EPLIN downregulation promotes epithelial-mesenchymal transition in prostate cancer cells and correlates with clinical lymph node metastasis

Oncogene. 2011 Dec 15;30(50):4941-52. doi: 10.1038/onc.2011.199. Epub 2011 May 30.

Abstract

Epithelial-mesenchymal transition (EMT) is a crucial mechanism for the acquisition of migratory and invasive capabilities by epithelial cancer cells. By conducting quantitative proteomics in experimental models of human prostate cancer (PCa) metastasis, we observed strikingly decreased expression of EPLIN (epithelial protein lost in neoplasm; or LIM domain and actin binding 1, LIMA-1) upon EMT. Biochemical and functional analyses demonstrated that EPLIN is a negative regulator of EMT and invasiveness in PCa cells. EPLIN depletion resulted in the disassembly of adherens junctions, structurally distinct actin remodeling and activation of β-catenin signaling. Microarray expression analysis identified a subset of putative EPLIN target genes associated with EMT, invasion and metastasis. By immunohistochemistry, EPLIN downregulation was also demonstrated in lymph node metastases of human solid tumors including PCa, breast cancer, colorectal cancer and squamous cell carcinoma of the head and neck. This study reveals a novel molecular mechanism for converting cancer cells into a highly invasive and malignant form, and has important implications in prognosis and treating metastasis at early stages.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adherens Junctions / metabolism
  • Adherens Junctions / pathology
  • Breast Neoplasms / metabolism
  • Breast Neoplasms / pathology
  • Carcinoma, Squamous Cell / metabolism
  • Carcinoma, Squamous Cell / pathology
  • Colorectal Neoplasms / metabolism
  • Colorectal Neoplasms / pathology
  • Cytoskeletal Proteins / biosynthesis*
  • Down-Regulation*
  • Epithelial-Mesenchymal Transition*
  • Female
  • Gene Expression Regulation, Neoplastic*
  • Head and Neck Neoplasms / metabolism
  • Head and Neck Neoplasms / pathology
  • Humans
  • Lymph Nodes / pathology
  • Lymphatic Metastasis
  • Male
  • Neoplasm Invasiveness
  • Neoplasm Proteins / biosynthesis*
  • Prostatic Neoplasms / metabolism*
  • Prostatic Neoplasms / pathology
  • Signal Transduction
  • beta Catenin / metabolism

Substances

  • Cytoskeletal Proteins
  • LIMA1 protein, human
  • Neoplasm Proteins
  • beta Catenin