Kindlin-2 could influence breast nodule elasticity and improve lymph node metastasis in invasive breast cancer

Sci Rep. 2017 Jul 28;7(1):6753. doi: 10.1038/s41598-017-07075-1.

Abstract

This study investigated the relationship between quantitative parameters of shear wave elastography (SWE, maximum elasticity [Emax], minimum elasticity [Emin], mean elasticity [Emean]), collagen intensity and Kindlin-2 expression in benign and malignant breast nodules, and if Kindlin-2 expression is related with lymph node metastasis. A total of 102 breast nodules from 102 patients were included in our study who underwent ultrasound elastography before surgery or core needle biopsy. There was a significant difference between benign and malignant breast nodules in Emax, Emean, collagen intensity and Kindlin-2 expression, but it had no difference in Emin. Collagen intensity and Kindlin-2 expression both correlated positively with Emax, but not with Emean. Among 38 malignant breast nodules, the average Emax of the metastasis group was higher than that of the non-metastasis group, but it had no statistical significance. Compared with the non-metastasis group, Kindlin-2 expression was considerably higher in the metastasis group. However, there was no difference in collagen intensity between the metastasis group and the non-metastasis group. In conclusion, Kindlin-2 and collagen might contribute to breast nodule elasticity through molecular mechanisms. In breast cancer, overexpression of Kindlin-2 might be a risk factor for lymph node metastasis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Breast Neoplasms / diagnosis
  • Breast Neoplasms / metabolism*
  • Breast Neoplasms / pathology*
  • Collagen / metabolism
  • Elasticity Imaging Techniques
  • Elasticity*
  • Female
  • Focal Adhesion Protein-Tyrosine Kinases / metabolism
  • Humans
  • Lymphatic Metastasis / pathology*
  • Membrane Proteins / metabolism*
  • Middle Aged
  • Neoplasm Invasiveness
  • Neoplasm Proteins / metabolism*
  • Phosphorylation
  • Smad2 Protein / metabolism

Substances

  • FERMT3 protein, human
  • Membrane Proteins
  • Neoplasm Proteins
  • Smad2 Protein
  • Collagen
  • Focal Adhesion Protein-Tyrosine Kinases