Skinner M, Harding J, Skare I, Jones L A, Cohen A S, Milunsky A, Skare J
Arthritis Center, Boston University School of Medicine, MA 02118.
Ophthalmology. 1992 Apr;99(4):503-8. doi: 10.1016/s0161-6420(92)31949-9.
An inherited type of amyloidosis was suspected in an individual of Italian descent who presented with vitreous opacities. Although no family history of amyloidosis was apparent, the patient's transthyretin gene was examined and found not to possess any of the known transthyretin mutations. Complete DNA sequencing revealed a substitution of adenine for thymine in the second base of codon 84 causing an amino acid change of asparagine for isoleucine. The mutation was confirmed by demonstrating the loss of an Sfa N1 restriction endonuclease site. Allele-specific DNA amplification by polymerase chain reaction also was used to confirm the mutation. Either of these tests can be used for diagnosis. Asparagine 84 represents the second mutation associated with amyloidosis to occur at codon 84.
一名有意大利血统、出现玻璃体混浊的个体被怀疑患有遗传性淀粉样变性。尽管没有明显的淀粉样变性家族史，但对该患者的转甲状腺素蛋白基因进行了检测，发现其不具有任何已知的转甲状腺素蛋白突变。完整的DNA测序显示，密码子84的第二个碱基处腺嘌呤替代胸腺嘧啶，导致异亮氨酸变为天冬酰胺的氨基酸变化。通过证明Sfa N1限制性内切酶位点的缺失证实了该突变。聚合酶链反应进行的等位基因特异性DNA扩增也用于证实该突变。这两种检测方法中的任何一种均可用于诊断。天冬酰胺84是密码子84处发生的与淀粉样变性相关的第二个突变。
