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2 results on '"cantharidin and norcantharidin"'

1. Inhibition of MZF1/c-MYC Axis by Cantharidin Impairs Cell Proliferation in Glioblastoma.

Author

Wang, Chie-Hong, Wu, Hsuan-Cheng, Hsu, Chen-Wei, Chang, Yun-Wei, Ko, Chiung-Yuan, Hsu, Tsung-I, Chuang, Jian-Ying, Tseng, Tsui-Hwa, and Wang, Shao-Ming

Subjects
*CELL proliferation, *ZINC-finger proteins, *CANCER cell proliferation, *GLIOBLASTOMA multiforme, *INHIBITION of cellular proliferation, *ASTROCYTES
Abstract

Myeloid zinc finger 1 (MZF1), also known as zinc finger protein 42, is a zinc finger transcription factor, belonging to the Krüppel-like family that has been implicated in several types of malignancies, including glioblastoma multiforme (GBM). MZF1 is reportedly an oncogenic gene that promotes tumor progression. Moreover, higher expression of MZF1 has been associated with a worse overall survival rate among patients with GBM. Thus, MZF1 may be a promising target for therapeutic interventions. Cantharidin (CTD) has been traditionally used in Chinese medicine to induce apoptosis and inhibit cancer cell proliferation; however, the mechanism by which CTD inhibits cell proliferation remains unclear. In this study, we found that the expression of MZF1 was higher in GBM tissues than in adjacent normal tissues and low-grade gliomas. Additionally, the patient-derived GBM cells and GBM cell lines presented higher levels of MZF1 than normal human astrocytes. We demonstrated that CTD had greater anti-proliferative effects on GBM than a derivative of CTD, norcantharidin (NCTD). MZF1 expression was strongly suppressed by CTD treatment. Furthermore, MZF1 enhanced the proliferation of GBM cells and upregulated the expression of c-MYC, whereas these effects were reversed by CTD treatment. The results of our study suggest that CTD may be a promising therapeutic agent for patients with GBM and suggest a promising direction for further investigation. [ABSTRACT FROM AUTHOR]

Published
2022
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2. Cantharidin and norcantharidin inhibit the ability of MCF-7 cells to adhere to platelets via protein kinase C pathway-dependent downregulation of α2 integrin

Author

Kai Chen, Zhenyu Li, Xin Xie, Min Tao, Qiong-Yan Zhang, Fei-Ran Gong, Wei Li, Yixiang Mao, Liu-Mei Shou, Lian Lian, and Kesheng Dai

Subjects
Blood Platelets, Cancer Research, Blotting, Western, Integrin alpha2, Down-Regulation, Apoptosis, Breast Neoplasms, Biology, cantharidin and norcantharidin, Real-Time Polymerase Chain Reaction, chemistry.chemical_compound, Platelet Adhesiveness, breast cancer, Cell Adhesion, Humans, RNA, Messenger, Enzyme Inhibitors, RNA, Small Interfering, Cell adhesion, Protein Kinase C, Cell Proliferation, platelet, Cantharidin, Wound Healing, Norcantharidin, integrin α2, Cell growth, Reverse Transcriptase Polymerase Chain Reaction, protein phosphatase 2A, Transcription Factor RelA, General Medicine, Articles, Cell cycle, Bridged Bicyclo Compounds, Heterocyclic, Flow Cytometry, Surface coating, Oncology, MCF-7, chemistry, Cancer cell, Cancer research, MCF-7 Cells, Female
Abstract

Cancer metastasis is a highly coordinated and dynamic multistep process in which cancer cells interact with a variety of host cells. Morphological studies have documented the association of circulating tumor cells with host platelets, where a surface coating of platelets protects tumor cells from mechanical trauma and the immune system. Cantharidin is an active constituent of mylabris, a traditional Chinese medicine. Cantharidin and norcantharidin are potent protein phosphatase 2A (PP2A) inhibitors that exhibit in vitro and in vivo antitumor activity against several types of cancer, including breast cancer. We investigated whether cantharidin and norcantharidin could repress the ability of MCF-7 breast cancer cells to adhere to platelets. Using MTT, clone formation, apoptosis, adhesion and wound-healing assays, we found that cantharidin and norcantharidin induced apoptosis and repressed MCF-7 cell growth, adhesion and migration. Moreover, we developed a flow cytometry-based analysis of tumor cell adhesion to platelets. We proved that cantharidin and norcantharidin repressed MCF-7 cell adhesion to platelets through downregulation of α2 integrin, an adhesion molecule present on the surface of cancer cells. The repression of α2 integrin expression was found to be executed through the protein kinase C pathway, the activation of which could have been due to PP2A inhibition.

Published
2013

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