Targeting the IDO1 pathway in cancer: from bench to bedside

Indoleamine 2, 3-dioxygenases (IDO1 and IDO2) and tryptophan 2, 3-dioxygenase (TDO) are tryptophan catabolic enzymes that catalyze the conversion of tryptophan into kynurenine. The depletion of tryptophan and the increase in kynurenine exert important immunosuppressive functions by activating T regu...

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Published inJournal of hematology and oncology Vol. 11; no. 1; pp. 100 - 12
Main Authors Liu, Ming, Wang, Xu, Wang, Lei, Ma, Xiaodong, Gong, Zhaojian, Zhang, Shanshan, Li, Yong
Format Journal Article
LanguageEnglish
Published England BioMed Central Ltd 02.08.2018
BioMed Central
BMC
Subjects
3-dioxygenases
Acids
Adoptive transfer
Antigens
Cancer
Cancer immunotherapy
Cancer therapies
Cancer vaccines
Care and treatment
Chimeric antigen receptors
Clinical trial
Clinical trials
Dioxygenase
Enzymes
Gene expression
Genetic aspects
Genomes
Hematology
IDO1
Immune checkpoint
Immunoglobulins
Immunoregulation
Immunosuppression
Immunosurveillance
Immunotherapy
Indoleamine 2
Kinases
Leukemia
Lymphocytes
Lymphocytes T
Metabolism
Metastasis
Natural killer cells
Oncology
Oxidases
Physiological aspects
Prostate
Review
Solid tumors
Suppressor cells
Tryptophan
Tumor necrosis factor-TNF
Tumors
Vascularization
United States
China
Indoleamine 2
Clinical trial
Immunosuppression
3-dioxygenases
Immunotherapy
IDO1
Online AccessGet full text

