AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts

J Clin Invest. 2007 Oct;117(10):2962-73. doi: 10.1172/JCI30710.

Abstract

The actin filament-associated protein AFAP-110 is an actin cross-linking protein first identified as a substrate of the viral oncogene v-Src. AFAP-110 regulates actin cytoskeleton integrity but also functions as an adaptor protein that affects crosstalk between Src and PKC. Here we investigated the roles of AFAP-110 in the tumorigenic process of prostate carcinoma. Using immunohistochemistry of human tissue arrays, we found that AFAP-110 was absent or expressed at very low levels in normal prostatic epithelium and benign prostatic hyperplasia but significantly increased in prostate carcinomas. The level of AFAP-110 in carcinomas correlated with the Gleason scores. Downregulation of AFAP-110 in PC3 prostate cancer cells inhibited cell proliferation in vitro and tumorigenicity and growth in orthotopic nude mouse models. Furthermore, downmodulation of AFAP-110 resulted in decreased cell-matrix adhesion and cell migration, defective focal adhesions, and reduced integrin beta1 expression. Reintroduction of avian AFAP-110 or a mutant disabling its interaction with Src restored these properties. However, expression of an AFAP-110 lacking the PKC-interacting domain failed to restore properties of parental cells. Thus, increased expression of AFAP-110 is associated with progressive stages of prostate cancer and is critical for tumorigenic growth, in part by regulating focal contacts in a PKC-dependent mechanism.

Publication types

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

MeSH terms

  • Animals
  • Carcinoma / metabolism
  • Carcinoma / pathology*
  • Cell Adhesion / genetics
  • Cell Line, Tumor
  • Cell Movement / genetics
  • Cell Proliferation
  • Cell Transformation, Neoplastic / metabolism*
  • Down-Regulation
  • Extracellular Matrix / pathology
  • Focal Adhesions / genetics
  • Focal Adhesions / metabolism*
  • Humans
  • Integrins / metabolism
  • Male
  • Mice
  • Mice, Nude
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Mutation
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Prostatic Neoplasms / metabolism
  • Prostatic Neoplasms / pathology*
  • Protein-Tyrosine Kinases / metabolism
  • Up-Regulation

Substances

  • AFAP 110
  • Integrins
  • Microfilament Proteins
  • Phosphoproteins
  • Protein-Tyrosine Kinases