Evidence map›Paper›PMID 8142256›Full record

ArticleBritish journal of cancer1994

Altered stability of etoposide-induced topoisomerase II-DNA complexes in resistant human leukaemia K562 cells.

M K Ritke, D Roberts, W P Allan, J Raymond, V V Bergoltz, J C Yalowich

Open access · bronzeAbstract read
In one paragraph

Article in British journal of cancer, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.1field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 67 citations in OpenAlex.

  1. Circumvention of Topoisomerase IIMolecular pharmacology · 2024
    Article
  2. Use of CRISPR/Cas9 with Homology-Directed Repair to Gene-Edit Topoisomerase IIThe Journal of pharmacology and experimental therapeutics · 2024
    Article
  3. Article
  4. Effects of hsa-miR-9-3p and hsa-miR-9-5p on Topoisomerase IIThe Journal of pharmacology and experimental therapeutics · 2023
    Article
  5. Review
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  19. Cadmium is a catalytic inhibitor of DNA topoisomerase II.Journal of inorganic biochemistry · 2011
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

M K RitkeDepartment of Pharmacology, University of Pittsburgh School of Medicine, Pennsylvania 15261.
D Roberts
W P Allan
J Raymond
V V Bergoltz
J C Yalowich
University of Pittsburgh · USSt. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SUZANNE J. BAKER · 1985 to 2026
$166.9M
RELATION OF VM-26 RESISTANCE TO MULTIDRUG RESISTANCER01CA039426 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI ROBERTS, DE WAYNE · 1985 to 1987
–
MECHANISMS AND MODULATION OF ETOPOSIDE--VP-16 RESISTANCER01CA051657 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI YALOWICH, JACK C. · 1989 to 1991
–
NCI NIH HHS CA-21765NCI NIH HHS CA-39426NCI NIH HHS CA-51657
6 · The paper itself

Abstract

K562 leukaemia cells were selected for resistance using 0.5 microM etoposide (VP-16). Cloned K/VP.5 cells were 30-fold resistant to growth inhibition by VP-16 and 5- to 13-fold resistant to m-AMSA, adriamycin and mitoxantrone. K/VP.5 cells did not overexpress P-glycoprotein; VP-16 accumulation was similar to that in K562 cells. VP-16-induced DNA damage was reduced in cells and nuclei from K/VP.5 cells compared with K562 cells. Topoisomerase II protein was reduced 3- to 7-fold and topoisomerase II alpha and topoisomerase II beta mRNAs were each reduced 3-fold in resistant cells. After drug removal, VP-16-induced DNA damage disappeared 1.7 times more rapidly and VP-16-induced DNA-topoisomerase II adducts dissociated 1.5 times more rapidly in K/VP.5 cells than in K562 cells. ATP (1 mM) was more effective in enhancing VP-16-induced DNA damage in nuclei isolated from sensitive cells than in nuclei from resistant cells. In addition, ATP (0.3-5 mM) stimulated VP-16-induced DNA-topoisomerase II adducts to a greater extent in K562 nuclei than in K/VP.5 nuclei. Taken together, these results indicate that resistance to VP-16 in a K562 subline is associated with a quantitative reduction in topoisomerase II protein and, in addition, a distinct qualitative alteration in topoisomerase II affecting the stability of drug-induced DNA-topoisomerase II complexes.

Indexed as

Antineoplastic AgentsCell NucleusDNA DamageDNA, NeoplasmDNA Topoisomerases, Type IIDrug ResistanceEtoposideHumansLeukemia, Myelogenous, Chronic, BCR-ABL PositiveRNA, NeoplasmTopoisomerase II InhibitorsTumor Cells, CulturedAntineoplastic AgentsDNA, NeoplasmDNA Topoisomerases, Type IIEtoposideRNA, NeoplasmTopoisomerase II Inhibitors

Identifiers

PMID8142256
PMCPMC1968798
OpenAlexW2091418004

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.