Ohashi Yuko Y, Kameoka Yosuke, Persad Amanda S, Koi Fumikazu, Yamagoe Satoshi, Hashimoto Katsuyuki, Suzuki Kazuo
Department of Bioactive Molecules, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku, Tokyo 162-8640, Japan.
Gene. 2004 Mar 3;327(2):195-200. doi: 10.1016/j.gene.2003.11.023.
Myeloperoxidase (MPO; EC 1.11.1.7) plays an important role in the host defense mechanism against microbial diseases. The neutrophil disorder characterized by the lack of MPO activity, is speculated to be associated with a decreased level of immunity. A Japanese patient was identified with complete MPO deficiency through automated hematography. Neutrophil function analysis revealed that MPO activity was significantly diminished with slightly elevated superoxide production. Mutational analysis of the patient revealed a glycine to serine substitution (G501S) in the exon 9 region. This mutation was not detected in the 96 healthy controls analyzed. The amino acid substitution found may be responsible for the failure of mature MPO production in the patient. This is the first case of MPO deficiency of G501S missense mutation identified in a Japanese patient.
髓过氧化物酶（MPO；EC 1.11.1.7）在宿主抵御微生物疾病的防御机制中发挥着重要作用。以缺乏MPO活性为特征的中性粒细胞紊乱，据推测与免疫力降低有关。通过自动血液学检查，一名日本患者被确诊为完全性MPO缺乏症。中性粒细胞功能分析显示，MPO活性显著降低，同时超氧化物生成略有增加。对该患者的突变分析显示，外显子9区域发生了甘氨酸到丝氨酸的替换（G501S）。在分析的96名健康对照中未检测到这种突变。发现的氨基酸替换可能是导致该患者成熟MPO生成失败的原因。这是在一名日本患者中首次发现的G501S错义突变导致的MPO缺乏症病例。
