Evidence map›Paper›PMID 27622714›Full record

ArticleScientific reports2016

Crocetin exploits p53-induced death domain (PIDD) and FAS-associated death domain (FADD) proteins to induce apoptosis in colorectal cancer.

Pallab Ray, Deblina Guha, Juni Chakraborty, Shuvomoy Banerjee, Arghya Adhikary, Samik Chakraborty, Tanya Das, Gaurisankar Sa

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 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
2.4field-weighted citation impact, top 10% 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, 66 citations in OpenAlex.

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  15. Crocin Promotes Apoptosis in Human EBV-Transformed B-Lymphocyte via Intrinsic Pathway.Mediterranean journal of hematology and infectious diseases · 2021
    Article
  16. Crocetin: A Systematic Review.Frontiers in pharmacology · 2021
    Review
  17. Review
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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

8 authors at 1 institution in 1 country.

Pallab RayDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata 700 054, India.
Deblina GuhaDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata 700 054, India.
Juni ChakrabortyDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata 700 054, India.
Shuvomoy BanerjeeDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata 700 054, India.
Arghya AdhikaryDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata 700 054, India.
Samik ChakrabortyDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata 700 054, India.
Tanya DasDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata 700 054, India.
Gaurisankar SaDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata 700 054, India.
Bose Institute · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tumor suppressor p53 preserves the genomic integrity by restricting anomaly at the gene level. The hotspots for mutation in half of all colon cancers reside in p53. Hence, in a p53-mutated cellular milieu targeting cancer cells may be achievable by targeting the paralogue(s) of p53. Here we have shown the effectiveness of crocetin, a dietary component, in inducing apoptosis of colon cancer cells with varying p53 status. In wild-type p53-expressing cancer cells, p53 in one hand transactivates BAX and in parallel up-regulates p53-induced death domain protein (PIDD) that in turn cleaves and activates BID through caspase-2. Both BAX and t-BID converge at mitochondria to alter the transmembrane potential thereby leading to caspase-9 and caspase-3-mediated apoptosis. In contrast, in functional p53-impaired cells, this phytochemical exploits p53-paralogue p73, which up-regulates FAS to cleave BID through FAS-FADD-caspase-8-pathway. These findings not only underline the phenomenon of functional switch-over from p53 to p73 in p53-impaired condition, but also validate p73 as a promising and potential target for cancer therapy in absence of functional p53.

Indexed as

Antineoplastic Agents, PhytogenicApoptosisbcl-2-Associated X ProteinBH3 Interacting Domain Death Agonist ProteinCarotenoidsCaspase 2Caspase 8Colorectal NeoplasmsCysteine EndopeptidasesDeath Domain Receptor Signaling Adaptor ProteinsFas-Associated Death Domain Proteinfas ReceptorHCT116 CellsHT29 CellsHumansMutationAntineoplastic Agents, PhytogenicBAX protein, humanbcl-2-Associated X ProteinBH3 Interacting Domain Death Agonist ProteinBID protein, humanCarotenoidsCASP2 protein, humanCASP8 protein, humanCaspase 2Caspase 8Cysteine EndopeptidasesDeath Domain Receptor Signaling Adaptor ProteinsFADD protein, humanFas-Associated Death Domain ProteinFAS protein, humanfas ReceptorPIDD1 protein, humanTP53 protein, humanTP73 protein, humantrans-sodium crocetinateTumor Protein p73Tumor Suppressor Protein p53Vitamin A

Identifiers

PMID27622714
PMCPMC5020693
OpenAlexW2519139576

What OpenQuestion holds

Textmetadata
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.