Inhibition of Topoisomerase II Catalytic Activity by Pyridoacridine Alkaloids from a Cystodytes sp. Ascidian: A Mechanism for the Apparent Intercalator-Induced Inhibition of Topoisomerase II

1994 ◽  
Vol 37 (22) ◽  
pp. 3819-3827 ◽  
Author(s):  
Leonard A. McDonald ◽  
Glenn S. Eldredge ◽  
Louis R. Barrows ◽  
Chris M. Ireland
Keyword(s):  
Catalytic Activity ◽  
Topoisomerase Ii ◽  
Pyridoacridine Alkaloids

Altered catalytic activity of and DNA cleavage by DNA topoisomerase II from human leukemic cells selected for resistance to VM-26

Biochemistry ◽  
1988 ◽  
Vol 27 (24) ◽  
pp. 8861-8869 ◽  
Author(s):  
Mary K. Danks ◽  
Carla A. Schmidt ◽  
Margaret C. Cirtain ◽  
D. Parker Suttle ◽  
William T. Beck
Keyword(s):  
Catalytic Activity ◽  
Dna Cleavage ◽  
Topoisomerase Ii ◽  
Leukemic Cells ◽  
Dna Topoisomerase Ii ◽  
Dna Topoisomerase ◽  
Human Leukemic Cells

Organoplatinum(II) Complexes with Nucleobase Motifs as Inhibitors of Human Topoisomerase II Catalytic Activity

2010 ◽  
Vol 5 (10) ◽  
pp. 2271-2280 ◽  
Author(s):  
Ping Wang ◽  
Chung-Hang Leung ◽  
Dik-Lung Ma ◽  
Wei Lu ◽  
Chi-Ming Che
Keyword(s):  
Catalytic Activity ◽  
Topoisomerase Ii

Inhibition of Topoisomerase II Catalytic Activity by Two Ruthenium Compounds:  A Ligand-Dependent Mode of Action†

Biochemistry ◽  
1999 ◽  
Vol 38 (14) ◽  
pp. 4382-4388 ◽  
Author(s):  
Y. N. Vashisht Gopal ◽  
D. Jayaraju ◽  
Anand K. Kondapi
Keyword(s):  
Catalytic Activity ◽  
Mode Of Action ◽  
Topoisomerase Ii ◽  
Ruthenium Compounds

scholarly journals A noncatalytic function of the topoisomerase II CTD in Aurora B recruitment to inner centromeres during mitosis

2016 ◽  
Vol 213 (6) ◽  
pp. 651-664 ◽  
Author(s):  
Heather Edgerton ◽  
Marnie Johansson ◽  
Daniel Keifenheim ◽  
Soumya Mukherjee ◽  
Jeremy M. Chacón ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Binding Site ◽  
Chromosome Segregation ◽  
Topoisomerase Ii ◽  
Histone H3 ◽  
Aurora B ◽  
Topoisomerase Iiα ◽  
Dna Topoisomerase ◽  
Topo Ii ◽  
Dna Topoisomerase Iiα

Faithful chromosome segregation depends on the precise timing of chromatid separation, which is enforced by checkpoint signals generated at kinetochores. Here, we provide evidence that the C-terminal domain (CTD) of DNA topoisomerase IIα (Topo II) provides a novel function at inner centromeres of kinetochores in mitosis. We find that the yeast CTD is required for recruitment of the tension checkpoint kinase Ipl1/Aurora B to inner centromeres in metaphase but is not required in interphase. Conserved CTD SUMOylation sites are required for Ipl1 recruitment. This inner-centromere CTD function is distinct from the catalytic activity of Topo II. Genetic and biochemical evidence suggests that Topo II recruits Ipl1 via the Haspin–histone H3 threonine 3 phosphorylation pathway. Finally, Topo II and Sgo1 are equally important for Ipl1 recruitment to inner centromeres. This indicates H3 T3-Phos/H2A T120-Phos is a universal epigenetic signature that defines the eukaryotic inner centromere and provides the binding site for Ipl1/Aurora B.

Azacyanines as Novel Topoisomerase II Alpha Inhibitors

2020 ◽  
Vol 17 (5) ◽  
pp. 666-671 ◽  
Author(s):  
Sercan Guloglu ◽  
Fahriye Nur Kirmaci ◽  
Özgül Persil Çetinkol ◽  
Mehrdad Forough ◽  
Aybuke Gulkaya
Keyword(s):  
Catalytic Activity ◽  
Small Molecules ◽  
Topoisomerase Ii ◽  
Chemotherapeutic Agents ◽  
Agarose Gel ◽  
Topoisomerase Iiα ◽  
Topoisomerase Ii Alpha ◽  
Topological Constraints ◽  
Different Types

Introduction: Topoisomerase II alpha (Topo IIα) has become one of the extensively exploited targets in chemotherapy due to its role in regulating the topological constraints of DNA during replication and transcription. Small molecules targeting Topo IIα’s activity such as etoposide (VP-16) and doxorubicin are extensively used in the treatment of many different types of cancer. Objective: Here, the effects of three small molecules, named as azacyanines, on Topo IIα have been assessed. Methods: In-vitro Topoisomerase IIα drug screening kit and agarose gel imaging were used for the assessment of Topo IIα’s activity. Results: Our results revealed that all the azacyanines investigated decreased the catalytic activity of Topo IIα dramatically. More importantly, the decrease in the catalytic activity of Topo IIα in the presence of azacyanines was higher than the presence of VP-16, which is a commercially available chemotherapy drug. Upon further investigation, it has been observed that Azamethyl’s catalytic inhibition of Topo IIα was concentration dependent and the catalytic activity of Topo IIα was almost completely abolished in the presence of 100.0 μM of Azamethyl. Conclusion: These findings reveal the potential of azacyanines as effective Topo IIα inhibitors and chemotherapeutic agents.

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