Silver stainings distinguish Lewy bodies and glial cytoplasmic inclusions: comparison between Gallyas-Braak and Campbell-Switzer methods
Silver stainings distinguish Lewy bodies and glial cytoplasmic inclusions: comparison between Gallyas-Braak and Campbell-Switzer methods
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DOI：
10.1007/s00401-005-1044-2
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发表时间：
2005-09-01
影响因子：
12.7
通讯作者：
Mizutani, T
中科院分区：
文献类型：
--
作者：
Uchihara, T;Nakamura, A;Mizutani, T
特发性帕金森病的路易体（Lewy bodies，LB）和多系统萎缩的胶质细胞胞质内含物（glial cytoplasmic inclusions，GCI）都是由磷酸化的α-突触核蛋白编织成不同细丝的病理性沉积物。虽然LB和GCI都被认为是每个独立的突触核蛋白病的标志，但直到现在，它们还不能根据其生化或免疫组化特征明确区分。我们已经研究了可能的差异，其嗜银功能和它们的关系，突触核蛋白样或泛素样免疫反应性（IR）。来自不同脑区的镜像切片对用抗α-突触核蛋白抗体、抗泛素抗体和噻嗪红（TR）进行三重荧光标记，噻嗪红是一种标记神经元结构如路易体或神经元缠结的荧光染料。随后使用Campbell-Switzer方法（CS）对其中一个配对切片进行染色，另一个使用Gallyas-Braak方法（GB）进行染色。通过比较配对的荧光标记切片上的相同显微镜视野，随后用CS或GB银染，可以确定每种结构的五种不同特征：α-突触核蛋白样IR，泛素样IR，TR亲和力，CS或GB嗜银性。GCI与CS和GB均表现出嗜银性，但对TR缺乏亲和力。与此相反，LB表现出嗜银与CS，但不与GB和一些亲和力TR。嗜银性的这些疾病特异性特征是一致的，并且不受检查的地区或病例的影响。虽然LB和GCI的免疫组织化学特征在表现出α-突触核蛋白和泛素的IR方面是相似的，但其嗜银谱的对比可能表明α-突触核蛋白的分子组成或构象可能存在差异。尽管这些经验上的差异仍然有待解释，但意识到这种明显的区别可能具有诊断和病理学意义。
Lewy bodies (LBs) of idiopathic Parkinson's disease and glial cytoplasmic inclusions (GCIs) of multiple system atrophy are pathological deposits both composed of phosphorylated alpha-synuclein woven into different filaments. Although both LBs and GCIs are considered to be hallmarks for each independent synucleinopathy, until now they could not be clearly distinguished on the basis of their biochemical or immunohistochemical features. We have examined possible differences in their argyrophilic features and their relation to synuclein-like or ubiquitin-like immunoreactivity (IR). Pairs of mirror sections from different brain areas were triple-fluorolabeled with an anti-alpha-synuclein antibody, an anti-ubiquitin antibody and thiazin red (TR), a fluorochrome that labels fibrillary structures such as Lewy bodies or neurofibrillary tangles. One of the paired sections was subsequently stained using the Campbell-Switzer method (CS), and the other by the Gallyas-Braak method (GB). By comparing of the same microscopic field on the paired fluorolabeled sections, subsequently silver-stained with either CS or GB, five different profiles of each structure could be determined: alpha-synuclein-like IR, ubiquitin-like IR, affinity to TR, argyrophilia with CS or GB. GCIs exhibited argyrophilia with both CS and GB but lacked affinity to TR. In contrast, LBs exhibited argyrophilia with CS but not with GB and some affinity to TR. These disease-specific profiles of argyrophilia were consistent, and were not influenced by areas or cases examined. Although immunohistochemical features of LBs and GCIs were similar in exhibiting IR for alpha-synuclein and ubiquitin, the contrast in their argyrophilic profiles may indicate possible differences in the molecular composition or conformation of alpha-synuclein. Even though these empirical differences still remain to be explained, awareness of this clear distinction is potentially of diagnostic and pathological relevance.