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Zinc finger protein SNAI1, commonly known as Snail, is a master transcription factor that orchestrates the epithelial-mesenchymal transition (EMT), a process where epithelial cells lose their polarity and adhesion to become migratory mesenchymal cells (UniProt P23333). While essential for embryonic development and wound healing, SNAI1 is pathologically reactivated in many cancers, where it promotes tumor invasion, metastasis, and resistance to apoptosis (PubMed: 25605116). SNAI1 primarily functions by binding to E-box elements in the promoter of the E-cadherin gene (CDH1), leading to its transcriptional repression and the subsequent breakdown of cell-cell junctions (PubMed: 31430190). Targeting SNAI1 mRNA using nucleic acid-based therapeutics, such as small interfering RNAs (siRNAs) or antisense oligonucleotides (ASOs), aims to silence the expression of this transcription factor at the pre-translational level to inhibit metastatic progression. Although no SNAI1-targeting drugs are currently FDA-approved, numerous preclinical studies have demonstrated that reducing SNAI1 levels can sensitize cancer cells to chemotherapy and limit the spread of solid tumors (PubMed: 25605116).
RNA interference or antisense-mediated degradation of SNAI1 mRNA to prevent the translation of the Snail protein.
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