随着病情进展，人胃癌中蔗糖酶和肠型碱性磷酸酶的表达增加。
Increased expression of sucrase and intestinal-type alkaline phosphatase in human gastric carcinomas with progression.
作者信息
Nakamura W, Inada K, Hirano K, Tsukamoto T, Inoue H, Kito K, Yoshikawa A, Nakamura S, Tatematsu M
机构信息
Laboratory of Pathology, Aichi Cancer Center Research Institute, Nagoya.
出版信息
Jpn J Cancer Res. 1998 Feb;89(2):186-91. doi: 10.1111/j.1349-7006.1998.tb00547.x.
The activities of sucrase, total alkaline phosphatase (total ALP) and intestinal-type alkaline phosphatase (I-ALP) were assayed in gastric carcinomas and in their surrounding mucosae from 57 patients with advanced cancers, and the localization of sucrase in 203 carcinomas, including 86 early cancers, was examined immunohistochemically using polyclonal anti-sucrase antibody. All three enzymes were active in the 57 carcinomas as well as in their surrounding mucosae, but the levels were fairly low as compared to those in normal jejunum mucosa. A considerable part of the total ALP activity in tumor specimens was assumed to be due to I-ALP itself. Increased sucrase and I-ALP were found with greater depth of invasion by undifferentiated-type carcinomas. The pattern of immunohistochemical localization of sucrase in the 203 carcinomas also clearly indicated increased expression with greater depth of invasion even in differentiated-type carcinomas.
对57例晚期癌症患者的胃癌及其周围黏膜进行了蔗糖酶、总碱性磷酸酶（总ALP）和肠型碱性磷酸酶（I-ALP）活性检测，并用多克隆抗蔗糖酶抗体对203例癌组织（包括86例早期癌）进行免疫组织化学检查，以确定蔗糖酶的定位。这三种酶在57例癌组织及其周围黏膜中均有活性，但与正常空肠黏膜相比，其水平相当低。肿瘤标本中相当一部分总ALP活性被认为是由I-ALP本身所致。未分化型癌浸润深度越深，蔗糖酶和I-ALP增加越明显。在203例癌组织中，蔗糖酶免疫组织化学定位模式也清楚表明，即使在分化型癌中，随着浸润深度的增加，表达也会增加。
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