Open Access Article
Arun K. B.a,
Aravind Madhavanb,
Reshmitha T. R.ac,
Sithara Thomasac and
P. Nisha*ac
aAgro Processing and Technology Division, National Institute for Interdisciplinary Science and Technology (CSIR-NIIST), Thiruvananthapuram-695019, Kerala, India. E-mail: bp.nisha@yahoo.com; Tel: +91 471 2515348
bMicrobial Processes and Technology Division, National Institute for Interdisciplinary Science and Technology (CSIR-NIIST), Thiruvananthapuram-695019, Kerala, India
cAcademy of Scientific and Innovative Research (AcSIR), New Delhi 110001, India
First published on 26th March 2026
Correction and removal of expression of concern for ‘Musa paradisiaca inflorescence induces human colon cancer cell death by modulating cascades of transcriptional events’ by Arun K. B. et al., Food Funct., 2018, 9, 511–524, https://doi.org/10.1039/C7FO01454F.
In the published data, a single β-actin blot was used as the loading control for caspase-3 and cleaved caspase-3, as well as for PARP and cleaved PARP. In repeated experiments, separate β-actin blots were used to normalize caspase-3, cleaved caspase-3, PARP, and cleaved PARP, even though the protein samples were obtained from the same HT-29 cell source. This approach was adopted to ensure improved accuracy and clarity in densitometric analysis and represents a more careful normalization strategy. In addition, the originally published figure did not clearly display molecular weight markers, which are necessary for accurate identification of the detected protein bands. The revised data confirm the original conclusions of the study, demonstrating that the methanol extract of plantain inflorescence induces apoptosis in HT-29 colon cancer cells. The figure should have been as shown here, with revised representative Western blot images including molecular weight markers and corresponding densitometric analyses normalized to individual β-actin controls. The authors apologise for any inconvenience caused.
The Methodology section has been updated and the first sentence of the Results in 3.9 Western blot analysis section has been corrected.
Methodology
Cells (1 × 105) were seeded in a 24-well culture plate for 1 day before treatment with the PI methanol extract. After 24 h incubation, the cells were collected and lysed for Western blot analysis. Antibodies specific to β-actin, BCL2, BAX, caspase 3, cleaved caspase 3, PARP, and cleaved PARP were used. After cell lysis, the protein concentration was determined with the Bradford method, and 40 μg of proteins were separated on 10% SDS polyacrylamide gel and transferred to a PVDF transfer membrane (Immobilon P™, Millipore®, USA). For immunoblotting, primary antibodies (1
:
1000) and IgG-HRP secondary antibody (1
:
2000) were used. After washing with wash buffer, the blots were developed using an enhanced chemiluminescence (ECL) substrate according to the manufacturer's instructions (Clarity Western ECL, Bio-Rad, USA). The pixel densities of specific protein bands were compared with the housekeeping gene β-actin using ImageJ software and were plotted to obtain graphs.
Results
The effects of PI methanol extract on the expression of various proteins involved in apoptosis were analyzed by Western blot analysis (Fig. 5).
An independent expert has viewed the corrected images and has concluded that they are consistent with the discussions and conclusions presented.
This correction supersedes the information provided in the expression of concern related to this article.
The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.
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