title: Vitamin D receptor regulates intestinal proteins involved in cell proliferation, migration and stress response.
abstract: BACKGROUND
  Genome-wide association studies found low plasma levels of 25-hydroxyvitamin D and vitamin D receptor (VDR) polymorphisms associated with a higher prevalence of pathological changes in the intestine such as chronic inflammatory bowel diseases.
  
  
  METHODS
  In this study, a proteomic approach was applied to understand the overall physiological importance of vitamin D in the small intestine, beyond its function in calcium and phosphate absorption.
  
  
  RESULTS
  In total, 569 protein spots could be detected by two-dimensional-difference in-gel electrophoresis (2D-DIGE), and 82 proteins were considered as differentially regulated in the intestinal mucosa of VDR-deficient mice compared to that of wildtype (WT) mice. Fourteen clearly detectable proteins were identified by MS/MS and further analyzed by western blot and/or real-time RT-PCR. The differentially expressed proteins are functionally involved in cell proliferation, cell adhesion and cell migration, stress response and lipid transport. Mice lacking VDR revealed higher levels of intestinal proteins associated with proliferation and migration such as the 37/67 kDa laminin receptor, collagen type VI (alpha 1 chain), keratin-19, tropomyosin-3, adseverin and higher levels of proteins involved in protein trafficking and stress response than WT mice. In contrast, proteins that are involved in transport of bile and fatty acids were down-regulated in small intestine of mice lacking VDR compared to WT mice. However, plasma and liver concentrations of cholesterol and triglycerides were not different between the two groups of mice.
  
  
  CONCLUSIONS
  Collectively, these data imply VDR as an important factor for controlling cell proliferation, migration and stress response in the small intestine.
authors.forename: Hagen
authors.initials: H
authors.lastname: Kühne
authors.forename: Alexandra
authors.initials: A
authors.lastname: Schutkowski
authors.forename: Susann
authors.initials: S
authors.lastname: Weinholz
authors.forename: Christina
authors.initials: C
authors.lastname: Cordes
authors.forename: Angelika
authors.initials: A
authors.lastname: Schierhorn
authors.forename: Kristin
authors.initials: K
authors.lastname: Schulz
authors.forename: Bettina
authors.initials: B
authors.lastname: König
authors.affiliation: Institute of Agricultural and Nutritional Sciences, Martin Luther University Halle-Wittenberg, Von-Danckelmann-Platz 2, D-06120 Halle (Saale), Germany. gabriele.stangl@landw.uni-halle.de.
authors.forename: Gabriele I
authors.initials: GI
authors.lastname: Stangl
mesh_terms: D000818:Animals; D002465:Cell Movement; D049109:Cell Proliferation; D005786:Gene Expression Regulation; D007413:Intestinal Mucosa / Q000378:metabolism*; D007421:Intestine, Small / Q000166:cytology / Q000378:metabolism; D008055:Lipids / Q000097:blood; D008099:Liver / Q000378:metabolism; D008297:Male; D020778:Matrix Metalloproteinase 2 / Q000235:genetics / Q000378:metabolism; D051379:Mice; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D018167:Receptors, Calcitriol / Q000502:physiology*; D017474:Receptors, Laminin / Q000235:genetics / Q000378:metabolism; D013312:Stress, Physiological; D059467:Transcriptome
chemical_list: D008055:Lipids; D018167:Receptors, Calcitriol; D017474:Receptors, Laminin; D020778:Matrix Metalloproteinase 2; C522362:Mmp2 protein, mouse