Nakagawa T, Kabuto M, Kubota T, Kodera T, Sato K
Department of Neurosurgery, Fukui Medical University, Japan.
Anticancer Res. 1999 Jul-Aug;19(4B):2963-8.
The production of amyloid beta protein precursor (APP), which is a potent inhibitor of matrix metalloproteinases and serine proteinases, in human astrocytic tumors (n = 17) and normal brain tissues (n = 3) was investigated. We found proteinase inhibitory activity at around 120 kD by trypsin reverse zymography in the culture media of explant cultures of anaplastic astrocytomas and glioblastomas, but not in those of astrocytomas and normal brain tissues. Immunohistochemistry using a monoclonal antibody against human APP demonstrated that APP was detectable mainly in tumor and endothelial cells. Semiquantative analysis of western blotting revealed that immunoreactivity for APP in the culture media of tumor explant cultures appeared to be increased associated with the malignancy of astrocytic tumors. These findings suggest that APP production may be related to the malignant progression of human astrocytic tumors.
研究了人星形细胞瘤（n = 17）和正常脑组织（n = 3）中淀粉样β蛋白前体（APP）的产生，APP是基质金属蛋白酶和丝氨酸蛋白酶的有效抑制剂。我们通过胰蛋白酶反向酶谱法在间变性星形细胞瘤和胶质母细胞瘤的外植体培养物的培养基中发现了约120 kD的蛋白酶抑制活性，但在星形细胞瘤和正常脑组织的培养基中未发现。使用抗人APP单克隆抗体的免疫组织化学表明，APP主要在肿瘤细胞和内皮细胞中可检测到。蛋白质印迹的半定量分析显示，肿瘤外植体培养物培养基中APP的免疫反应性似乎随着星形细胞瘤的恶性程度增加而增加。这些发现表明，APP的产生可能与人类星形细胞瘤的恶性进展有关。
