PMID- 29051706
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20201001
IS  - 1178-6469 (Print)
IS  - 1178-6469 (Electronic)
IS  - 1178-6469 (Linking)
VI  - 10
DP  - 2017
TI  - Investigation of the Tissue Distribution and Physiological Roles of Indoleamine 
      2,3-Dioxygenase-2.
PG  - 1178646917735098
LID - 10.1177/1178646917735098 [doi]
LID - 1178646917735098
AB  - Indoleamine 2,3-dioxygenase-2 (IDO2) is 1 of the 3 enzymes that can catalyze the 
      first step in the kynurenine pathway of tryptophan metabolism. Of the 2 other 
      enzymes, tryptophan 2,3-dioxygenase is highly expressed in the liver and has a 
      role in tryptophan homeostasis, whereas indoleamine 2,3-dioxygenase-1 (IDO1) 
      expression is induced by inflammatory stimuli. Indoleamine 2,3-dioxygenase-2 is 
      reportedly expressed comparatively narrow, including in liver, kidney, brain, and 
      in certain immune cell types, and it does not appear to contribute significantly 
      to systemic tryptophan catabolism under normal physiological conditions. Here, we 
      report the identification of an alternative splicing pattern, including the use 
      of an alternative first exon, that is conserved in the mouse Ido1 and Ido2 genes. 
      These findings prompted us to assess IDO2 protein expression and enzymatic 
      activity in tissues. Our analysis, undertaken in Ido2( +/+) and Ido2(-/-) mice 
      using immunohistochemistry and measurement of tryptophan and kynurenine levels, 
      suggested an even more restricted pattern of tissue expression than previously 
      reported. We found IDO2 protein to be expressed in the liver with a 
      perinuclear/nuclear, rather than cytoplasmic, distribution. Consistent with 
      earlier reports, we found Ido2 (-/-) mice to be phenotypically similar to their 
      Ido2(+/+) counterparts regarding levels of tryptophan and kynurenine in the 
      plasma and liver. Our findings suggest a specialized function or regulatory role 
      for IDO2 associated with its particular subcellular localization.
FAU - Jusof, Felicita F
AU  - Jusof FF
AD  - Molecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, 
      The University of Sydney, Camperdown, NSW, Australia.
AD  - Department of Physiology, Faculty of Medicine, The University of Malaya, Kuala 
      Lumpur, Malaysia.
FAU - Bakmiwewa, Supun M
AU  - Bakmiwewa SM
AD  - Molecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, 
      The University of Sydney, Camperdown, NSW, Australia.
FAU - Weiser, Silvia
AU  - Weiser S
AD  - Molecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, 
      The University of Sydney, Camperdown, NSW, Australia.
FAU - Too, Lay Khoon
AU  - Too LK
AD  - Molecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, 
      The University of Sydney, Camperdown, NSW, Australia.
FAU - Metz, Richard
AU  - Metz R
AD  - NewLink Genetics Corporation, Ames, IA, USA.
FAU - Prendergast, George C
AU  - Prendergast GC
AD  - Lankenau Institute for Medical Research, Wynnewood, PA, USA.
FAU - Fraser, Stuart T
AU  - Fraser ST
AD  - Discipline of Physiology, Bosch Institute and School of Medical Sciences, The 
      University of Sydney, Camperdown, NSW, Australia.
FAU - Hunt, Nicholas H
AU  - Hunt NH
AD  - Molecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, 
      The University of Sydney, Camperdown, NSW, Australia.
FAU - Ball, Helen J
AU  - Ball HJ
AD  - Molecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, 
      The University of Sydney, Camperdown, NSW, Australia.
LA  - eng
PT  - Journal Article
DEP - 20171009
PL  - United States
TA  - Int J Tryptophan Res
JT  - International journal of tryptophan research : IJTR
JID - 101513378
PMC - PMC5638149
OTO - NOTNLM
OT  - Tryptophan
OT  - indoleamine 2,3-dioxygenase
OT  - kynurenine
OT  - tryptophan 2,3-dioxygenase
COIS- Declaration of conflicting interests:The author(s) declared no potential 
      conflicts of interest with respect to the research, authorship, and/or 
      publication of this article.
EDAT- 2017/10/21 06:00
MHDA- 2017/10/21 06:01
PMCR- 2017/10/09
CRDT- 2017/10/21 06:00
PHST- 2017/06/07 00:00 [received]
PHST- 2017/08/30 00:00 [accepted]
PHST- 2017/10/21 06:00 [entrez]
PHST- 2017/10/21 06:00 [pubmed]
PHST- 2017/10/21 06:01 [medline]
PHST- 2017/10/09 00:00 [pmc-release]
AID - 10.1177_1178646917735098 [pii]
AID - 10.1177/1178646917735098 [doi]
PST - epublish
SO  - Int J Tryptophan Res. 2017 Oct 9;10:1178646917735098. doi: 
      10.1177/1178646917735098. eCollection 2017.