Determination of kynurenic acid in human serum and its correlation with the concentration of certain amino acids
Determination of kynurenic acid in human serum and its correlation with the concentration of certain amino acids
复制标题
DOI：
10.1016/j.cca.2006.09.019
复制
发表时间：
2007-02-01
影响因子：
5
通讯作者：
Toyo'oka, Toshimasa
中科院分区：
文献类型：
--
作者：
Fukushima, Takeshi;Mitsuhashi, Shogo;Toyo'oka, Toshimasa
背景资料：犬尿烯酸（KYNA）-一种色氨酸代谢产物，对多巴胺能和胆碱能受体具有拮抗活性;已被认为与神经系统疾病有一定关系。因此，血清KYNA可能是临床诊断的重要指标。方法：测定35例健康人血清中KYNA和氨基酸的浓度（21名男性和14名女性）]通过具有荧光检测的HPLC测定;因此，在这些受试者中检查KYNA浓度与几种氨基酸浓度之间的相关性。在本研究中检查的氨基酸中，在健康受试者中，特别是男性（r =-0.687，p < 0.01），KYNA和谷氨酰胺（Gln）浓度之间观察到显著负相关（r =-0.452，p <0.01），并且未观察到年龄相关的变化。除Gln外，配偶血清中Gly和Ala浓度与KYNA浓度呈显著负相关（r分别为-0.440和-0.456，p < 0.05）。体内KYNA和Gln浓度之间的显著相关性可以支持先前的发现，即负责KYNA生物合成的犬尿氨酸氨基转移酶I（KAT I），与Gln转氨酶K（GTK）相同，后者催化Gln转氨为2-酮谷氨酸。体内KYNA和Gln浓度可能由于KATI/GTK活性的改变而受到影响。(c)2006 Elsevier B. V.保留所有权利。
Background: Kynurenic acid (KYNA)-a tryptophan metabolite-elicits antagonistic activity against glutaminergic and cholinergic receptors; it has been suggested to have some relationship with neurological disorders. Considering this, serum KYNA may be an important marker in clinical diagnosis. We determined serum KYNA concentration and elucidate its correlation with several amino acids in human serum.Methods: KYNA and amino acids concentrations in human serum of healthy subjects [n=35 (21 males and 14 females)] were determined by HPLC with fluorescence detection; thus, the correlation between KYNA concentration and that of several amino acids was examined in these subjects.Results: Of the amino acids examined in this study, a significant negative correlation was observed between KYNA and glutamine (Gln) concentrations (r=-0.452, p < 0.01) in the healthy subjects, particularly males (r=-0.687, p < 0.01), and age-related changes were not observed. In addition to Gln, Gly and Ala concentrations showed a significant negative correlation with KYNA concentration in the serum of mate subjects (r=-0.440 and -0.456, respectively, p < 0.05).Conclusion: The significant correlation between KYNA and Gln concentrations in vivo may support the previous finding that kynurenine aminotransferase I (KAT I), responsible for the biosynthesis of KYNA, was identical to Gln transaminase K (GTK), which catalyses the transamination of Gln to 2-oxoglutamic acid. Both KYNA and Gln concentrations in vivo might be influenced due to altered KAT I/GTK activity. (c) 2006 Elsevier B.V. All rights reserved.