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依赖镁离子的三磷酸腺苷酶作为B细胞起源淋巴瘤的酶组织化学标志物。

Mg2+-dependent adenosine triphosphatase as an enzyme histochemical marker for the lymphomas of B-cell origin.

作者信息

Harigaya K, Mikata A, Suzuki H, Ohishi T, Kageyama K, Minato K, Shimoyama M

出版信息

Am J Pathol. 1979 Nov;97(2):359-80.

PMID:160756
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2042476/
Abstract

Twenty-nine cases of malignant lymphoma were studied by the enzyme histochemical method and membrane surface markers. Strong adenosine triphosphatase (ATPase) activity was demonstrated in 15 cases of 20 B lymphomas and in one case of null-cell lymphoma (1/1) by a light- and electron-microscopic enzyme histochemical method according to Wachstein et al. Neoplastic cells in nodules of 2 nodular lymphomas (0/2) and in 8 cases of T lymphomas (0/8) did not show any ATPase activity enzyme-histochemically. The ATPase activity of B lymphomas was electron-microscopically demonstrated on the plasma membrane of lymphoma cells but not in the cytoplasmic organelles. The specificity of ATPase activity in B lymphomas was also examined enzyme-histochemically with reference to normal lymphoid tissues. Such specificity was similar to that of non-neoplastic B lymphocytes of primary follicles and the mantle zone of secondary follicles in lymphoid tissues. Therefore, ATPase is one of the useful enzyme histochemical markers in differentiating T and B subclasses of malignant lymphomas.

摘要

采用酶组织化学方法和膜表面标志物对29例恶性淋巴瘤进行了研究。根据瓦施泰因等人的方法，通过光镜和电镜酶组织化学方法，在20例B淋巴瘤中的15例以及1例无细胞淋巴瘤（1/1）中显示出强三磷酸腺苷酶（ATPase）活性。2例结节性淋巴瘤结节中的肿瘤细胞（0/2）以及8例T淋巴瘤中的肿瘤细胞（0/8）在酶组织化学上未显示任何ATPase活性。B淋巴瘤的ATPase活性在电镜下显示于淋巴瘤细胞的质膜上，而非细胞质细胞器中。还参照正常淋巴组织通过酶组织化学方法检查了B淋巴瘤中ATPase活性的特异性。这种特异性与淋巴组织中初级滤泡的非肿瘤性B淋巴细胞以及次级滤泡套区的非肿瘤性B淋巴细胞相似。因此，ATPase是区分恶性淋巴瘤T和B亚类的有用酶组织化学标志物之一。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/3dca6769826a/amjpathol00237-0173-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/a50a0889420d/amjpathol00237-0172-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/a02c7d7aae5d/amjpathol00237-0176-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/977e27a716d8/amjpathol00237-0178-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/f962d28218bb/amjpathol00237-0174-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/1f75cc2fe476/amjpathol00237-0171-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/0faf7081305d/amjpathol00237-0171-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/7daf358d3ee6/amjpathol00237-0170-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/4c7b50bb74d3/amjpathol00237-0175-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/bc79b69c5e0d/amjpathol00237-0179-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/3dca6769826a/amjpathol00237-0173-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/a50a0889420d/amjpathol00237-0172-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/a02c7d7aae5d/amjpathol00237-0176-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/977e27a716d8/amjpathol00237-0178-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/f962d28218bb/amjpathol00237-0174-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/1f75cc2fe476/amjpathol00237-0171-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/0faf7081305d/amjpathol00237-0171-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/7daf358d3ee6/amjpathol00237-0170-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/4c7b50bb74d3/amjpathol00237-0175-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/bc79b69c5e0d/amjpathol00237-0179-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808d/2042476/3dca6769826a/amjpathol00237-0173-a.jpg

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Histochemistry of hepatic phosphatases of a physiologic pH; with special reference to the demonstration of bile canaliculi.生理pH值下肝脏磷酸酶的组织化学；特别提及胆小管的显示
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