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一种轻度人类短链烯酰辅酶A水合酶缺乏症的临床、生化及代谢特征:N-乙酰-S-(2-羧丙基)半胱氨酸排泄增加的意义

Clinical, biochemical and metabolic characterisation of a mild form of human short-chain enoyl-CoA hydratase deficiency: significance of increased N-acetyl-S-(2-carboxypropyl)cysteine excretion.

作者信息

Yamada Kenichiro, Aiba Kaori, Kitaura Yasuyuki, Kondo Yusuke, Nomura Noriko, Nakamura Yuji, Fukushi Daisuke, Murayama Kei, Shimomura Yoshiharu, Pitt James, Yamaguchi Seiji, Yokochi Kenji, Wakamatsu Nobuaki

机构信息

Department of Genetics, Institute for Developmental Research, Aichi Human Service Center, Kasugai, Aichi, Japan.

Department of Pediatrics, Toyohashi Municipal Hospital, Toyohashi, Aichi, Japan.

出版信息

J Med Genet. 2015 Oct;52(10):691-8. doi: 10.1136/jmedgenet-2015-103231. Epub 2015 Aug 6.

Abstract

BACKGROUND

Short-chain enoyl-CoA hydratase-ECHS1-catalyses many metabolic pathways, including mitochondrial short-chain fatty acid β-oxidation and branched-chain amino acid catabolic pathways; however, the metabolic products essential for the diagnosis of ECHS1 deficiency have not yet been determined. The objective of this report is to characterise ECHS1 and a mild form of its deficiency biochemically, and to determine the candidate metabolic product that can be efficiently used for neonatal diagnosis.

METHODS

We conducted a detailed clinical, molecular genetics, biochemical and metabolic analysis of sibling patients with ECHS1 deficiency. Moreover, we purified human ECHS1, and determined the substrate specificity of ECHS1 for five substrates via different metabolic pathways.

RESULTS

Human ECHS1 catalyses the hydration of five substrates via different metabolic pathways, with the highest specificity for crotonyl-CoA and the lowest specificity for tiglyl-CoA. The patients had relatively high (∼7%) residual ECHS1 enzyme activity for crotonyl-CoA and methacrylyl-CoA caused by the compound heterozygous mutations (c.176A>G, (p.N59S) and c.413C>T, (p.A138V)) with normal mitochondrial complex I-IV activities. Affected patients excrete large amounts of N-acetyl-S-(2-carboxypropyl)cysteine, a metabolite of methacrylyl-CoA.

CONCLUSIONS

Laboratory data and clinical features demonstrated that the patients have a mild form of ECHS1 deficiency harbouring defective valine catabolic and β-oxidation pathways. N-Acetyl-S-(2-carboxypropyl) cysteine level was markedly high in the urine of the patients, and therefore, N-acetyl-S-(2-carboxypropyl)cysteine was regarded as a candidate metabolite for the diagnosis of ECHS1 deficiency. This metabolite is not part of current routine metabolic screening protocols, and its inclusion, therefore, holds immense potential in accurate diagnosis.

摘要

背景

短链烯酰辅酶A水合酶-ECHS1催化多种代谢途径,包括线粒体短链脂肪酸β-氧化和支链氨基酸分解代谢途径;然而,尚未确定对ECHS1缺乏症诊断至关重要的代谢产物。本报告的目的是从生化角度对ECHS1及其轻度缺乏形式进行表征,并确定可有效用于新生儿诊断的候选代谢产物。

方法

我们对患有ECHS1缺乏症的同胞患者进行了详细的临床、分子遗传学、生化和代谢分析。此外,我们纯化了人ECHS1,并通过不同代谢途径确定了ECHS1对五种底物的底物特异性。

结果

人ECHS1通过不同代谢途径催化五种底物的水合作用,对巴豆酰辅酶A的特异性最高,对惕格酰辅酶A的特异性最低。由于复合杂合突变(c.176A>G,(p.N59S)和c.413C>T,(p.A138V)),患者对巴豆酰辅酶A和甲基丙烯酰辅酶A具有相对较高(约7%)的残余ECHS1酶活性,线粒体复合体I-IV活性正常。受影响的患者排泄大量N-乙酰-S-(2-羧丙基)半胱氨酸,这是甲基丙烯酰辅酶A的一种代谢产物。

结论

实验室数据和临床特征表明,这些患者患有轻度ECHS1缺乏症,缬氨酸分解代谢和β-氧化途径存在缺陷。患者尿液中N-乙酰-S-(2-羧丙基)半胱氨酸水平显著升高,因此,N-乙酰-S-(2-羧丙基)半胱氨酸被视为诊断ECHS1缺乏症的候选代谢产物。这种代谢产物不是当前常规代谢筛查方案的一部分,因此,将其纳入对于准确诊断具有巨大潜力。

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