血小板糖蛋白IIIa上一种罕见的亮氨酸40/精氨酸40多态性与人类血小板抗原1b相关。
A rare leucine 40/arginine40 polymorphism on platelet glycoprotein IIIa is linked to the human platelet antigen 1b.
作者信息
Walchshofer S, Ghali D, Fink M, Panzer-Grümayer E R, Panzer S
机构信息
Institute for Blood Group Serology, University of Vienna, Austria.
出版信息
Vox Sang. 1994;67(2):231-4. doi: 10.1111/j.1423-0410.1994.tb01666.x.
A rare polymorphism on glycoprotein (GP) IIIa is reported. Sequencing of a 482-base-pair (bp) PCR product of the genomic DNA of GPIIIa revealed a single-base exchange of a G<==>T polymorphism at base 12,569 that created an additional restriction site for MspI. This single-point mutation (frequency in Caucasians 0.00386) is on the HPA-1b gene (HPA-1bvar) and codominantly inherited. The exchange of a G for a T results in a leucine-to-arginine substitution at amino acid 40 from the NH2 terminus. The binding of anti-HPA-1a and -1b antibodies to HPA-1bvar platelets is not influenced.
据报道，糖蛋白（GP）IIIa存在一种罕见的多态性。对GPIIIa基因组DNA的482个碱基对（bp）的PCR产物进行测序，发现在第12569位碱基处存在一个G<==>T多态性的单碱基交换，这为MspI创造了一个额外的限制性酶切位点。这个单点突变（在白种人中的频率为0.00386）位于HPA-1b基因（HPA-1bvar）上，呈共显性遗传。G被T替换导致从NH2末端起第40位氨基酸处的亮氨酸被精氨酸取代。抗HPA-1a和-1b抗体与HPA-1bvar血小板的结合不受影响。
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