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Abstract Indoleamine 2, 3-dioxygenases (IDO1 and IDO2) and tryptophan 2, 3-dioxygenase (TDO) are tryptophan catabolic enzymes that catalyze the conversion of tryptophan into kynurenine. The depletion of tryptophan and the increase in kynurenine exert important immunosuppressive functions by activating T regulatory cells and myeloid-derived suppressor cells, suppressing the functions of effector T and natural killer cells, and promoting neovascularization of solid tumors. Targeting IDO1 represents a therapeutic opportunity in cancer immunotherapy beyond checkpoint blockade or adoptive transfer of chimeric antigen receptor T cells. In this review, we discuss the function of the IDO1 pathway in tumor progression and immune surveillance. We highlight recent preclinical and clinical progress in targeting the IDO1 pathway in cancer therapeutics, including peptide vaccines, expression inhibitors, enzymatic inhibitors, and effector inhibitors.
AbstractList Indoleamine 2, 3-dioxygenases (IDO1 and IDO2) and tryptophan 2, 3-dioxygenase (TDO) are tryptophan catabolic enzymes that catalyze the conversion of tryptophan into kynurenine. The depletion of tryptophan and the increase in kynurenine exert important immunosuppressive functions by activating T regulatory cells and myeloid-derived suppressor cells, suppressing the functions of effector T and natural killer cells, and promoting neovascularization of solid tumors. Targeting IDO1 represents a therapeutic opportunity in cancer immunotherapy beyond checkpoint blockade or adoptive transfer of chimeric antigen receptor T cells. In this review, we discuss the function of the IDO1 pathway in tumor progression and immune surveillance. We highlight recent preclinical and clinical progress in targeting the IDO1 pathway in cancer therapeutics, including peptide vaccines, expression inhibitors, enzymatic inhibitors, and effector inhibitors.
Abstract Indoleamine 2, 3-dioxygenases (IDO1 and IDO2) and tryptophan 2, 3-dioxygenase (TDO) are tryptophan catabolic enzymes that catalyze the conversion of tryptophan into kynurenine. The depletion of tryptophan and the increase in kynurenine exert important immunosuppressive functions by activating T regulatory cells and myeloid-derived suppressor cells, suppressing the functions of effector T and natural killer cells, and promoting neovascularization of solid tumors. Targeting IDO1 represents a therapeutic opportunity in cancer immunotherapy beyond checkpoint blockade or adoptive transfer of chimeric antigen receptor T cells. In this review, we discuss the function of the IDO1 pathway in tumor progression and immune surveillance. We highlight recent preclinical and clinical progress in targeting the IDO1 pathway in cancer therapeutics, including peptide vaccines, expression inhibitors, enzymatic inhibitors, and effector inhibitors.
Indoleamine 2, 3-dioxygenases (IDO1 and IDO2) and tryptophan 2, 3-dioxygenase (TDO) are tryptophan catabolic enzymes that catalyze the conversion of tryptophan into kynurenine. The depletion of tryptophan and the increase in kynurenine exert important immunosuppressive functions by activating T regulatory cells and myeloid-derived suppressor cells, suppressing the functions of effector T and natural killer cells, and promoting neovascularization of solid tumors. Targeting IDO1 represents a therapeutic opportunity in cancer immunotherapy beyond checkpoint blockade or adoptive transfer of chimeric antigen receptor T cells. In this review, we discuss the function of the IDO1 pathway in tumor progression and immune surveillance. We highlight recent preclinical and clinical progress in targeting the IDO1 pathway in cancer therapeutics, including peptide vaccines, expression inhibitors, enzymatic inhibitors, and effector inhibitors.Indoleamine 2, 3-dioxygenases (IDO1 and IDO2) and tryptophan 2, 3-dioxygenase (TDO) are tryptophan catabolic enzymes that catalyze the conversion of tryptophan into kynurenine. The depletion of tryptophan and the increase in kynurenine exert important immunosuppressive functions by activating T regulatory cells and myeloid-derived suppressor cells, suppressing the functions of effector T and natural killer cells, and promoting neovascularization of solid tumors. Targeting IDO1 represents a therapeutic opportunity in cancer immunotherapy beyond checkpoint blockade or adoptive transfer of chimeric antigen receptor T cells. In this review, we discuss the function of the IDO1 pathway in tumor progression and immune surveillance. We highlight recent preclinical and clinical progress in targeting the IDO1 pathway in cancer therapeutics, including peptide vaccines, expression inhibitors, enzymatic inhibitors, and effector inhibitors.
ArticleNumber 100
Audience Academic
Author Ma, Xiaodong
Liu, Ming
Wang, Xu
Gong, Zhaojian
Zhang, Shanshan
Wang, Lei
Li, Yong
Author_xml – sequence: 1
  givenname: Ming
  surname: Liu
  fullname: Liu, Ming
– sequence: 2
  givenname: Xu
  surname: Wang
  fullname: Wang, Xu
– sequence: 3
  givenname: Lei
  surname: Wang
  fullname: Wang, Lei
– sequence: 4
  givenname: Xiaodong
  surname: Ma
  fullname: Ma, Xiaodong
– sequence: 5
  givenname: Zhaojian
  surname: Gong
  fullname: Gong, Zhaojian
– sequence: 6
  givenname: Shanshan
  surname: Zhang
  fullname: Zhang, Shanshan
– sequence: 7
  givenname: Yong
  orcidid: 0000-0001-8838-1714
  surname: Li
  fullname: Li, Yong
BackLink https://www.ncbi.nlm.nih.gov/pubmed/30068361$$D View this record in MEDLINE/PubMed
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Issue 1
Keywords Indoleamine 2
Clinical trial
Immunosuppression
3-dioxygenases
Immunotherapy
IDO1
Language English
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Snippet Indoleamine 2, 3-dioxygenases (IDO1 and IDO2) and tryptophan 2, 3-dioxygenase (TDO) are tryptophan catabolic enzymes that catalyze the conversion of tryptophan...
Abstract Indoleamine 2, 3-dioxygenases (IDO1 and IDO2) and tryptophan 2, 3-dioxygenase (TDO) are tryptophan catabolic enzymes that catalyze the conversion of...
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SubjectTerms 3-dioxygenases
Acids
Adoptive transfer
Antigens
Cancer
Cancer immunotherapy
Cancer therapies
Cancer vaccines
Care and treatment
Chimeric antigen receptors
Clinical trial
Clinical trials
Dioxygenase
Enzymes
Gene expression
Genetic aspects
Genomes
Hematology
IDO1
Immune checkpoint
Immunoglobulins
Immunoregulation
Immunosuppression
Immunosurveillance
Immunotherapy
Indoleamine 2
Kinases
Leukemia
Lymphocytes
Lymphocytes T
Metabolism
Metastasis
Natural killer cells
Oncology
Oxidases
Physiological aspects
Prostate
Review
Solid tumors
Suppressor cells
Tryptophan
Tumor necrosis factor-TNF
Tumors
Vascularization
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Title Targeting the IDO1 pathway in cancer: from bench to bedside
URI https://www.ncbi.nlm.nih.gov/pubmed/30068361
https://www.proquest.com/docview/2090415923
https://www.proquest.com/docview/2082093971
https://pubmed.ncbi.nlm.nih.gov/PMC6090955
https://doaj.org/article/fffe982f6b0b4727a20c94acd505f767
Volume 11
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