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CYP24A1 mRNA encodes the Cytochrome P450 family 24 subfamily A member 1 enzyme, which is the primary catalyst for the inactivation of the active form of vitamin D, 1,25-dihydroxyvitamin D3 (calcitriol). By performing 24-hydroxylation, the enzyme converts calcitriol into calcitroic acid for excretion, thereby serving as a critical regulator of systemic calcium and phosphate levels (Source: UniProt P24298; PubMed: 21835226). In clinical contexts, the overexpression of CYP24A1 is frequently observed in various malignancies, such as lung and breast cancer, where it depletes local vitamin D levels and potentially facilitates tumor progression by neutralizing vitamin D's anti-proliferative effects (Source: PubMed: 17218402). Conversely, loss-of-function mutations in the CYP24A1 gene lead to idiopathic infantile hypercalcemia, characterized by severe hypercalcemia and nephrocalcinosis due to impaired vitamin D degradation (Source: PubMed: 22451445). Therapeutic strategies targeting CYP24A1 include small molecule inhibitors like CTA018 and experimental RNA-targeted approaches (siRNA/ASOs) aimed at reducing enzyme expression to treat vitamin D deficiency or enhance the efficacy of vitamin D analogs in cancer and chronic kidney disease (Source: PubMed: 25613668). These interventions aim to maintain therapeutic levels of calcitriol while minimizing the risk of hypercalcemia associated with systemic vitamin D administration.
Inhibition of the encoded 24-hydroxylase enzyme to prevent the breakdown of active vitamin D (calcitriol); RNA interference or antisense-mediated knockdown of mRNA to reduce protein expression (Source: PubMed: 25613668).
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