The Two Faces of Interferon-γ in Cancer
Top Cited Papers
- 1 October 2011
- journal article
- review article
- Published by American Association for Cancer Research (AACR) in Clinical Cancer Research
- Vol. 17 (19), 6118-6124
- https://doi.org/10.1158/1078-0432.ccr-11-0482
Abstract
Interferon-γ is a cytokine whose biological activity is conventionally associated with cytostatic/cytotoxic and antitumor mechanisms during cell-mediated adaptive immune response. It has been used clinically to treat a variety of malignancies, albeit with mixed results and side effects that can be severe. Despite ample evidence implicating a role for IFN-γ in tumor immune surveillance, a steady flow of reports has suggested that it may also have protumorigenic effects under certain circumstances. We propose that, in fact, IFN-γ treatment is a double-edged sword whose anti- and protumorigenic activities are dependent on the cellular, microenvironmental, and/or molecular context. As such, inhibition of the IFN-γ/IFN-γ receptor pathway may prove to be a viable new therapeutic target for a subset of malignancies. Clin Cancer Res; 17(19); 6118–24. ©2011 AACR.Keywords
This publication has 91 references indexed in Scilit:
- Interferon-γ links ultraviolet radiation to melanomagenesis in miceNature, 2011
- Interferon γ limits the effectiveness of melanoma peptide vaccinesBlood, 2011
- Type I interferon: friend or foe?The Journal of Experimental Medicine, 2010
- Cross-regulation of Signaling Pathways by Interferon-γ: Implications for Immune Responses and Autoimmune DiseasesImmunity, 2009
- CD4+ T Cells Regulate Pulmonary Metastasis of Mammary Carcinomas by Enhancing Protumor Properties of MacrophagesCancer Cell, 2009
- A phosphorylation-acetylation switch regulates STAT1 signalingGenes & Development, 2009
- Regulation of interferon and Toll‐like receptor signaling during macrophage activation by opposing feedforward and feedback inhibition mechanismsImmunological Reviews, 2008
- Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformationsProceedings of the National Academy of Sciences of the United States of America, 2008
- Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domainGenes & Development, 2006
- The Three Es of Cancer ImmunoeditingAnnual Review of Immunology, 2004