Role of Lamin A and emerin in maintaining nuclear morphology in different subtypes of ovarian epithelial cancer

Watabe, Shiori; Kobayashi, Sayaka; Hatori, Motoaki; Nishijima, Yoshimi; Inoue, N.; Ikota, Hayato; Iwase, Akira; Yokoo, Hideaki; Saio, Masanao

doi:10.3892/ol.2021.13127

Cited by 6 publications

(5 citation statements)

References 28 publications

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“…Given that EMD has more than 30 phosphorylation sites and more than five known O‐GlcNAcylated sites, 9 whether phosphorylation and O‐GlcNAcylation would affect the ubiquitination and ISGylation of EMD, and even other post‐translational modifications are also involved in their dynamic balance, which can be further explored in subsequent studies. Based on the known high expression of EMD in breast cancer and ovarian epithelial cancer, 12,13 we further supplemented the evidence of high expression of EMD in LUAD and clarified the relevant mechanism to a certain extent. These results provide basis for individualized treatment of cancer.…”

Section: Discussionmentioning

confidence: 96%

“…Although EMD has been reported to be highly expressed in some types of tumours, 12,13 its tumour-progression role has not been largely understood. In this study, we observed that the cancer-promoting effect of EMD was achieved by binding and restricting the function of PDHA (Figures 5 and 6).…”

Section: Discussionmentioning

confidence: 99%

“…11 Furthermore, EMD has been implicated in the regulation of gene expression, cellular signalling, and nuclear and genomic structure. 11 Although EMD was highly expressed in various types of cancers including ovarian epithelial cancer 12 and breast cancer, 13 how EMD exerts its ontogenetic role in cancer progression remain largely uncovered.…”

Section: Introductionmentioning

confidence: 99%

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ISGylation of EMD promotes its interaction with PDHA to inhibit aerobic oxidation in lung adenocarcinoma

Zhang

Cui

Cao

et al. 2022

J Cellular Molecular Medi

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Abnormal nuclear structure caused by dysregulation of skeletal proteins is a common phenomenon in tumour cells. However, how skeletal proteins promote tumorigenesis remains uncovered. Here, we revealed the mechanism by which skeletal protein Emerin (EMD) promoted glucose metabolism to induce lung adenocarcinoma (LUAD). Firstly, we identified that EMD was highly expressed and promoted the malignant phenotypes in LUAD. The high expression of EMD might be due to its low level of ubiquitination. Additionally, the ISGylation at lysine 37 of EMD inhibited lysine 36 ubiquitination and upregulated EMD stability. We further explored that EMD could inhibit aerobic oxidation and stimulate glycolysis. Mechanistically, via its β‐catenin interaction domain, EMD bound with PDHA, stimulated serine 293 and 300 phosphorylation and inhibited PDHA expression, facilitated glycolysis of glucose that should enter the aerobic oxidation pathway, and EMD ISGylation was essential for EMD‐PDHA interaction. In clinical LUAD specimens, EMD was negatively associated with PDHA, while positively associated with EMD ISGylation, tumour stage and diameter. In LUAD with higher glucose level, EMD expression and ISGylation were higher. Collectively, EMD was a stimulator for LUAD by inhibiting aerobic oxidation via interacting with PDHA. Restricting cancer‐promoting role of EMD might be helpful for LUAD treatment.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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ISGylation of EMD promotes its interaction with PDHA to inhibit aerobic oxidation in lung adenocarcinoma

Zhang

Cui

Cao

et al. 2022

J Cellular Molecular Medi

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“…A role for LMNA/C in cancer is receiving increasing attention. Evidence implicates LMNA/C in preserving nuclear integrity in ovarian epithelial cancer subtypes [ 88 ] and non-small-cell lung carcinoma cells [ 79 ]. Accordingly, lower LMNA/C levels in invasive breast cancer cells confer increased nuclear deformations enabling enhanced cell invasiveness [ 89 ].…”

Section: Discussionmentioning

confidence: 99%

Restructuring of Lamina-Associated Domains in Senescence and Cancer

Bellanger

Madsen-Østerbye

Galigniana

et al. 2022

Cells

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Induction of cellular senescence or cancer is associated with a reshaping of the nuclear envelope and a broad reorganization of heterochromatin. At the periphery of mammalian nuclei, heterochromatin is stabilized at the nuclear lamina via lamina-associated domains (LADs). Alterations in the composition of the nuclear lamina during senescence lead to a loss of peripheral heterochromatin, repositioning of LADs, and changes in epigenetic states of LADs. Cancer initiation and progression are also accompanied by a massive reprogramming of the epigenome, particularly in domains coinciding with LADs. Here, we review recent knowledge on alterations in chromatin organization and in the epigenome that affect LADs and related genomic domains in senescence and cancer.

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“…The NE controls several cellular processes whose dysregulation is observed in cancer, including genomic stability cell migration and resistance to mechanical stress [7]. Thus, it is not surprising that altered expression of NE components is prevalent in multiple cancer types [8][9][10]. Deregulation of NE proteins results in abnormal nuclei with enlarged size and aberrant shape, a hallmark of cancer cells commonly used for diagnosis [11].…”

Section: Introductionmentioning

confidence: 99%

Altered expression and localization of nuclear envelope proteins in a prostate cancer cell system

Sandoval,

Garrido,

Camacho

et al. 2024

Preprint

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Background. The nuclear envelope (NE), which is composed of the outer and inner nuclear membranes, the nuclear pore complex and the nuclear lamina, regulates a plethora of cellular processes, including those that restrict cancer development (genomic stability, cell cycle regulation, and cell migration). Thus, impaired NE is functionally related to tumorigenesis, and monitoring of NE alterations is used to diagnose cancer. However, the chronology of NE changes occurring during cancer evolution and the connection between them remained to be precisely defined, due to the lack of appropriate cell models. Methods. The expression and subcellular localization of NE proteins (lamins A/C and B1 and the inner nuclear membrane proteins emerin and β-dystroglycan [β-DG]) during prostate cancer progression were analyzed, using confocal microscopy and western blot assays, and a prostate cancer cell system comprising RWPE-1 epithelial prostate cells and several prostate cancer cell lines with different invasiveness. Results. Deformed nuclei and the mislocalization and low expression of lamin A/C, lamin B1, and emerin became more prominent as the invasiveness of the prostate cancer lines increased. Suppression of lamin A/C expression was an early event during prostate cancer evolution, while a more extensive deregulation of NE proteins, including β-DG, occurred in metastatic prostate cells. Conclusion. The RWPE-1 cell line-based system was found to be suitable for the correlation of NE impairment with prostate cancer invasiveness and determination of the chronology of NE alterations during prostate carcinogenesis. Further study of this cell system would help to identify biomarkers for prostate cancer prognosis and diagnosis.

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Role of Lamin A and emerin in maintaining nuclear morphology in different subtypes of ovarian epithelial cancer

Cited by 6 publications

References 28 publications

ISGylation of EMD promotes its interaction with PDHA to inhibit aerobic oxidation in lung adenocarcinoma

ISGylation of EMD promotes its interaction with PDHA to inhibit aerobic oxidation in lung adenocarcinoma

Restructuring of Lamina-Associated Domains in Senescence and Cancer

Altered expression and localization of nuclear envelope proteins in a prostate cancer cell system

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