EMAP-II-dependent lymphocyte killing is associated with hypoxia in colorectal cancer

Br J Cancer. 2006 Sep 18;95(6):735-43. doi: 10.1038/sj.bjc.6603299. Epub 2006 Aug 22.

Abstract

Endothelial-monocyte-activating polypeptide-II (EMAP-II) is a novel multifunctional polypeptide with proinflammatory activity. We have previously shown that the recombinant and native forms of EMAP-II can induce apoptosis in mitogen-stimulated lymphocytes, and that the release of this protein into the extracellular milieu is enhanced by hypoxia. We hypothesised that hypoxia may lead to death of tumour-infiltrating lymphocytes (TILs) via an EMAP-II-dependent mechanism, thereby assisting tumours to evade the immune system. In this study, we used immunohistochemistry to detect EMAP-II, active caspase-3 and cleaved Poly (ADP-ribose) Polymerase (PARP) as indicators of apoptosis in TILs, and carbonic anhydrase IX (CA IX) as a surrogate marker of hypoxia. EMAP-II expression is associated with regions of hypoxia, and furthermore there is a significant association between TILs apoptosis and the presence of hypoxia. Using a coculture model of colorectal cancer cell/lymphocyte interactions, we were also able to demonstrate lymphocyte apoptosis induced by tumour cells, with concomitant caspase-3 activity. Lymphocyte killing was enhanced by direct cell-cell contact, particularly by tumour cells exposed to hypoxic conditions. Our data support the hypothesis that hypoxia plays a role in immune evasion by tumour cells, through EMAP-II-dependent lymphocyte killing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Neoplasm / biosynthesis
  • Apoptosis / immunology
  • Carbonic Anhydrase IX
  • Carbonic Anhydrases / biosynthesis
  • Caspase 3 / biosynthesis
  • Caspase 3 / immunology
  • Cell Hypoxia / immunology*
  • Cell Line, Tumor
  • Coculture Techniques
  • Colorectal Neoplasms / immunology*
  • Colorectal Neoplasms / pathology
  • Cytokines / biosynthesis
  • Cytokines / chemistry
  • Cytokines / immunology*
  • Humans
  • Immunohistochemistry
  • Lymphocytes / immunology*
  • Lymphocytes / pathology
  • Neoplasm Proteins / biosynthesis
  • Neoplasm Proteins / chemistry
  • Neoplasm Proteins / immunology*
  • Poly(ADP-ribose) Polymerases / immunology
  • RNA-Binding Proteins / biosynthesis
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / immunology*
  • T-Lymphocytes / immunology
  • Tumor Cells, Cultured

Substances

  • Antigens, Neoplasm
  • Cytokines
  • Neoplasm Proteins
  • RNA-Binding Proteins
  • small inducible cytokine subfamily E, member 1
  • Poly(ADP-ribose) Polymerases
  • Caspase 3
  • CA9 protein, human
  • Carbonic Anhydrase IX
  • Carbonic Anhydrases