Immunocytochemical identification of amyloid in formalin-fixed paraffin sections.
Immunocytochemical identification of amyloid in formalin-fixed paraffin sections.
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福尔马林固定石蜡切片中淀粉样蛋白的免疫细胞化学鉴定。
DOI：
10.1007/bf00517130
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发表时间：
1981
期刊：
影响因子：
--
通讯作者：
Cohen,AS
中科院分区：
文献类型：
--
作者：
Shirahama,T;Skinner,M;Cohen,AS
用免疫细胞化学方法(未标记抗体酶)，对原发性、继发性和家族性淀粉样变性患者的肝、脾、肾和酪蛋白诱导的小鼠淀粉样变性模型的肝、脾、肾进行了免疫细胞化学分析。所有类型的淀粉样蛋白沉淀物与相应种类的抗AP呈阳性反应。抗人AA与人次级淀粉样蛋白沉积呈阳性反应，抗鼠AA与酪蛋白诱导的小鼠淀粉样蛋白沉积呈阳性反应，但无种属交叉反应。抗免疫球蛋白轻链在任何淀粉样蛋白类型的沉积物上，或在原发或家族性淀粉样变性的组织中，抗AA没有产生显著的反应产物沉积。结果表明，淀粉样蛋白AA和AP可以通过常规的组织学制备作为抗原存活，抗AP可以作为同一物种内任何淀粉样蛋白沉积的通用标记物，AA型淀粉样蛋白可以用这种方法识别，而AL型目前可能还没有可行的通用标记物。
Formalin-fixed paraffin sections of livers, spleens and kidneys from patients with primary, secondary and familial amyloidosis as well as from a casein-induced murine amyloid model were analysed by an immunocy-tochemical (unlabeled antibody enzyme) method utilizing antisera to amyloid-related proteins. All amyloid deposits of all amyloid types showed positive reactions with anti-AP of the respective species. Positive reaction of anti-human AA to human secondary amyloid deposits and of anti-mouse AA to the deposits of casein-induced murine amyloid was also observed, but there was no species cross reactivity. No significant deposition of the reaction products was produced by anti-immunoglobulin light chains on deposits of any amyloid type, or by anti-AA in the tissues from primary or familial amyloidosis. The results indicate that amyloid proteins AA and AP can survive as antigens through routine histologic preparation, that anti-AP can be a universal marker for deposits of any amyloid type within the same species, and that AA-type amyloid can be identified by this method while there may as yet be no feasible universal marker for the AL-type at present.