Lectin histochemistry of murine WAP-T mammary cancer reveals similar glycoconjugate changes to those in human breast cancer

Anticancer Res. 2014 Dec;34(12):7045-53.

Abstract

Background: The WAP-T mouse model is an established clinically relevant model of breast cancer. Lectins have been used to study malignant progression in clinical studies. We investigated lectin binding sites to test for the clinical relevance of this model.

Materials and methods: Samples of the WAP-T mouse mammary tissues, from normal tissues to undifferentiated higher tumor grades were stained using an indirect technique with nine different lectins for intensity of lectin binding.

Results: HPA bound to the luminal epithelium in higher tumor grades in a similar pattern to that in human breast cancer. BSA-IB4 bound to luminal epithelium in hyperplasia and increased towards higher grades, comparable to previous clinical studies. PHA-L-binding to myoepithelium and luminal epithelium increased from hyperplasia to higher grades, comparable to findings in human breast cancer.

Conclusion: The results of our study support the hypothesis that lectin binding sites change similarly in WAP-T and human breast cancer, stressing the similarity of this model with the clinical setting.

Keywords: Breast cancer; lectin histochemistry; malignant progression; mouse model.

MeSH terms

  • Animals
  • Binding Sites
  • Breast Neoplasms / metabolism*
  • Breast Neoplasms / pathology
  • Coloring Agents
  • Female
  • Glycoconjugates
  • Humans
  • Hyperplasia
  • Lectins / metabolism*
  • Mammary Neoplasms, Animal / metabolism*
  • Mammary Neoplasms, Animal / pathology
  • Mannose-Binding Lectins / metabolism
  • Mice
  • Neoplasm Grading
  • Phytohemagglutinins / metabolism
  • Plant Lectins / metabolism
  • Protein Binding
  • Ribosome Inactivating Proteins / metabolism
  • Staining and Labeling
  • Tumor Cells, Cultured

Substances

  • Coloring Agents
  • Glycoconjugates
  • Lectins
  • Mannose-Binding Lectins
  • Phytohemagglutinins
  • Plant Lectins
  • Sambucus nigra lectins
  • Ulex europaeus lectins
  • leukoagglutinins, plants
  • snowdrop lectin
  • Ribosome Inactivating Proteins