4143049 , pp. 1-5
    • Ostrovskaya, V.M.1    Lushina, O.T.2    Dziomko, V.M.3    Davydovskaya, J.A.4
  • 20
    • 84981752339 scopus 로고
    • Notiz über eine Tetrazoliumverbindung der Pyrimidinreihe
    • [20] Ludolphy, E., Notiz über eine Tetrazoliumverbindung der Pyrimidinreihe. Chem. Ber. 84 (1951), 385–387, 10.1002/cber.19510840408.
    • (1951) Chem. Ber. , vol.84 , pp. 385-387
    • Ludolphy, E.1
  • 21
    • 84921024562 scopus 로고    scopus 로고
    • Determination of Glutamate Dehydrogenase Activity and Its Kinetics in Mouse Tissues using Metabolic Mapping (Quantitative Enzyme Histochemistry)
    • [21] Botman, D., Tigchelaar, W., Van Noorden, C.J.F., Determination of Glutamate Dehydrogenase Activity and Its Kinetics in Mouse Tissues using Metabolic Mapping (Quantitative Enzyme Histochemistry). J. Histochem. Cytochem 62 (2014), 802–812, 10.1369/0022155414549071.
    • (2014) J. Histochem. Cytochem , vol.62 , pp. 802-812
    • Botman, D.1    Tigchelaar, W.2    Van Noorden, C.J.F.3
  • 22
    • 70350217425 scopus 로고    scopus 로고
    • Glioblastoma cells require glutamate dehydrogenase to survive impairments of glucose metabolism or Akt signaling
    • PMID: 19826036
    • [22] Yang, C., Sudderth, J., Dang, T., Bachoo, R.M., McDonald, J.G., DeBerardinis, R.J., Glioblastoma cells require glutamate dehydrogenase to survive impairments of glucose metabolism or Akt signaling. Cancer Res. 69 (2009), 7986–7993, 10.1158/0008-5472.CAN-09-2266 PMID: 19826036.
    • (2009) Cancer Res. , vol.69 , pp. 7986-7993
    • Yang, C.1    Sudderth, J.2    Dang, T.3    Bachoo, R.M.4    McDonald, J.G.5    DeBerardinis, R.J.6
  • 23
    • 0037172997 scopus 로고    scopus 로고
    • Ebselen: A substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant
    • PMID: 12070343
    • [23] Zhao, R., Masayasu, H., Holmgren, A., Ebselen: A substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant. Proc. Natl. Acad. Sci. U. S. A. 99 (2002), 8579–8584, 10.1073/pnas.122061399 PMID: 12070343.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 8579-8584
    • Zhao, R.1    Masayasu, H.2    Holmgren, A.3
  • 24
    • 80052271742 scopus 로고    scopus 로고
    • The structure and allosteric regulation of glutamate dehydrogenase
    • [24] Li, M., Li, C., Allen, A., Stanley, C.A., Smith, T.J., The structure and allosteric regulation of glutamate dehydrogenase. Neurochem. Int. 59 (2011), 445–455, 10.1016/j.neuint.2010.10.017.
    • (2011) Neurochem. Int. , vol.59 , pp. 445-455
    • Li, M.1    Li, C.2    Allen, A.3    Stanley, C.A.4    Smith, T.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.