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Calcium-regulated heat-stable protein 1 (CARHSP1) mRNA encodes a cytoplasmic protein, also known as CRHSP-24, which contains a highly conserved cold-shock domain (CSD) (Pfeiffer et al., 2011; PubMed). The encoded protein functions as a critical RNA-binding protein (RBP) that regulates the stability of specific target transcripts, most notably the pro-inflammatory cytokine Tumor Necrosis Factor-alpha (TNF-alpha) (Jiang et al., 2025; PMC). By binding to AU-rich elements in the 3'-untranslated region of TNF-alpha mRNA, CARHSP1 prevents its degradation, thereby ensuring robust cytokine production during inflammatory responses (Pfeiffer et al., 2011; PubMed). Recent research has expanded its role to oncology, demonstrating that CARHSP1 stabilizes IL-17RA mRNA to promote tumor growth, metastasis, and immune evasion in prostate cancer (Jiang et al., 2025; PMC). Additionally, CARHSP1 has been identified as a driver of radioresistance in glioblastoma, where its upregulation activates inflammatory signaling pathways that protect tumor cells from radiation-induced death (Cell Death Dis, 2021; PubMed). Targeting CARHSP1 mRNA using RNA-based therapeutics, such as siRNA or antisense oligonucleotides, represents a promising strategy to modulate these pathways for the treatment of chronic inflammation and resistant cancers (Cell Death Dis, 2021; PubMed). However, therapeutic development must consider the protein's involvement in metabolic processes, including its role as a negative regulator of gluconeogenic genes through interactions with PPAR-alpha (Ma'ayan Lab; GeneCards).
Targeted degradation of the CARHSP1 mRNA transcript via RNA interference or antisense mechanisms to reduce the expression of the CARHSP1 protein, thereby destabilizing downstream pro-inflammatory and oncogenic transcripts.
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