PMID- 26269528
OWN - NLM
STAT- MEDLINE
DCOM- 20160525
LR  - 20211108
IS  - 2326-6074 (Electronic)
IS  - 2326-6066 (Linking)
VI  - 3
IP  - 9
DP  - 2015 Sep
TI  - Tumoral Immune Resistance Mediated by Enzymes That Degrade Tryptophan.
PG  - 978-85
LID - 10.1158/2326-6066.CIR-15-0095 [doi]
AB  - Cancer patients mount T-lymphocyte responses against antigens expressed 
      selectively by their malignancy, but these responses often fail to control their 
      disease, because tumors select mechanisms that allow them to resist immune 
      destruction. Among the numerous resistance mechanisms that have been proposed, 
      metabolic inhibition of T cells by tryptophan catabolism deserves particular 
      attention, because of the frequent expression of tryptophan-degrading enzymes in 
      human tumors, and because in vitro and in vivo studies have shown that their 
      enzymatic activity can be readily blocked by pharmacologic inhibitors, thereby 
      restoring T-cell-mediated tumor cell killing and paving the way to targeted 
      therapeutic intervention. In view of recent observations, and taking into account 
      the differences between human and mouse data that differ in several aspects, in 
      this Cancer Immunology at the Crossroads article, we discuss the role of the 
      three enzymes that have been proposed to control tryptophan catabolism in tumoral 
      immune resistance: indoleamine 2,3-dioxygenase 1 (IDO1), tryptophan 
      2,3-dioxygenase (TDO), and indoleamine 2,3-dioxygenase 2 (IDO2).
CI  - (c)2015 American Association for Cancer Research.
FAU - van Baren, Nicolas
AU  - van Baren N
AD  - Ludwig Institute for Cancer Research, Brussels, Belgium. de Duve Institute, 
      Universite catholique de Louvain, Brussels, Belgium.
FAU - Van den Eynde, Benoit J
AU  - Van den Eynde BJ
AD  - Ludwig Institute for Cancer Research, Brussels, Belgium. WELBIO (Walloon 
      Excellence in Life Sciences and Biotechnology), Brussels, Belgium. de Duve 
      Institute, Universite catholique de Louvain, Brussels, Belgium. 
      benoit.vandeneynde@bru.licr.org.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20150812
PL  - United States
TA  - Cancer Immunol Res
JT  - Cancer immunology research
JID - 101614637
RN  - 0 (IDO1 protein, human)
RN  - 0 (IDO2 protein, human)
RN  - 0 (Indoleamine-Pyrrole 2,3,-Dioxygenase)
RN  - 8DUH1N11BX (Tryptophan)
RN  - EC 1.13.11.11 (Tryptophan Oxygenase)
SB  - IM
MH  - Humans
MH  - Indoleamine-Pyrrole 2,3,-Dioxygenase/physiology
MH  - Lymphocytes, Tumor-Infiltrating/immunology
MH  - Neoplasms/enzymology/*immunology
MH  - Tryptophan/*metabolism
MH  - Tryptophan Oxygenase/physiology
MH  - Tumor Escape/*immunology
EDAT- 2015/08/14 06:00
MHDA- 2016/05/26 06:00
CRDT- 2015/08/14 06:00
PHST- 2015/04/09 00:00 [received]
PHST- 2015/06/03 00:00 [accepted]
PHST- 2015/08/14 06:00 [entrez]
PHST- 2015/08/14 06:00 [pubmed]
PHST- 2016/05/26 06:00 [medline]
AID - 2326-6066.CIR-15-0095 [pii]
AID - 10.1158/2326-6066.CIR-15-0095 [doi]
PST - ppublish
SO  - Cancer Immunol Res. 2015 Sep;3(9):978-85. doi: 10.1158/2326-6066.CIR-15-0095. 
      Epub 2015 Aug 12.