Suppr超能文献

导致人类疾病的NT5E突变与NT5E蛋白的细胞内运输错误有关。

NT5E mutations that cause human disease are associated with intracellular mistrafficking of NT5E protein.

作者信息

Fausther Michel, Lavoie Elise G, Goree Jessica R, Baldini Giulia, Dranoff Jonathan A

机构信息

Division of Gastroenterology & Hepatology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, United States of America; Research Service, Central Arkansas VA Healthcare System, Little Rock, Arkansas, United States of America.

Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, United States of America.

出版信息

PLoS One. 2014 Jun 2;9(6):e98568. doi: 10.1371/journal.pone.0098568. eCollection 2014.

Abstract

Ecto-5'-nucleotidase/CD73/NT5E, the product of the NT5E gene, is the dominant enzyme in the generation of adenosine from degradation of AMP in the extracellular environment. Nonsense (c.662C→A, p.S221X designated F1, c.1609dupA, p.V537fsX7 designated F3) and missense (c.1073G→A, p.C358Y designated F2) NT5E gene mutations in three distinct families have been shown recently to cause premature arterial calcification disease in human patients. However, the underlying mechanisms by which loss-of-function NT5E mutations cause human disease are unknown. We hypothesized that human NT5E gene mutations cause mistrafficking of the defective proteins within cells, ultimately blocking NT5E catalytic function. To test this hypothesis, plasmids encoding cDNAs of wild type and mutant human NT5E tagged with the fluorescent probe DsRed were generated and used for transfection and heterologous expression in immortalized monkey COS-7 kidney cells that lack native NT5E protein. Enzyme histochemistry and Malachite green assays were performed to assess the biochemical activities of wild type and mutant fusion NT5E proteins. Subcellular trafficking of fusion NT5E proteins was monitored by confocal microscopy and western blot analysis of fractionated cell constituents. All 3 F1, F2, and F3 mutations result in a protein with significantly reduced trafficking to the plasma membrane and reduced ER retention as compared to wild type protein. Confocal immunofluorescence demonstrates vesicles containing DsRed-tagged NT5E proteins (F1, F2 and F3) in the cell synthetic apparatus. All 3 mutations resulted in absent NT5E enzymatic activity at the cell surface. In conclusion, three familial NT5E mutations (F1, F2, F3) result in novel trafficking defects associated with human disease. These novel genetic causes of human disease suggest that the syndrome of premature arterial calcification due to NT5E mutations may also involve a novel "trafficking-opathy".

摘要

胞外5'-核苷酸酶/CD73/NT5E是NT5E基因的产物,是细胞外环境中由AMP降解生成腺苷过程中的主要酶。最近研究表明,三个不同家族中NT5E基因的无义突变(c.662C→A,p.S221X命名为F1;c.1609dupA,p.V537fsX7命名为F3)和错义突变(c.1073G→A,p.C358Y命名为F2)可导致人类患者过早发生动脉钙化疾病。然而,功能丧失型NT5E突变导致人类疾病的潜在机制尚不清楚。我们推测,人类NT5E基因突变会导致细胞内缺陷蛋白的错误运输,最终阻断NT5E的催化功能。为验证这一假设,构建了编码野生型和突变型人NT5E cDNA且带有荧光探针DsRed的质粒,并用于在缺乏天然NT5E蛋白的永生化猴COS-7肾细胞中进行转染和异源表达。通过酶组织化学和孔雀石绿测定法评估野生型和突变型融合NT5E蛋白的生化活性。通过共聚焦显微镜和分级分离细胞成分的蛋白质印迹分析监测融合NT5E蛋白的亚细胞运输。与野生型蛋白相比,所有三种F1、F2和F3突变均导致运输至质膜的蛋白显著减少且内质网滞留减少。共聚焦免疫荧光显示在细胞合成装置中有含有DsRed标记的NT5E蛋白(F1、F2和F3)的囊泡。所有三种突变均导致细胞表面缺乏NT5E酶活性。总之,三种家族性NT5E突变(F1、F2、F3)导致与人类疾病相关的新型运输缺陷。这些人类疾病的新遗传病因表明,NT5E突变引起的过早动脉钙化综合征可能还涉及一种新型的“运输病”。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/627e/4041762/1b19f15b7bd8/pone.0098568.g001.jpg

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验