Role of NAD[P]H: quinone oxidoreductase [NQO1] in apoptosis induction by aziridinylbenzoquinones RH1 and MeDZQ

• Autorzy: Nemeikaite-Ceniene A. , Dringeliene A. , Sarlauskas J. , Cenas N.
• Języki publikacji: EN

Abstrakty

EN

We aimed to characterize the role of NAD(P)H : quinone oxidoreductase (NQO1) in apoptosis induction by antitumour quinones RH1 (2,5-diaziridinyl-3-hydroxymethyl-6-methyl-1,4-benzoquinone) and MeDZQ (2,5-dimethyl-3,6-diaziridinyl-1,4-benzoquinone). Digitonin-permeabilized FLK cells catalyzed NADPH-dependent single- and two-electron reduction of RH1 and MeDZQ. At equitoxic concentrations, RH1 and MeDZQ induced apoptosis more efficiently than the nonalkylating duroquinone or H2O2. The antioxidant N,N'-diphenyl-p-phenylene diamine, desferrioxamine, and the inhibitor of NQO1 dicumarol, protected against apoptosis induction by all compounds investigated, but to a different extent. The results of multiparameter regression analysis indicate that RH1 and MeDZQ most likely induce apoptosis via NQO1-linked formation of alkylating species but not via NQO1-linked redox cycling.

Słowa kluczowe

EN

aziridinylbenzoquinone; 2,5-dimetrhyl-3,6-diaziridinyl-1,4-benzoquinone; oxidative stress; cytotoxicity; quinone oxidoreductase; apoptosis induction

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2005
• Tom: 52
• Numer: 4
• Opis fizyczny: p.937-941,fig.,ref.

Twórcy

autor

Nemeikaite-Ceniene A.

• Vilnius University, Vilnius, Lithuania

autor

Dringeliene A.

autor

Sarlauskas J.

autor

Cenas N.

Bibliografia

• Asher G, Lotem J, Sachs L, Shaul Y (2004) Methods Enzymol 382B: 278–293.
• Cameron DW, Giles RGF (1968) J Chem Soc C: 1461–1464.
• Danson S, Ward TH, Butler J, Ranson M (2004) Cancer Treatment Rev 30: 437–449.
• Dees C, Godfrey VL, Foster JS, Schulz RD, Travis CC (1994) Cancer Lett 86: 33–40.
• DiFrancesco AM, Ward TH, Butler J (2004) Methods Enzymol 382B: 174–193.
• Kim JY, Kim CH, Stratford IJ, Patterson AV, Hendry JH (2004) Int J Radiat Oncol Biol Phys 58: 376–485.
• Lee C-S, Hartley JA, Berardini MD, Butler J, Siegel D, Ross D, Gibson NW (1992) Biochemistry 31: 3019–3025.
• McCord JM, Fridovich I (1969) J Biol Chem 244: 6049–6055.
• McGee MM, Campiani G, Ramunno A, Nacci V, Lawler M, Williams DC (2002) J Biol Chem 277: 1383–1389.
• Mercille S, Massie B (1994) Biotechnol Bioeng 44: 1140–1145.
• Nemeikaitė A, Čėnas N (1993) FEBS Lett 326: 65–68.
• Nemeikaitė-Čėnienė A, Šarlauskas J, Anusevičius Ž, Nivinskas H, Čėnas N (2003) Arch Biochem Biophys 416: 110–118.
• Ngo EO, Nutter LM, Sura T, Gutierrez PL (1998) Chem Res Toxicol 11: 360–368.
• O’Brien PJ (1991) Chem-Biol Interact 80: 1–41.
• Ollinger K, Brunmark A (1991) J Biol Chem 266: 21496–21503.
• Pantano C, Shrivastava P, McElhinney B, Janssen-Heininger Y (2003) J Biol Chem 278: 44091–4406.
• Qiu X, Forman HJ, Schonthal AH, Cadenas E (1996) J Biol Chem 271: 31915–31921.
• Qiu XB, Schonthal AH, Cadenas E (1998) Free Rad Biol Med 24: 848–854.
• Ross D, Kepa HJ, Winski S, Beall HD, Anwar A, Siegel D (2000) Chem-Biol Interact 129: 77–97.
• Sun X, Ross D (1996) Chem-Biol Interact 100: 267–276.
• Tudor G, Gutierrez P, Aguilera-Gutierrez A, Sausville EA (2003) Biochem Pharmacol 65: 1061–1075.
• Winski SL, Hargreaves RH, Butler J, Ross D (1998) Clin Cancer Res 4: 3083–3088.