Bohlega Saeed, Al-Ajlan Huda, Al-Saif Amr
Department of Neurosciences, King Faisal Specialist Hospital and Research Center, Riyadh, Saudi Arabia.
Department of Genetics, King Faisal Specialist Hospital and Research Center, Riyadh, Saudi Arabia.
Eur J Hum Genet. 2014 May;22(5):640-3. doi: 10.1038/ejhg.2013.210. Epub 2013 Oct 2.
Fibulin-1 is an extracellular matrix protein that has an important role in the structure of elastic fibers and basement membranes of various tissues. Using homozygosity mapping and exome sequencing, we discovered a missense mutation, p.(Cys397Phe), in fibulin-1 in three patients from a consanguineous family presented with a novel syndrome of syndactyly, undescended testes, delayed motor milestones, mental retardation and signs of brain atrophy. The mutation discovered segregated with the phenotype and was not found in 374 population-matched alleles. The affected cysteine is highly conserved across vertebrates and its mutation is predicted to abolish a disulfide bond that defines the tertiary structure of fibulin-1. Our findings emphasize the crucial role fibulin-1 has in development of the central nervous system and various connective tissues.
纤连蛋白-1是一种细胞外基质蛋白,在各种组织的弹性纤维和基底膜结构中起重要作用。通过纯合子定位和外显子组测序,我们在一个近亲家庭的三名患者中发现了纤连蛋白-1中的一个错义突变p.(Cys397Phe),这些患者表现出一种新的综合征,包括并指、隐睾、运动发育迟缓、智力障碍和脑萎缩迹象。发现的突变与表型共分离,在374个群体匹配的等位基因中未发现。受影响的半胱氨酸在脊椎动物中高度保守,预计其突变会消除一个定义纤连蛋白-1三级结构的二硫键。我们的发现强调了纤连蛋白-1在中枢神经系统和各种结缔组织发育中的关键作用。