Studies on mechanism of 8-methoxypsoralen–DNA interaction in the dark

Arabzadeh, AmirAhmad; Bathaie, S. Zahra; Farsam, H; Amanlou, Massoud; Saboury, Ali Akbar; Shockravi, Abbas; Moosavi-Movahedi, Ali Akbar

doi:10.1016/s0378-5173(02)00020-0

Cited by 37 publications

(14 citation statements)

References 32 publications

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“…S-phase arrest induced by 8-MOP in HepG2 cells indicates its probable inhibition on DNA replication. It agrees with previous report that 8-MOP, independent of the UV irradiation, binds to DNA as an intercalator at low drug load [16]. It is speculated that 8-MOP binds to DNA, subsequently leads to cell cycle arrest and cell proliferation inhibition.…”

Section: Discussionsupporting

confidence: 92%

8-Methoxypsoralen Induces Intrinsic Apoptosis in HepG2 Cells: Involvement of Reactive Oxygen Species Generation and ERK1/2 Pathway Inhibition

Yang

Xiong

Luo

et al. 2015

Cell Physiol Biochem

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Background/Aims: 8-Methoxypsoralen (8-MOP), a formerly considered photosensitizing agent, induces apoptosis when used alone. On this basis, the present study was designed to explore the effects and mechanisms of 8-MOP-induced apoptosis in human hepatocellular carcinoma HepG2 cells, independent of its photoactivation. Methods: We analyzed the cell viability with MTT assay. Flow cytometry was used to examine the apoptosis rate, mitochondrial membrane potential (MMP) and reactive oxygen species (ROS) generation after specific staining. The expression and location of apoptosis-associated protein as well as the activation status of cell signaling pathway were determined by Western blot analysis. Results: 8-MOP significantly decreased cell viability and induced cell apoptosis through mitochondrial apoptotic pathway, as demonstrated by increased Bax/Bcl-2 ratio, collapsed MMP, and induced cytochrome c release (Cyt c) and apoptosis-inducing factor (AIF) transposition. ROS generation was significantly increased by 8-MOP and the eradication of ROS significantly abolished 8-MOP-induced apoptosis. In addition, the activation of ERK1/2 was drastically decreased by 8-MOP as ERK inhibitor PD98059, indicating a role of ERK1/2 signaling pathway in 8-MOP-induced cell apoptosis. Conclusion: 8-MOP induces intrinsic apoptosis by increasing ROS generation and inhibiting ERK1/2 pathway in HepG2 cells. The findings are important in substantiating the anti-tumor role of 8-MOP in cancer therapy.

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Section: Discussionsupporting

confidence: 92%

8-Methoxypsoralen Induces Intrinsic Apoptosis in HepG2 Cells: Involvement of Reactive Oxygen Species Generation and ERK1/2 Pathway Inhibition

Yang

Xiong

Luo

et al. 2015

Cell Physiol Biochem

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“…Equation (11) can be solved for [L] and then substituted into the equation (12), and rearranged to give a quadratic equation with the real root [46,50]: The sum of heat evolutions following the i th titration step, q i , can be expressed as…”

Section: Ligand Binding In One Binding Site (1:1 Stochiometry)mentioning

confidence: 99%

“…Thermodynamic analysis of the observed heat effects that permits quantitative characterization of the energetic processes is associated with the binding reaction. ITC gives invaluable information about biomacromolecule-ligand interaction [6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23], protein denaturation [24][25][26][27][28], allosteric transition [29][30], enzyme inhibition [31][32][33][34][35], quality, safety and shelf-life of materials and material stability [36][37][38][39][40][41]. Different methods have been reported for data analysis of ligand binding study by ITC [42][43][44][45][46][47][48][49][50][51][52]…”

