MGr1-Ag/37LRP induces cell adhesion-mediated drug resistance through FAK/PI3K and MAPK pathway in gastric cancer

Cancer Sci. 2014 Jun;105(6):651-9. doi: 10.1111/cas.12414. Epub 2014 May 12.

Abstract

It is well known that tumor microenvironment plays a vital role in drug resistance and cell adhesion-mediated drug resistance (CAM-DR), a form of de novo drug resistance. In our previous study, we reported that MGr1-Ag/37LRP ligation-induced adhesion participated in protecting gastric cancer cells from a number of apoptotic stimuli caused by chemotherapeutic drugs. Further study suggested that MGr1-Ag could prompt CAM-DR through interaction with laminin. However, the MGr1-Ag-initiated intracellular signal transduction pathway is still unknown. In this study, our experimental results showed that gastric cancer MDR cell lines mediated CAM-DR through upregulation of Bcl-2 by MGr1-Ag interaction with laminin. Further study found that, as a receptor of ECM components, MGr1-Ag/37LRP may activate the downstream signal pathway PI3K/AKT and MAPK/ERK through interaction with phosphorylated FAK. Moreover, the sensitivity to chemotherapeutic drugs could be significantly enhanced by inhibiting MGr1-Ag/37LRP expression through mAbs, siRNA, and antisense oligonucleotide. According to these results, we concluded that the FAK/PI3K and MAPK signal pathway plays an important role in MGr1-Ag-mediated CAM-DR in gastric cancer. MGr1-Ag/37LRP might be a potential effective reversal target to MDR in gastric cancer.

Keywords: CAM-DR; FAK/PI3K; MAPK; MGr1-Ag/37LRP; gastric cancer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology
  • Antigens, Neoplasm / genetics
  • Antigens, Neoplasm / metabolism*
  • Cell Adhesion
  • Drug Resistance, Neoplasm*
  • Focal Adhesion Kinase 1 / metabolism
  • Humans
  • Laminin / metabolism
  • Male
  • Mice
  • Mice, Nude
  • Mitogen-Activated Protein Kinases / metabolism*
  • Phosphatidylinositol 3-Kinases / metabolism*
  • Proto-Oncogene Proteins c-bcl-2 / biosynthesis
  • RNA Interference
  • RNA, Small Interfering
  • Receptors, Laminin / genetics
  • Receptors, Laminin / metabolism*
  • Ribosomal Proteins / genetics
  • Ribosomal Proteins / metabolism*
  • Signal Transduction
  • Stomach Neoplasms / drug therapy*
  • Stomach Neoplasms / pathology
  • Tumor Cells, Cultured
  • Tumor Microenvironment
  • Up-Regulation
  • Vincristine / pharmacology

Substances

  • Antibodies, Monoclonal
  • Antigens, Neoplasm
  • Laminin
  • MGr1-antigen, human
  • Proto-Oncogene Proteins c-bcl-2
  • RNA, Small Interfering
  • RPSA protein, human
  • Receptors, Laminin
  • Ribosomal Proteins
  • Vincristine
  • Phosphatidylinositol 3-Kinases
  • Focal Adhesion Kinase 1
  • PTK2 protein, human
  • Mitogen-Activated Protein Kinases