The Anti-Inflammatory Effects of Vitamin D in Tumorigenesis

Int J Mol Sci. 2018 Sep 13;19(9):2736. doi: 10.3390/ijms19092736.


In conjunction with the classical functions of regulating intestinal, bone, and kidney calcium and phosphorus absorption, as well as bone mineralization of vitamin D, the population-based association between low vitamin D status and increased cancer risk is now generally accepted. Inflammation is causally related to oncogenesis. It is widely thought that vitamin D plays an important role in the modulation of the inflammation system by regulating the production of inflammatory cytokines and immune cells, which are crucial for the pathogenesis of many immune-related diseases. Mechanistic studies have shown that vitamin D influences inflammatory processes involved in cancer progression, including cytokines, prostaglandins, MAP kinase phosphatase 5 (MKP5), the nuclear factor kappa B (NF-κB) pathway, and immune cells. Multiple studies have shown that vitamin D has the potential to inhibit tumor development by interfering with the inflammation system. The present review summarizes recent studies of the mechanisms of vitamin D on regulating the inflammation system, which contributes to its potential for cancer prevention and therapy. This review helps answer whether inflammation mediates a causal relationship between vitamin D and tumorigenesis.

Keywords: cytokines; immune cells; inflammation; tumorigenesis; vitamin D.

Publication types

  • Review

MeSH terms

  • Animals
  • Anti-Inflammatory Agents / immunology
  • Anti-Inflammatory Agents / therapeutic use*
  • Carcinogenesis / drug effects*
  • Carcinogenesis / immunology*
  • Dual-Specificity Phosphatases / metabolism
  • Humans
  • Inflammation / prevention & control
  • Mitogen-Activated Protein Kinase Phosphatases / metabolism
  • NF-kappa B / metabolism
  • Vitamin D / immunology
  • Vitamin D / therapeutic use*


  • Anti-Inflammatory Agents
  • NF-kappa B
  • Vitamin D
  • DUSP10 protein, human
  • Mitogen-Activated Protein Kinase Phosphatases
  • Dual-Specificity Phosphatases