GLIAL FIBRILLARY ACIDIC PROTEIN AND S-100 PROTEIN IN HUMAN HEPATIC-ENCEPHALOPATHY - IMMUNOCYTOCHEMICAL DEMONSTRATION OF DISSOCIATION OF 2 GLIA-ASSOCIATED PROTEINS
GLIAL FIBRILLARY ACIDIC PROTEIN AND S-100 PROTEIN IN HUMAN HEPATIC-ENCEPHALOPATHY - IMMUNOCYTOCHEMICAL DEMONSTRATION OF DISSOCIATION OF 2 GLIA-ASSOCIATED PROTEINS
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DOI：
10.1007/bf00689509
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发表时间：
1986-01-01
影响因子：
12.7
通讯作者：
BUDKA, H
中科院分区：
文献类型：
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作者：
KIMURA, T;BUDKA, H
应用过氧化物酶-抗过氧化物酶标记法，比较了8例肝性脑病(包括4例肝豆状核变性和4例肝硬变)和8例年龄匹配的对照组大脑皮层、基底节和白质中胶质纤维酸性蛋白和S-100蛋白(S100P)的免疫细胞化学染色模式。大多数阿尔茨海默病II型胶质细胞表达S100P，而不表达GFAP，与正常原浆型星形胶质细胞相似，可能是特殊类型的反应性星形胶质细胞保留了原浆星形胶质细胞的特征。少数阿尔茨海默病II细胞对GFAP呈轻度核周免疫反应；有些细胞同时缺乏这两种标记。提示这两种蛋白在阿尔茨海默病中的代谢变化具有一定的谱系。GFAP阳性的阿尔茨海默病II细胞仅局限于基底节和邻近灰质的白质，提示GFAP在阿尔茨海默病II中的表达可能受局部因素的调节。阿尔茨海默病的I型细胞和Opalski细胞对这两种蛋白均呈免疫阳性反应，证实了它们的星形胶质细胞来源以及与阿尔茨海默病II不同的特征。形态计量学比较，胶质纤维酸性蛋白阳性细胞在皮质中的比例减少(P<；0.001)，但在白质中的比例不明显(P<；0.1)，证实了早期的数据表明，HE脑中胶质纤维酸性蛋白的显著减少仅限于灰质。在壳核，获得性HE组胶质纤维酸性蛋白阳性胶质细胞比例减少，而肝豆状核变性S病无此改变，可能是由于肝豆状核变性的胶质纤维细胞增生与肝豆状核变性的严重实质损害有关。相比之下，S100P免疫反应阳性的胶质细胞在任何研究区域都没有显著变化(P>；0.1)，这表明在HE中S100P的神经胶质代谢是完整的。GFAP和S100P之间的这种明显分离将阿尔茨海默病II定义为一种特殊的胶质反应，具有相当选择性的GFAP代谢缺陷(“胶质纤维营养不良”)。
Immunocytochemical staining patterns for glial fibrillary acidic protein (GFAP) and S-100 protein (S100P) were compared in cerebral cortex, basal ganglia and white matter of eight cases with hepatic encephalopathy (HE), including four cases of Wilson''s disease and four of liver cirrhosis, and of eight age-matched control, using the peroxidase-anti-peroxidase method on adjacent paraffin sections. The majority of Alzheimer type II glia (Alzg II) showed prominent immunoreactivity for S100P but not for GFAP, resembling normal astrocytes of protoplasmic type; Alzg II might be interpreted as being peculiar types of reactive astrocytes retaining characteristics of protoplasmic astrocytes. A small number of Alzg II cells showed slight perinuclear immunoreactivity for GFAP; some lacked both markers. This suggests a spectrum of metabolic changes in these two proteins in Alzg II. GFAP-positive Alzg II cells were restricted to basal ganglia and white matter adjacent to grey matter, indicating that expression of GFAP in Alzg II might be modulated by local factors. Alzheimer type I cells and Opalski cells in Wilson''s disease were immunoreactive for both proteins, confirming their astroglial origin and different character from that of Alzg II. In morphometric comparison, the proportion of GFAP-positive glial cells decreased in the cortex (P < 0.001) but not significantly in the white matter (0.05 < P < 0.1), confirming earlier data that the prominent reduction of GFAP in HE brains is restricted to the grey matter. In the putamen, the proportion of GFAP-positive glia decreased in acquired HE (0.01 < P < 0.05), but not in Wilson''s disease, probably resulting from prominent fibrous glial proliferation related to severe parenchymal damage in Wilson''s disease. In contrast, glial cells immunoreactive for S100P did not significantly change (P > 0.1) in any of the areas studied, indicating an intact glial metabolism of S100P in HE. This clear dissociation between GFAP and S100P defines Alzg II as a peculiar glial reaction with a rather selective deficit of GFAP metabolism ("gliofibrillary dystrophy").