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May 7, 2026Journal of Biochemical and Molecular Toxicology0 citations

Patulin Affects the Hydroxylation of Vitamin D by Downregulating 25‐hydroxylase (CYP2R1) and 25‐hydroxyvitamin D 1‐alpha‐hydroxylase (CYP27B1) Expression and Interfering Their Substrate Binding Sites

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SLShangyun LuJGJing GaoHZHuixia Zhang

Key Points

  • This study aims to investigate how patulin influences the metabolism of vitamin D by affecting specific enzymes involved in its activation.
  • Examined the effects of patulin on the expression of 25-hydroxylase (CYP2R1) and 25-hydroxyvitamin D 1-alpha-hydroxylase (CYP27B1).
  • Evaluated the impact of patulin on substrate binding sites and hydroxylation processes in liver and kidney models.
  • Patulin downregulated CYP2R1 expression, leading to impaired conversion of vitamin D to its active forms.
  • CYP27B1 expression was also decreased, further affecting vitamin D metabolism.
  • Resulting deficiencies in activated vitamin D products 25(OH)D and 1,25(OH)2D were observed, correlating with potential health risks.

Abstract

ABSTRACT Patulin (PAT) is a mycotoxin that grows on various fruits and grains, and its toxicity research mainly focuses on organ toxicity. However, the research on its impact on nutritional metabolism is still unclear. Vitamin D is an important nutrient and has been reported to have multiple physiological functions. Vitamin D deficiency has been reported to be associated with the risk of developing diseases such as fatal cancers, autoimmune disorders, cardiovascular disease, neurocognitive function impairment, and type 2 diabetes. However, vitamin D need to be converted into biologically active forms through two steps of hydroxylation in the liver or kidney by 25‐hydroxylase (CYP2R1) and 25‐hydroxyvitamin D 1‐alpha‐hydroxylase (CYP27B1). In this study, we found that PAT can cause liver and kidney injury, and affect the levels of activated vitamin D products 25(OH)D and 1,25(OH) 2 D. Specifically, we demonstrated that PAT affects the hydroxylation of vitamin D by downregulating 25‐hydroxylase (CYP2R1) and 25‐hydroxyvitamin D 1‐alpha‐hydroxylase (CYP27B1) expression and interfering their substrate binding sites. This study can provide a basis for a more comprehensive assessment of the impact of environmental pollution, food safety, and other issues on human health.

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Cite This Study

Lu et al. (2026) studied this question.

synapsesocial.com/papers/69fc2c718b49bacb8b347f15https://doi.org/10.1002/jbt.70877
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