The phosphorylation status of VASP at serine 322 can be predictive for aggressiveness of invasive ductal carcinoma

Oncotarget. 2015 Oct 6;6(30):29740-52. doi: 10.18632/oncotarget.4965.

Abstract

Vasodilator-stimulated phosphoprotein (VASP) signaling is critical for dynamic actin reorganization processes that define the motile phenotype of cells. Here we show that VASP is generally highly expressed in normal breast tissue and breast cancer. We also show that the phosphorylation status of VASP at S322 can be predictive for breast cancer progression to an aggressive phenotype. Our data indicate that phosphorylation at S322 is gradually decreased from normal breast to DCIS, luminal/ER+, HER2+ and basal-like/TN phenotypes. Similarly, the expression levels of PKD2, the kinase that phosphorylates VASP at this site, are decreased in invasive ductal carcinoma samples of all three groups. Overall, the phosphorylation status of this residue may serve as an indicator of aggressiveness of breast tumors.

Keywords: VASP; breast cancer; invasive; phosphorylation.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Breast Neoplasms / genetics
  • Breast Neoplasms / metabolism*
  • Breast Neoplasms / pathology
  • Carcinoma, Ductal / genetics
  • Carcinoma, Ductal / metabolism*
  • Carcinoma, Ductal / pathology
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism*
  • Cell Line
  • Cell Line, Tumor
  • Cell Movement / genetics
  • Disease Progression
  • HeLa Cells
  • Humans
  • Immunoblotting
  • Immunohistochemistry
  • Kaplan-Meier Estimate
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Microscopy, Confocal
  • Mutation
  • Neoplasm Invasiveness
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Prognosis
  • Protein Kinase D2
  • Protein Kinases / genetics
  • Protein Kinases / metabolism
  • Serine / genetics
  • Serine / metabolism*
  • Tissue Array Analysis

Substances

  • Cell Adhesion Molecules
  • Microfilament Proteins
  • Phosphoproteins
  • Protein Kinase D2
  • vasodilator-stimulated phosphoprotein
  • Serine
  • Protein Kinases