Evidence map›Paper›PMID 26596838›Full record

ArticleTumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine2016

Aspirin acetylates wild type and mutant p53 in colon cancer cells: identification of aspirin acetylated sites on recombinant p53.

Guoqiang Ai, Rakesh Dachineni, D Ramesh Kumar, Srinivasan Marimuthu, Lloyd F Alfonso, G Jayarama Bhat

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In one paragraph

Article in Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.7field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Article
  6. Review
  7. Article
  8. Acetylsalicylic Acid-Primus Inter Pares in Pharmacology.Molecules (Basel, Switzerland) · 2022
    Review
  9. Article
  10. Aspirin Mediates Its Antitumoral Effect Through Inhibiting PTTG1 in Pituitary Adenoma.The Journal of clinical endocrinology and metabolism · 2022
    Article
  11. Review
  12. Review
  13. Review
  14. Review
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  16. Article
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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 3 institutions in 1 country.

Guoqiang AiDepartment of Pharmaceutical Sciences, College of Pharmacy, Avera Health and Sciences Center, South Dakota State University, Brookings, SD, USA.
Rakesh DachineniDepartment of Pharmaceutical Sciences, College of Pharmacy, Avera Health and Sciences Center, South Dakota State University, Brookings, SD, USA.
D Ramesh KumarDepartment of Pharmaceutical Sciences, College of Pharmacy, Avera Health and Sciences Center, South Dakota State University, Brookings, SD, USA.
Srinivasan MarimuthuAyurveda Research Institute for Mother & Child Health Care, Poojapura, Trivandrum, Kerala, India.
Lloyd F AlfonsoSchool of Pharmacy, D'Youville College, 320 Porter Avenue, Buffalo, NY, 14201, USA.
G Jayarama BhatDepartment of Pharmaceutical Sciences, College of Pharmacy, Avera Health and Sciences Center, South Dakota State University, Brookings, SD, USA. Jayarama.gunaje@sdstate.edu.
Avera Health · USD'Youville College · USSouth Dakota State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aspirin's ability to inhibit cell proliferation and induce apoptosis in cancer cell lines is considered to be an important mechanism for its anti-cancer effects. We previously demonstrated that aspirin acetylated the tumor suppressor protein p53 at lysine 382 in MDA-MB-231 human breast cancer cells. Here, we extended these observations to human colon cancer cells, HCT 116 harboring wild type p53, and HT-29 containing mutant p53. We demonstrate that aspirin induced acetylation of p53 in both cell lines in a concentration-dependent manner. Aspirin-acetylated p53 was localized to the nucleus. In both cell lines, aspirin induced p21(CIP1). Aspirin also acetylated recombinant p53 (rp53) in vitro suggesting that it occurs through a non-enzymatic chemical reaction. Mass spectrometry analysis and immunoblotting identified 10 acetylated lysines on rp53, and molecular modeling showed that all lysines targeted by aspirin are surface exposed. Five of these lysines are localized to the DNA-binding domain, four to the nuclear localization signal domain, and one to the C-terminal regulatory domain. Our results suggest that aspirin's anti-cancer effect may involve acetylation and activation of wild type and mutant p53 and induction of target gene expression. This is the first report attempting to characterize p53 acetylation sites targeted by aspirin.

Indexed as

AcetylationAspirinCell Line, TumorCell NucleusColonic NeoplasmsCyclin-Dependent Kinase Inhibitor p21HCT116 CellsHT29 CellsHumansLysineMutant ProteinsProtein Processing, Post-TranslationalProtein TransportRecombinant ProteinsTumor Suppressor Protein p53AspirinCyclin-Dependent Kinase Inhibitor p21LysineMutant ProteinsRecombinant ProteinsTumor Suppressor Protein p53AcetylationAnti-cancer effectsApoptosisAspirinp53

Identifiers

PMID26596838
OpenAlexW2252755405

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.