Primary localized cutaneous nodular amyloidosis: case report and biochemical analysis of amyloid.

Dermatologica Pub Date : 1991-01-01 DOI:10.1159/000247649
A Konohana, Y Teraki, S Tajima, Y Araki, K Kitamura, T Nishikawa
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引用次数: 7

Abstract

We report a patient with scalp lesions of primary localized cutaneous nodular amyloidosis. The extensive examination revealed no systemic involvement. Analysis of glycosaminoglycans (GAGs) in amyloid deposits showed a twofold increase as compared with normal skin, which was due to the increase in dermatan sulfate. Local disorders of GAG metabolism may be related to the amyloid fibril formation. Amyloid fibrils were purified and identified electron-microscopically, which consisted of two major 12,000- and 13,000-dalton and minor 29,000- and 48,000-dalton peptides. Western blotting analysis showed a minor 29,000-dalton peptide reactive with antibodies against both kappa and lambda light chains of immunoglobulin. There is a possibility that some components of amyloid in some cases of primary localized cutaneous nodular amyloidosis may consist of both kappa and lambda immunoglobulin light chains.

原发性皮肤局部结节性淀粉样变性:1例报告及淀粉样蛋白生化分析。
我们报告一个病人的头皮病变原发性局限性皮肤结节淀粉样变。广泛检查未发现全身病变。淀粉样蛋白沉积物中的糖胺聚糖(GAGs)分析显示,与正常皮肤相比,其含量增加了两倍,这是由于皮肤硫酸酯的增加。局部GAG代谢紊乱可能与淀粉样纤维的形成有关。淀粉样蛋白原纤维由两个主要的12,000和13,000道尔顿肽和次要的29,000和48,000道尔顿肽组成。Western blotting分析显示,该蛋白与免疫球蛋白kappa和lambda轻链抗体均有轻微的29,000道尔顿肽反应。在一些原发性局限性皮肤结节性淀粉样变性病例中,淀粉样蛋白的某些成分可能由免疫球蛋白轻链和免疫球蛋白轻链组成。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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