scholarly journals Serum Indoleamine 2,3-Dioxygenase Activity Predicts Prognosis of Pulmonary Tuberculosis

2012 ◽  
Vol 19 (3) ◽  
pp. 436-442 ◽  
Author(s):  
Yuzo Suzuki ◽  
Takafumi Suda ◽  
Kazuhiro Asada ◽  
Seiichi Miwa ◽  
Masako Suzuki ◽  
...  

ABSTRACTTuberculosis (TB) continues to be a major health problem, and there are few biomarkers for predicting prognosis. Indoleamine 2,3-dioxygenase (IDO), a potent immunoregulatory molecule, catalyzes the rate-limiting step of tryptophan (Trp) degradation in the kynurenine (Kyn) pathway. An increase in IDO activity determined by the serum Trp/Kyn ratio has been shown to be associated with poor prognosis in cancers and bacteremia. In TB, however, there are no studies measuring serum IDO activity to determine its clinical significance. We evaluated serum IDO activity with 174 pulmonary TB (PTB) patients and 85 controls, using liquid chromatography/electrospray ionization tandem mass spectrometry. IDO activity was estimated by calculating the serum Kyn-to-Trp ratio. PTB patients had significantly higher Kyn concentrations and IDO activity and significantly lower Trp concentrations (P< 0.0001,P< 0.0001, andP< 0.0001, respectively) than the controls. Of 174 PTB patients, 39 (22.4%) died. The patients who died had significantly higher concentrations of Kyn and significantly lower Trp concentrations, resulting in significantly higher IDO activity (P< 0.0001,P< 0.0001, andP< 0.0001, respectively). In a receiver operating characteristic (ROC) analysis, serum IDO activity had the highest area under the curve (0.850), and this activity was an independent prognostic factor in multivariate analysis. These results suggest that serum IDO activity can be used as a novel prognostic marker in PTB.

2009 ◽  
Vol 37 (2) ◽  
pp. 408-412 ◽  
Author(s):  
Sara A. Rafice ◽  
Nishma Chauhan ◽  
Igor Efimov ◽  
Jaswir Basran ◽  
Emma Lloyd Raven

The family of haem dioxygenases catalyse the initial oxidative cleavage of L-tryptophan to N-formylkynurenine, which is the first, rate-limiting, step in the L-kynurenine pathway. In the present paper, we discuss and compare structure and function across the family of haem dioxygenases by focusing on TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase), including a review of recent structural information for both enzymes. The present paper describes how the recent development of recombinant expression systems has informed our more detailed understanding of the substrate binding, catalytic activity and mechanistic properties of these haem dioxygenases.


2018 ◽  
Vol 26 (4) ◽  
pp. 198-203
Author(s):  
Samah Sajad Kadim ◽  
Mohammad O. Al-Mohammadi ◽  
Ali K. Shaaeli

The gallbladder (GB) is an assistant organ of the digestive system, It is  located under the liver and attached to the biliary system, And it is responsible for controlling release of bile and the storage. Gallstone disease a major health problem worldwide. In 10–15% of adults contain gallstone disease. This study (case control) consists of  one hundred sixty (160) patients are included in this study randomly selected  and consisted of 130 females and 30 males. All patients are examined 24 hr. Before operation, Intra operatively and 24hr post operatively. Decreased gallbladder motility and the decrease of cholesterol 7 –alpha hydroxylase activity, which regulate the novo bile salt synthesis. The rate-limiting step of bile acid synthesis is acting between the liver-specific CYP 7A1 (CYP450). Thus, Alteration in CYP gene control also has an impact on bile acid synthesis and lipid metabolism.


2008 ◽  
Vol 36 (6) ◽  
pp. 1120-1123 ◽  
Author(s):  
Sarah J. Thackray ◽  
Christopher G. Mowat ◽  
Stephen K. Chapman

The haem proteins TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase) are specific and powerful oxidation catalysts that insert one molecule of dioxygen into L-tryptophan in the first and rate-limiting step in the kynurenine pathway. Recent crystallographic and biochemical analyses of TDO and IDO have greatly aided our understanding of the mechanisms employed by these enzymes in the binding and activation of dioxygen and tryptophan. In the present paper, we briefly discuss the function, structure and possible catalytic mechanism of these enzymes.


1978 ◽  
Vol 39 (02) ◽  
pp. 496-503 ◽  
Author(s):  
P A D’Amore ◽  
H B Hechtman ◽  
D Shepro

SummaryOrnithine decarboxylase (ODC) activity, the rate-limiting step in the synthesis of polyamines, can be demonstrated in cultured, bovine, aortic endothelial cells (EC). Serum, serotonin and thrombin produce a rise in ODC activity. The serotonin-induced ODC activity is significantly blocked by imipramine (10-5 M) or Lilly 11 0140 (10-6M). Preincubation of EC with these blockers together almost completely depresses the 5-HT-stimulated ODC activity. These observations suggest a manner by which platelets may maintain EC structural and metabolic soundness.


Diabetes ◽  
1993 ◽  
Vol 42 (2) ◽  
pp. 296-306 ◽  
Author(s):  
D. C. Bradley ◽  
R. A. Poulin ◽  
R. N. Bergman

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