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Literature summary for 2.1.1.319 extracted from

  • Shen, Y.; Zhong, J.; Liu, J.; Liu, K.; Zhao, J.; Xu, T.; Zeng, T.; Li, Z.; Chen, Y.; Ding, W.; Wen, G.; Zu, X.; Cao, R.
    Protein arginine N-methyltransferase2 reverses tamoxifen resistance in breast cancer cells through suppression of ER-alpha36 (2018), Oncol. Rep., 39, 2604-2612 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Homo sapiens P55345
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-

Synonyms

Synonyms Comment Organism
PRMT2
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 Homo sapiens
protein arginine N-methyltransferase 2
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 Homo sapiens

General Information

General Information Comment Organism
drug target investigation of the role of the enzyme (PRMT2) in breast cancer progression and for developing a new endocrine therapeutic strategy for breast cancer patients with tamoxifen resistance Homo sapiens
metabolism tamoxifen treatment induces a decrease in the enzyme (PRMT2) and an increase in ER-alpha36 as well as ER-alpha36-mediated non-genomic effect in MDA-MB-231 cells, which are relatively resistant to tamoxifen by contrast to MCF-7 cells. PRMT2 is able to interact with ER-alpha36 directly, suppress ER-alpha36 and downstream PI3K/Akt and MAPK/ERK signaling, reversing the tamoxifen resistance of breast cancer cells Homo sapiens