Histone Demethylase JMJD2D Interacts With β-Catenin to Induce Transcription and Activate Colorectal Cancer Cell Proliferation and Tumor Growth in Mice

Peng, Kesong; Kou, Lele; Yu, Li; Bai, Chaonan; Li, Ming; Mo, Pingli; Li, Wengang; Yu, Chundong

doi:10.1053/j.gastro.2018.11.036

Cited by 88 publications

(83 citation statements)

References 36 publications

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“…A study showed that the expression of PCNA, Cyclin-D1, MMP-2, and MMP-9 genes can induce the formation of colorectal cancer and promote cancer cell proliferation, migration, and invasion [23], suggesting that these genes may be closely related to cell proliferation and migration. Some other studies reported that PCNA and Cyclin-D1 mainly regulate cell proliferation and that MMP-2 and MMP-9 play important roles in cell migration and invasion [24,25].…”

Section: Discussionmentioning

confidence: 99%

Advanced Glycation End Products Induce Proliferation and Migration of Human Aortic Smooth Muscle Cells through PI3K/AKT Pathway

Yuan

Hou

et al. 2020

BioMed Research International

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Advanced glycation end products (AGEs) have been widely regarded as an important inducing factor in the pathogenesis of diabetic arteriosclerosis, and the proliferation and migration of vascular smooth muscle cells (VSMCs) are also involved in this process. However, it is not clear whether AGEs promote atherosclerosis by inducing the proliferation and migration of VSMCs. To figure out this question, this study investigated the effects of AGEs on the proliferation and migration of human aorta vascular smooth muscle cells (HASMCs) and the underlying mechanisms. This study evaluated the effects of different concentrations of AGEs on cell proliferation and migration. CCK8, transwell, and western blotting assays demonstrated that AGEs significantly increased cell proliferation and migration in a concentration-dependent manner and that the optimal proproliferative and promigratory concentrations of AGEs were 10 mg/L and 20 mg/L, respectively. AGE-induced cell proliferation, migration, and expression of filament actin (F-actin) were markedly attenuated by a PI3K inhibitor (LY2940002). Additionally, the phosphorylation of AKT was reduced when the receptor of advanced glycation end product (RAGE) gene was silenced by lentivirus transfection, which led to a concomitant reduction of the expression of proliferation and migration-related proteins. These data indicate that AGEs may activate the PI3K/AKT pathway through RAGE and thus facilitate the proliferation and migration of HASMCs.

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Section: Discussionmentioning

confidence: 99%

Advanced Glycation End Products Induce Proliferation and Migration of Human Aortic Smooth Muscle Cells through PI3K/AKT Pathway

Yuan

Hou

et al. 2020

BioMed Research International

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“…KDM4D stimulates p53 transcriptional activity and target gene expression by decreasing H3K9me3 levels at the p53 promoter . Expression levels of KMD4D are higher in human colorectal tumors than healthy colon and positively correlated with proliferating cell nuclear antigen expression . KDM4D‐knockout mice and wild‐type mice treated with the KDM4D inhibitor 5‐chloro‐8‐hydroxyquinoline develop fewer colitis‐associated colorectal tumors than controls.…”

Section: Altered Expression and Functions Of Kdm4s In Cancermentioning

confidence: 99%

“…While single knockout (KO) mice for Kdm4a-Kdm4d and double knockout mice for Kdm4a/Kdm4b and Kdm4b/ Kdm4c are viable, Kdm4a/Kdm4c double-and Kdm4a/ Kdm4b/Kdm4c triple-knockout mice are embryonic lethal, suggesting functional redundancy within the KDM4 family. [14][15][16][17] Kdm4a/Kdm4b/Kdm4c triple-knockout perturb the progression of acute myeloid leukemia (AML) in mice, whereas Kdm4c single knockout does not have any effect, indicating that KDM4 catalytic activity is required for the survival of AML cells. 14 Knockdown of KDM4B, KDM4C, and KDM4D in xenograft mice inhibits the proliferation of breast cancer, 18 AML, 19 and colorectal cancer (CRC) cells, 17 respectively.…”

Section: Introductionmentioning

confidence: 99%

“…[14][15][16][17] Kdm4a/Kdm4b/Kdm4c triple-knockout perturb the progression of acute myeloid leukemia (AML) in mice, whereas Kdm4c single knockout does not have any effect, indicating that KDM4 catalytic activity is required for the survival of AML cells. 14 Knockdown of KDM4B, KDM4C, and KDM4D in xenograft mice inhibits the proliferation of breast cancer, 18 AML, 19 and colorectal cancer (CRC) cells, 17 respectively. Also, Kdm4d knockout mice develop fewer colitis-associated colorectal tumors than controls.…”

Section: Introductionmentioning

confidence: 99%

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Advances in histone demethylase KDM4 as cancer therapeutic targets

et al. 2020

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The KDM4 subfamily H3K9 histone demethylases are epigenetic regulators that control chromatin structure and gene expression by demethylating histone H3K9, H3K36, and H1.4K26. The KDM4 subfamily mainly consists of four proteins (KDM4A‐D), all harboring the Jumonji C domain (JmjC) but with differential substrate specificities. KDM4A‐C proteins also possess the double PHD and Tudor domains, whereas KDM4D lacks these domains. KDM4 proteins are overexpressed or deregulated in multiple cancers, cardiovascular diseases, and mental retardation and are thus potential therapeutic targets. Despite extensive efforts, however, there are very few KDM4‐selective inhibitors. Defining the exact physiological and oncogenic functions of KDM4 demethylase will provide the foundation for the discovery of novel potent inhibitors. In this review, we focus on recent studies highlighting the oncogenic functions of KDM4s and the interplay between KDM4‐mediated epigenetic and metabolic pathways in cancer. We also review currently available KDM4 inhibitors and discuss their potential as therapeutic agents for cancer treatment.

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“…Except for the above-mentioned proteins, other proteins, such as Wnt4, ring finger protein 43 (RNF43) [42], zinc and ring finger 3 [43], serine/threonine kinases [44], cellular homologue of myelocytomatosis viral oncogene (c-Myc), the cell cycle regulator D1 (cyclin D1) [45], surviving, Mitogen-activated protein kinase 1 as well as CK1e and traf2and-nck-interacting kinase, have also been discovered to be closely associated with the Wnt signaling pathway, while different proteins appear to play different roles in biochemical signaling mechanisms. Moreover, a series of receptors are also involved in the Wnt/β-catenin pathway.…”

Section: Relevant Proteins and Receptors In The Wnt/β-catenin Pathwaymentioning

confidence: 99%

Natural products against renin-angiotensin system for antifibrosis therapy

Yang

Chen

Liu

et al. 2019

European Journal of Medicinal Chemistry

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Histone Demethylase JMJD2D Interacts With β-Catenin to Induce Transcription and Activate Colorectal Cancer Cell Proliferation and Tumor Growth in Mice

Cited by 88 publications

References 36 publications

Advanced Glycation End Products Induce Proliferation and Migration of Human Aortic Smooth Muscle Cells through PI3K/AKT Pathway

Advanced Glycation End Products Induce Proliferation and Migration of Human Aortic Smooth Muscle Cells through PI3K/AKT Pathway

Advances in histone demethylase KDM4 as cancer therapeutic targets

Natural products against renin-angiotensin system for antifibrosis therapy

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