在淀粉样变性的组织学消退后，体内存在一种预激发状态。
A primed state exists in vivo following histological regression of amyloidosis.
作者信息
Hawkins P N, Pepys M B
机构信息
Department of Medicine, Royal Postgraduate Medical School, London, England, UK.
出版信息
Clin Exp Immunol. 1990 Aug;81(2):325-8. doi: 10.1111/j.1365-2249.1990.tb03339.x.
Abstract
Using a sensitive, quantitative, and non-invasive in vivo method, based on the specific binding of serum amyloid P component to amyloid fibrils, we have directly documented the spontaneous resolution of AA amyloid deposits in mice, and the prolonged existence thereafter of a primed state of enhanced susceptibility to further amyloid deposition. These results may have important implications for understanding and management of amyloidosis in humans.
摘要
我们采用了一种基于血清淀粉样蛋白P成分与淀粉样纤维特异性结合的灵敏、定量且非侵入性的体内方法，直接记录了小鼠体内AA淀粉样沉积物的自发消退，以及此后对进一步淀粉样沉积易感性增强的预激发状态的长期存在。这些结果可能对理解和治疗人类淀粉样变性具有重要意义。
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Clin Exp Immunol. 1986 Dec;66(3):691-700.
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Specific localization and imaging of amyloid deposits in vivo using 123I-labeled serum amyloid P component.使用123I标记的血清淀粉样蛋白P成分在体内对淀粉样沉积物进行特异性定位和成像。
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