Portal amyloid: novel amyloid deposits in gastrointestinal veins?
Portal amyloid: novel amyloid deposits in gastrointestinal veins?
复制标题
门静脉淀粉样蛋白：胃肠静脉中新的淀粉样蛋白沉积物？
DOI：
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发表时间：
1996
影响因子：
4.6
通讯作者：
R. Linke
中科院分区：
文献类型：
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作者：
C. Rocken;W. Saeger;R. Linke
目的
详细说明老年人胃肠血管中的非特征性淀粉样蛋白沉积。
材料和方法
采用刚果红染色法对110例85岁及85岁以上患者的连续尸检胃肠道进行淀粉样蛋白检查。使用针对淀粉样蛋白A、载脂蛋白A-I、载脂蛋白A-II、载脂蛋白B、载脂蛋白C-I、溶菌酶、λ和κ轻链淀粉样蛋白原纤维蛋白、甲状腺素运载蛋白、β 2-微球蛋白和淀粉样蛋白P组分的抗血清进行淀粉样蛋白沉积物的免疫组织化学分类。电镜检查评价超微结构特征。
结果
110例中38例（35%）有胃肠道淀粉样蛋白沉积。在17例病例中，淀粉样纤维蛋白被化学鉴定。在5例（5%）中，淀粉样蛋白无法分类，因为淀粉样蛋白沉积物不存在于用于免疫组织化学的较深连续切片中。在13例（11%）血管淀粉样蛋白沉积无法表征，因为他们没有表现出免疫反应性与任何一个面板的纤维蛋白的所有主要脑外淀粉样蛋白的特异性抗体。在三个单独的情况下，血管淀粉样蛋白沉积物显示出可变的免疫反应性，与存款是阴性的一些血管。在这16例病例中，化学上无反应的血管淀粉样蛋白有几个一致的特征：它只影响小肠和大肠的血管，局限于肠系膜静脉，它由位于碎片弹性纤维附近的小圆点或逗号样沉积物组成，并且它表现出淀粉样蛋白P组分的免疫染色不一致。
结论
无反应性的胃肠道淀粉样沉积物（我们称之为“门脉淀粉样沉积物”）具有相似的形态学特征，提示它们有共同的起源。确定门静脉淀粉样蛋白是否代表一种新的淀粉样蛋白需要化学分析。
OBJECTIVE
To specify uncharacterized amyloid deposits in gastrointestinal vessels of the elderly.
MATERIALS AND METHODS
The gastrointestinal tracts from 110 consecutive autopsies of individuals aged 85 years and older were examined for amyloid using Congo red staining. Immunohistochemical classification of the amyloid deposits was conducted using antisera directed against amyloid A, apolipoprotein A-I, apolipoprotein A-II, apolipoprotein B, apolipoprotein C-I, lysozyme, lambda and kappa light chain amyloid fibril proteins, transthyretin, beta2-microglobulin, and amyloid P component. Electron microscopic examination assessed the ultrastructural features.
RESULTS
Thirty-eight (35%) of the 110 cases had gastrointestinal amyloid deposits. In 17 cases the amyloid fibril proteins were defined immunohistochemically. In five cases (5%) the amyloid could not be classified because amyloid deposits were not present in the deeper serial sections used for immunohistochemistry. In 13 cases (11%) the vascular amyloid deposits could not be characterized because they did not demonstrate immunoreactivity with any of a panel of antibodies specific for the fibril proteins of all major extracerebral amyloids. In three individual cases, the vascular amyloid deposits showed variable immunoreactivity, with deposits being negative in some vessels. The immunohistochemically nonreactive vascular amyloid in these 16 cases had several consistent features: it affected only vessels of the small and large intestine, it was limited to mesenteric veins, it consisted of small dot- or comma-like deposits located in close proximity to fragmented elastic fibers, and it demonstrated inconsistent immunostaining for amyloid P component.
CONCLUSIONS
The similar morphologic characteristics of nonreactive gastrointestinal amyloid deposits, which we have designated "portal amyloid," suggest a common origin. Determination of whether portal amyloid represents a new type of amyloid will require chemical analysis.