Glucocerebrosidase processing in normal fibroblasts and in fibroblasts from patients with type I, type II, and type III Gaucher disease.
Glucocerebrosidase processing in normal fibroblasts and in fibroblasts from patients with type I, type II, and type III Gaucher disease.
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正常成纤维细胞和 I 型、II 型和 III 型戈谢病患者的成纤维细胞中葡萄糖脑苷脂酶的加工。
DOI：
10.1073/pnas.83.19.7472
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发表时间：
1986
影响因子：
11.1
通讯作者：
Kuhl,W
中科院分区：
文献类型：
--
作者：
Beutler,E;Kuhl,W
用[3H]亮氨酸标记正常受试者和三种类型戈谢病患者的成纤维细胞。使用亲和纯化的琼脂糖结合抗体免疫沉淀葡糖脑苷脂酶抗原。正常细胞最初形成60 kDa的多肽抗原，其逐渐被平均63 kDa的宽抗原带取代。该位置对应于成熟成纤维细胞和胎盘酶的位置。葡萄糖脑苷脂酶的加工在六个无关的患者与I型戈谢病和III型戈谢病的患者是完全一样的正常。相比之下，3例严重的婴儿（II型）形式的疾病表现出一个非常不稳定的酶，60 kDa的带出现短暂的和成熟的63 kDa的带从未见过。这些结果表明，II型戈谢病可以很好地区别于I型疾病凭借非常不稳定的酶前体。与一些早期报道相反，I型疾病中葡萄糖脑苷脂酶的加工似乎完全正常。
Fibroblasts from normal subjects and patients with the three types of Gaucher disease were labeled with [3H]leucine. Glucocerebrosidase antigen was immunoprecipitated using affinity-purified Sepharose-bound antibody. Normal cells initially formed a 60-kDa polypeptide antigen that was gradually replaced by a broad band of antigen averaging 63 kDa. This position corresponds with that of mature fibroblast and placental enzyme. Processing of glucocerebrosidase in six unrelated patients with type I Gaucher disease and one patient with type III Gaucher disease was exactly the same as normal. In contrast, three patients with the severe infantile (type II) form of the disease manifested a very unstable enzyme; the 60-kDa band appeared transiently and the mature 63-kDa band was never seen. These results indicate that type II Gaucher disease may well be distinguishable from type I disease by virtue of the very unstable enzyme precursor. Contrary to some earlier reports, processing of glucocerebrosidase in type I disease appears to be entirely normal.