Please use this identifier to cite or link to this item:
Title: Vitamin C enhances co-localization of novel TET1 nuclear bodies with both Cajal and PML bodies in colorectal cancer cells
Authors: El Osmani, Nour
Prévostel, Corinne
Picque Lasorsa, Laurence
El Harakeh, Mohammad
Radwan, Zeina
Mawlawi, Hiba
El Sabban, Marwan
Shirinian, Margret
Dassouki, Zeina
Affiliations: Department of Medical Laboratory Sciences 
Keywords: 5hmC
Cajal bodies
PML bodies
Nuclear bodies
Partner proteins
vitamin C
Issue Date: 2024-12
Publisher: National Library of Medicine
Part of: Epigenetics
Volume: 19
Issue: 1
Deregulation of ten-eleven Translocation protein 1 (TET1) is commonly reported to induce imbalances in gene expression and subsequently to colorectal cancer development (CRC). On the other hand, vitamin C (VitC) improves the prognosis of colorectal cancer by reprogramming the cancer epigenome and limiting chemotherapeutic drug resistance events. In this study, we aimed to characterize TET1-specific subcellular compartments and evaluate the effect of VitC on TET1 compartmentalization in colonic tumour cells. We demonstrated that TET1 is concentrated in coarse nuclear bodies (NB) and 5-hydroxymethylcytosine (5hmC) in foci in colorectal cancer cells (HCT116, Caco-2, and HT-29). To our knowledge, this is the first report of a novel intracellular localization profile of TET1 and its demethylation marker, 5hmC, in CRC cells. Interestingly, we found that TET1-NBs frequently interacted with Cajal bodies, but not with promyelocytic leukaemia (PML) bodies. In addition, we report that VitC treatment of HCT116 cells induces 5hmC foci biogenesis and triggers 5hmC marks to form active complexes with nuclear body components, including both Cajal and PML proteins. Our data highlight novel NB-concentrating TET1 in CRC cells and demonstrate that VitC modulates TET1-NBs' interactions with other nuclear structures. These findings reveal novel TET1-dependent cellular functions and potentially provide new insights for CRC management.
DOI: 10.1080/15592294.2024.2337142
Open URL: Link to full text
Type: Journal Article
Appears in Collections:Department of Medical Laboratory Sciences

Show full item record

Record view(s)

checked on May 25, 2024

Google ScholarTM


Dimensions Altmetric

Dimensions Altmetric

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.