ECM overrides DNA damage-induced cell cycle arrest and apoptosis in small-cell lung cancer cells through beta1 integrin-dependent activation of PI3-kinase

Cell Death Differ. 2006 Oct;13(10):1776-88. doi: 10.1038/sj.cdd.4401849. Epub 2006 Jan 27.

Abstract

The emergence of resistance to chemotherapy remains a principle problem in the treatment of small-cell lung cancer (SCLC). We demonstrate that extracellular matrix (ECM) activates phosphatidyl inositol 3-kinase (PI3-kinase) signaling in SCLC cells and prevents etoposide-induced caspase-3 activation and subsequent apoptosis in a beta1 integrin/PI3-kinase-dependent manner. Crucially we show that etoposide and radiation induce G2/M cell cycle arrest in SCLC cells prior to apoptosis and that ECM prevents this by overriding the upregulation of p21(Cip1/WAF1) and p27(Kip1) and the downregulation of cyclins E, A and B. These effects are abrogated by pharmacological and genetic inhibition of PI3-kinase signaling. Importantly we show that chemoprotection is not mediated by altered SCLC cell proliferation or DNA repair. Thus, ECM via beta1 integrin-mediated PI3-kinase activation overrides treatment-induced cell cycle arrest and apoptosis, allowing SCLC cells to survive with persistent DNA damage, providing a model to account for the emergence of acquired drug resistance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents / pharmacology
  • Apoptosis* / drug effects
  • Apoptosis* / radiation effects
  • Carcinoma, Small Cell / metabolism*
  • Carcinoma, Small Cell / pathology*
  • Carcinoma, Small Cell / therapy
  • Cell Adhesion
  • Cell Cycle*
  • Cell Line, Tumor
  • DNA Damage
  • Etoposide / pharmacology
  • Extracellular Matrix / metabolism*
  • Glycogen Synthase Kinase 3 / metabolism
  • Glycogen Synthase Kinase 3 beta
  • Humans
  • Integrin beta1 / metabolism*
  • Laminin / metabolism
  • Lung Neoplasms / metabolism*
  • Lung Neoplasms / pathology*
  • Lung Neoplasms / therapy
  • Mutation
  • Phosphatidylinositol 3-Kinases / metabolism*
  • Phosphorylation
  • Protein-Tyrosine Kinases / metabolism
  • Proto-Oncogene Proteins c-akt / genetics
  • Proto-Oncogene Proteins c-akt / metabolism
  • Vanadates / pharmacology

Substances

  • Antineoplastic Agents
  • Integrin beta1
  • Laminin
  • Vanadates
  • Etoposide
  • Phosphatidylinositol 3-Kinases
  • Protein-Tyrosine Kinases
  • Glycogen Synthase Kinase 3 beta
  • Proto-Oncogene Proteins c-akt
  • Glycogen Synthase Kinase 3