Ezrin, a membrane-cytoskeletal linking protein, is involved in the process of invasion of endometrial cancer cells

Cancer Lett. 1999 Dec 1;147(1-2):31-8. doi: 10.1016/s0304-3835(99)00272-4.

Abstract

In order to study ezrin function in tumor growth and invasion, we used two cell lines of human endometrial cancers. Ishikawa, the low-metastatic endometrial cancer cell line, and its subclone (mEIIL) with high-metastatic activity and higher ezrin expression were treated with a ezrin antisense phosphorothioate oligonucleotides (ePONs) pulse four times before the in vitro growth assay and Matrigel invasion assay. ePONs significantly suppressed the number of both cells that penetrated through Matrigel membrane (inhibition rate; 40.1 +/- 7.5% (Ishikawa), 42.7 +/- 2.4% (mEIIL), mean +/- SD, n = 6, P < 0.05, Student's t-test), whereas they showed no effect on cell proliferation. Ezrin expression at the protein level was inhibited by ePONs. These data suggest that ezrin expression is required for invasion. The association of high ezrin expression in mEIIL and its higher ability to migrate through Matrigel may at least in part indicate functional significance of ezrin in endometrial cancer metastasis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenocarcinoma / genetics
  • Adenocarcinoma / metabolism*
  • Adenocarcinoma / pathology
  • Blotting, Northern
  • Cell Division / drug effects
  • Cell Movement / drug effects
  • Collagen / metabolism
  • Cytoskeletal Proteins / biosynthesis
  • Cytoskeletal Proteins / physiology*
  • Drug Combinations
  • Endometrial Neoplasms / genetics
  • Endometrial Neoplasms / metabolism*
  • Endometrial Neoplasms / pathology
  • Female
  • Humans
  • Laminin / metabolism
  • Membrane Proteins / physiology*
  • Membranes, Artificial
  • Microfilament Proteins / biosynthesis
  • Neoplasm Invasiveness
  • Oligonucleotides, Antisense / pharmacology
  • Phosphoproteins / antagonists & inhibitors
  • Phosphoproteins / biosynthesis
  • Phosphoproteins / genetics*
  • Proteoglycans / metabolism
  • RNA, Messenger / biosynthesis
  • Spectrin / biosynthesis
  • Tumor Cells, Cultured
  • alpha Catenin

Substances

  • CTNNA1 protein, human
  • Cytoskeletal Proteins
  • Drug Combinations
  • Laminin
  • Membrane Proteins
  • Membranes, Artificial
  • Microfilament Proteins
  • Oligonucleotides, Antisense
  • Phosphoproteins
  • Proteoglycans
  • RNA, Messenger
  • alpha Catenin
  • ezrin
  • matrigel
  • Spectrin
  • moesin
  • Collagen