由胶原蛋白III中甘氨酸400突变为谷氨酸、甘氨酸595突变为半胱氨酸以及甘氨酸1003突变为天冬氨酸引起的IV型埃勒斯-当洛综合征：临床特征、生化筛查及分子确诊

Ehlers-Danlos syndrome type IV caused by Gly400Glu, Gly595Cys and Gly1003Asp substitutions in collagen III: clinical features, biochemical screening, and molecular confirmation.

作者信息

Mackay K, Raghunath M, Superti-Furga A, Steinmann B, Dalgleish R

机构信息

Department of Genetics, University of Leicester, United Kingdom.

出版信息

Clin Genet. 1996 Jun;49(6):286-95. doi: 10.1111/j.1399-0004.1996.tb03790.x.

DOI:10.1111/j.1399-0004.1996.tb03790.x

PMID:8884076

Abstract

Three patients with Ehlers-Danlos syndrome type IV (EDS IV) and biochemical evidence of structural defects in collagen III were investigated for mutations within the collagen III gene (COL3A1). Single strand conformation polymorphism analysis of alpha 1 (III) cDNA indicated the presence of different heterozygous sequence changes in each of the patients. Nucleotide sequencing revealed mutations leading to the substitution of glycine 400 with glutamic acid, glycine 595 with cysteine, and glycine 1003 with aspartic acid. EDS IV is a life-threatening disorder which, as the clinical histories of our patients and their families show, still often escapes diagnosis. Biochemical and molecular studies can clarify the diagnosis and help provide appropriate management and counselling.

摘要

对3例患有IV型埃勒斯-当洛综合征（EDS IV）且有III型胶原结构缺陷生化证据的患者，进行了III型胶原基因（COL3A1）内突变的研究。α1（III）cDNA的单链构象多态性分析表明，每名患者均存在不同的杂合序列变化。核苷酸测序显示，突变导致第400位甘氨酸被谷氨酸取代、第595位甘氨酸被半胱氨酸取代、第1003位甘氨酸被天冬氨酸取代。EDS IV是一种危及生命的疾病，正如我们患者及其家族的临床病史所示，它仍常常难以被诊断出来。生化和分子研究能够明确诊断，并有助于提供适当的治疗和咨询。