The kynurenine pathway is activated in human obesity and shifted toward kynurenine monooxygenase activation.
Lille, France. In Obesity (silver Spring), Oct 2015
The expression of several KP enzyme genes (indoleamine 2,3-dioxygenase 1 [IDO1], kynureninase [KYNU], kynurenine 3-monooxygenase [KMO], and kynurenine aminotransferase III [CCBL2]) was increased in the omental adipose tissue of women with obesity compared to lean (P < 0.05), and their expression was induced by proinflammatory cytokines in human primary adipocytes (P < 0.05), except for KMO that is not expressed in these cells.
Structure and mechanism of kynureninase.
Athens, United States. In Arch Biochem Biophys, 2014
In this pathway, kynureninase catalyzes the hydrolysis of l-kynurenine (in bacteria) or 3-hydroxy-l-kynurenine (in eukaryotes) to give anthranilic acid or 3-hydroxyanthranilic acid, respectively, and l-alanine.
Involvement of the kynurenine pathway in human glioma pathophysiology.
Sydney, Australia. In Plos One, 2013
Our data revealed that interferon-gamma (IFN-γ) stimulation significantly potentiated the expression of the KP enzymes, IDO-1 IDO-2, kynureninase (KYNU), kynurenine hydroxylase (KMO) and significantly down-regulated 2-amino-3-carboxymuconate semialdehyde decarboxylase (ACMSD) and kynurenine aminotransferase-I (KAT-I) expression in cultured human glioma cells.
[Enzymes of the kynurenine pathway].
In Postepy Hig Med Dosw, 2000
In this review, the role of kynurenine pathway enzymes (tryptophan 2,3-dioxygenase, indoleamine 2,3-dioxygenase, formamidase, kynurenine aminotransferase, kynurenine 3-hydroxylase, kynureninase, 3-hydroxyanthranilic acid oxygenase, picolinic carboxylase, quinolinic acid phosphoribosyltransferase) in the synthesis of tryptophan products degradation was described.