Fol. Biol. 2023, 69, 81-90

https://doi.org/10.14712/fb2023069030081

Homeobox Protein PROX1 Expression is Negatively Regulated by Histone Deacetylase 1 and c-JUN Complex in MDA-MB-231 Human Breast Cancer Cells

Munki Jeong, Euitaek Jung, Sukjin Oh, Soon Young Shin

Department of Biological Sciences, Sanghuh College of Life Sciences, Konkuk University, Seoul 05029, Republic of Korea

Received July 2022
Accepted October 2023

References

1. Benítez, J., Osorio, A., Barroso, A. et al. (1997) A region of allelic imbalance in 1q31–32 in primary breast cancer coincides with a recombination hot spot. Cancer Res. 57, 4217-4220.
2. Bird, A. (2002) DNA methylation patterns and epigenetic memory. Genes Dev. 16, 6-21. <https://doi.org/10.1101/gad.947102>
3. Burke, Z., Oliver, G. (2002) Prox1 is an early specific marker for the developing liver and pancreas in the mammalian foregut endoderm. Mech. Dev. 118, 147-155. <https://doi.org/10.1016/S0925-4773(02)00240-X>
4. Chambers, A. F., Matrisian, L. (1997) Changing views of the role of matrix metalloproteinases in metastasis. J. Natl. Cancer Inst. 89, 1260-1270. <https://doi.org/10.1093/jnci/89.17.1260>
5. Cockett, M. I., Murphy, G., Birch, M. et al. (1998) Matrix metalloproteinases and metastatic cancer. Biochem. Soc. Symp. 63, 295-313.
6. Doe, C. Q., Chu-LaGraff, Q., Wright, D. M. et al. (1991) The prospero gene specifies cell fates in the Drosophila central nervous system. Cell 65, 451-464. <https://doi.org/10.1016/0092-8674(91)90463-9>
7. Elsir, T., Smits, A., Lindström, M. S. et al. (2012) Transcription factor PROX1: its role in development and cancer. Cancer Metastasis Rev. 31, 793-805. <https://doi.org/10.1007/s10555-012-9390-8>
8. Foulkes, W. D., Smith, I. E., Reis-Filho, J. S. (2010) Triple-negative breast cancer. N. Engl. J. Med. 363, 1938-1948. <https://doi.org/10.1056/NEJMra1001389>
9. Fuks, F. (2005) DNA methylation and histone modifications: teaming up to silence genes. Curr. Opin. Genet. Dev. 15, 490-495. <https://doi.org/10.1016/j.gde.2005.08.002>
10. Gramolelli, S., Cheng, J., Martinez-Corral, I. et al. (2018) PROX1 is a transcriptional regulator of MMP14. Sci. Rep. 8, 1-13. <https://doi.org/10.1038/s41598-018-27739-w>
11. Gujral, P., Mahajan, V., Lissaman, A. C. et al. (2020) Histone acetylation and the role of histone deacetylases in normal cyclic endometrium. Reprod. Biol. Endocrinol. 18, 84. <https://doi.org/10.1186/s12958-020-00637-5>
12. Kähäri, V. M., Saarialho-Kere, U. (1999) Trends in molecular medicine: matrix metalloproteinases and their inhibitors in tumour growth and invasion. Ann. Med. 31, 34-45. <https://doi.org/10.3109/07853899909019260>
13. Kudo-Saito, C., Shirako, H., Takeuchi, T. et al. (2009) Cancer metastasis is accelerated through immunosuppression during Snail-induced EMT of cancer cells. Cancer Cell 15, 195-206. <https://doi.org/10.1016/j.ccr.2009.01.023>
14. Lavado, A., Oliver, G. (2007) Prox1 expression patterns in the developing and adult murine brain. Dev. Dyn. 236, 518-524. <https://doi.org/10.1002/dvdy.21024>
15. Liu, Y., Zhu, P., Wang, Y. et al. (2015) Antimetastatic therapies of the polysulfide diallyl trisulfide against triple-negative breast cancer (TNBC) via suppressing MMP2/9 by blocking NF-κB and ERK/MAPK signaling pathways. PLoS One 10, e0123781. <https://doi.org/10.1371/journal.pone.0123781>
16. Liu, Y., Zhang, J.-B., Qin, Y. et al. (2013) PROX1 promotes hepatocellular carcinoma metastasis by way of up‐regulating hypoxia‐inducible factor 1α expression and protein stability. Hepatology 58, 692-705. <https://doi.org/10.1002/hep.26398>
17. Marks, P. A. (2007) Discovery and development of SAHA as an anticancer agent. Oncogene 26, 1351-1356. <https://doi.org/10.1038/sj.onc.1210204>