Section: Introductionmentioning

confidence: 99%

A review on the ligand binding studies by isothermal titration calorimetry

Saboury

2006

JICS

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Thermodynamics of biomacromolecule ligand interaction is very important to understand the structure function relationship in proteins. One of the most powerful techniques useful to obtain additional information about the structure of proteins in biophysical chemistry field is isothermal titration calorimetry (ITC). An ITC experiment is a titration of a biomacromolecule solution by a solution containing a reactant (ligand) at constant temperature to obtain the exchanged heat of the reaction. The total concentration of ligand is the independent variable under experimental control. There are many reports on data analysis for ITC to find the number of binding sites (g), the equilibrium constant (K), the Gibbs free energy of binding process (ΔG), the enthalpy of binding (ΔH) and the entropy of binding (ΔS). Moreover, ITC gives information about the type of reaction, electrostatic and hydrophobic interactions, including determination of cooperativity characterization in binding process by calculating the Hill coefficient (n). A double reciprocal plot and a graphical fitting method are two simple methods used in the enzyme inhibition and metal binding to a protein. Determination of a binding isotherm needs more ITC experiments and more complex data analysis. Protein denaturation by ligand includes two processes of binding and denaturation so that ITC data analysis are more complex. However, the enthalpy of denaturation process obtained by ITC help to understand the fine structure of a protein.

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“…Isothermal titration calorimetry (ITC) gives invaluable information about biomacromolecule-ligand interaction, [1][2][3][4][5][6][7][8][9] protein denaturation, [10][11][12][13][14] kinetic parameters 15 and enzyme inhibition. [16][17][18][19][20] The correlation of structural and calorimetric measurements is one of the fundamental areas of advance incorporating ITC data.…”

Section: Introductionmentioning

confidence: 99%

Thermodynamic Study of Myelin Basic Protein upon Interaction with [Hg²⁺] Using Extension Solvation Model

et al. 2010

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Mercury ion interaction with myelin basic protein (MBP) was studied at 300 K in 30 mmol/L tris buffer, pH＝7 by isothermal titration calorimetry (ITC). An extended solvation model was used for Hg 2＋＋MBP interaction over the whole range of Hg 2＋ concentrations. The binding parameters recovered from the solvation model were attributed to the structural changes of MBP due to its interaction with mercury ion. It was found that mercury ion acted as a noncooperative effector of MBP, and there is a set of two identical and independent binding sites for Hg 2＋ ions.The dissociation equilibrium constant is 97.6 µmol/L. The molar enthalpy change of binding is -11.25 kJ•mol -1 .

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Studies on mechanism of 8-methoxypsoralen–DNA interaction in the dark

Cited by 37 publications

References 32 publications

8-Methoxypsoralen Induces Intrinsic Apoptosis in HepG2 Cells: Involvement of Reactive Oxygen Species Generation and ERK1/2 Pathway Inhibition

8-Methoxypsoralen Induces Intrinsic Apoptosis in HepG2 Cells: Involvement of Reactive Oxygen Species Generation and ERK1/2 Pathway Inhibition

A review on the ligand binding studies by isothermal titration calorimetry

Thermodynamic Study of Myelin Basic Protein upon Interaction with [Hg²⁺] Using Extension Solvation Model

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Studies on mechanism of 8-methoxypsoralen–DNA interaction in the dark

Cited by 37 publications

References 32 publications

8-Methoxypsoralen Induces Intrinsic Apoptosis in HepG2 Cells: Involvement of Reactive Oxygen Species Generation and ERK1/2 Pathway Inhibition

8-Methoxypsoralen Induces Intrinsic Apoptosis in HepG2 Cells: Involvement of Reactive Oxygen Species Generation and ERK1/2 Pathway Inhibition

A review on the ligand binding studies by isothermal titration calorimetry

Thermodynamic Study of Myelin Basic Protein upon Interaction with [Hg2+] Using Extension Solvation Model

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Thermodynamic Study of Myelin Basic Protein upon Interaction with [Hg²⁺] Using Extension Solvation Model