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Behind the scenes of vitamin D binding protein - more than vitamin D binding – Oct 2015

Best Pract Res Clin Endocrinol Metab. 2015 Oct;29(5):773-86. doi: 10.1016/j.beem.2015.06.006. Epub 2015 Jul 2.
Delanghe JR1, Speeckaert R1, Speeckaert MM2.
1 Department of Clinical Chemistry, Ghent University Hospital, Ghent, Belgium.
2 Department of Clinical Chemistry, Ghent University Hospital, Ghent, Belgium; Department of Nephrology, Ghent University Hospital, Ghent, Belgium.

Although being discovered in 1959, the number of published papers in recent years reveals that vitamin D binding protein (DBP), a member of the albuminoid superfamily, is a hot research topic.
Besides the three major phenotypes (

  • DBP1F,
  • DBP1S and
  • DBP2),

more than 120 unique variants have been described of this polymorphic protein.
The presence of DBP has been demonstrated in different body fluids (

  • serum,
  • urine,
  • breast milk,
  • ascitic fluid,
  • cerebrospinal fluid,
  • saliva and
  • seminal fluid) and
  • organs (brain, heart, lungs, kidneys, placenta, spleen, testes and uterus).

Although the major function is binding, solubilization and transport of vitamin D and its metabolites, the name of this glycoprotein hides numerous other important biological functions.

In this review, we will focus on the analytical aspects of the determination of DBP and discuss in detail the multifunctional capacity [

  • actin scavenging,
  • binding of fatty acids,
  • chemotaxis,
  • binding of endotoxins,
  • influence on T cell response and
  • influence of vitamin D binding protein-macrophage activating factor (DBP-MAF) on bone metabolism and cancer]

of this abundant plasma protein.

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