18. Merino, F., Pospich, S., Raunser, S. (2020) Towards a structural understanding of the remodeling of the actin cytoskeleton. Semin. Cell Dev. Biol. 102, 51-64. <https://doi.org/10.1016/j.semcdb.2019.11.018>
19. Munster, P. N., Troso-Sandoval, T., Rosen, N. et al. (2001) The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells. Cancer Res. 61, 8492-8497.
20. Nan, X., Ng, H. H., Johnson, C. A. et al. (1998) Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature 393, 386-389. <https://doi.org/10.1038/30764>
21. Petrova, T. V., Mäkinen, T., Mäkelä, T. P. et al. (2002) Lymphatic endothelial reprogramming of vascular endothelial cells by the Prox-1 homeobox transcription factor. EMBO J. 21, 4593-4599. <https://doi.org/10.1093/emboj/cdf470>
22. Pinkas, J., Leder, P. (2002) MEK1 signaling mediates transformation and metastasis of EpH4 mammary epithelial cells independent of an epithelial to mesenchymal transition. Cancer Res. 62, 4781-4790.
23. Risebro, C. A., Searles, R. G., Melville, A. A. et al. (2009) Prox1 maintains muscle structure and growth in the developing heart. Development 136, 495-505. <https://doi.org/10.1242/dev.030007>
24. Rudzińska, M., Czarnocka, B. (2020) The impact of transcription factor prospero homeobox 1 on the regulation of thyroid cancer malignancy. Int. J. Mol. Sci. 21, 3220. <https://doi.org/10.3390/ijms21093220>
25. Sanna, M. D., Galeotti, N. (2018) The HDAC1/c-JUN complex is essential in the promotion of nerve injury-induced neuropathic pain through JNK signaling. Eur. J. Pharmacol. 825, 99-106. <https://doi.org/10.1016/j.ejphar.2018.02.034>
26. Sethi, G., Sung, B., Aggarwal, B. B. (2008) TNF: a master switch for inflammation to cancer. Front. Biosci. 13, 5094-5107. <https://doi.org/10.2741/3066>
27. Seto, E., Yoshida, M. (2014) Erasers of histone acetylation: the histone deacetylase enzymes. Cold Spring Harb. Perspect. Biol. 6, a018713. <https://doi.org/10.1101/cshperspect.a018713>
28. Shin, S. Y., Kim, C. G., Jung, Y. J. et al. (2016) The UPR inducer DPP23 inhibits the metastatic potential of MDA-MB-231 human breast cancer cells by targeting the Akt-IKK-NF-κB-MMP-9 axis. Sci. Rep. 6, 34134. <https://doi.org/10.1038/srep34134>
29. Sosa-Pineda, B., Wigle, J. T., Oliver, G. (2000) Hepatocyte migration during liver development requires Prox1. Nat. Genet. 25, 254-255. <https://doi.org/10.1038/76996>
30. Suarez-Carmona, M., Lesage, J., Cataldo, D. et al. (2017) EMT and inflammation: inseparable actors of cancer progression. Mol. Oncol. 11, 805-823. <https://doi.org/10.1002/1878-0261.12095>
31. Versmold, B., Felsberg, J., Mikeska, T. et al. (2007) Epigenetic silencing of the candidate tumor suppressor gene PROX1 in sporadic breast cancer. Int. J. Cancer 121, 547-554. <https://doi.org/10.1002/ijc.22705>
32. West, A. C., Johnstone, R. W. (2014) New and emerging HDAC inhibitors for cancer treatment. J. Clin. Invest. 124, 30-39. <https://doi.org/10.1172/JCI69738>
33. Westermarck, J., Kähäri, V. M. (1999) Regulation of matrix metalloproteinase expression in tumour invasion. FASEB J. 13, 781-792. <https://doi.org/10.1096/fasebj.13.8.781>
34. Wigle, J. T., Chowdhury, K., Gruss, P. et al. (1999) Prox1 function is crucial for mouse lens-fibre elongation. Nat. Genet. 21, 318-322. <https://doi.org/10.1038/6844>
35. Zhang, Y., Weinberg, R. A. (2018) Epithelial-to-mesenchymal transition in cancer: complexity and opportunities. Front. Med. 12, 361-373. <https://doi.org/10.1007/s11684-018-0656-6>
36. Zinovieva, R. D., Duncan, M. K., Johnson, T. R. et al. (1996) Structure and chromosomal localization of the human homeobox gene Prox 1. Genomics 35, 517-522. <https://doi.org/10.1006/geno.1996.0392>
front cover

ISSN 0015-5500 (Print) ISSN 2533-7602 (Online)

Open access journal

Archive