Suppr超能文献

磷酸核糖焦磷酸合成酶活性过高作为一名年轻女性尿酸产生过多的原因

Phosphoribosylpyrophosphate synthetase overactivity as a cause of uric acid overproduction in a young woman.

作者信息

García-Pavía Pablo, Torres Rosa J, Rivero Manuel, Ahmed Maqbool, García-Puig Juan, Becker Michael A

机构信息

La Paz University Hospital, Madrid, Spain.

出版信息

Arthritis Rheum. 2003 Jul;48(7):2036-41. doi: 10.1002/art.11058.

Abstract

Overactivity of phosphoribosylpyrophosphate synthetase (PRS) is an X chromosome-linked disorder of purine metabolism that is characterized by gout with uric acid overproduction and, in some families, neurodevelopmental impairment. We present the case of a 24-year-old Spanish woman with renal colic and hyperuricemia, which first manifested at age 11 years. Results of enzymatic and genetic studies supported the view that accelerated purine nucleotide and uric acid production in this woman resulted from defective allosteric regulation of PRS activity, which is, in turn, a consequence of a mutation in one of the patient's PRPS1 genes: an A-to-T substitution at nucleotide 578, encoding leucine for histidine at amino acid residue 192 of the mature PRS1 isoform. A previous example of disordered regulation of PRS1 activity in a family with a different substitution at the same amino acid residue strengthens this proposed mechanism. This is the first reported instance of PRS overactivity in which the propositus and sole affected family member is a woman.

摘要

磷酸核糖焦磷酸合成酶(PRS)活性过高是一种X染色体连锁的嘌呤代谢紊乱疾病,其特征为痛风伴尿酸生成过多,在一些家族中还伴有神经发育障碍。我们报告了一例24岁西班牙女性病例,该患者有肾绞痛和高尿酸血症,首次发病于11岁。酶学和遗传学研究结果支持以下观点:该女性嘌呤核苷酸和尿酸生成加速是由于PRS活性的变构调节缺陷所致,而这又是患者其中一个PRPS1基因突变的结果:核苷酸578处发生A到T的替换,导致成熟PRS1同工型氨基酸残基192处的组氨酸被亮氨酸取代。先前一个家族中同一氨基酸残基发生不同替换导致PRS1活性调节紊乱的例子进一步支持了这一推测机制。这是首例报道的PRS活性过高病例,先证者及唯一受影响的家族成员为女性。

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验