Konohana A, Teraki Y, Tajima S, Araki Y, Kitamura K, Nishikawa T
Department of Dermatology, Nippon Kokan Hospital, Kawasaki, Japan.
Dermatologica. 1991;183(2):114-9. doi: 10.1159/000247649.
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.
我们报告了一例原发性局限性皮肤结节性淀粉样变伴头皮病变的患者。全面检查未发现系统性受累。对淀粉样沉积物中糖胺聚糖(GAGs)的分析显示,与正常皮肤相比增加了两倍,这是由于硫酸皮肤素增加所致。GAG代谢的局部紊乱可能与淀粉样纤维的形成有关。淀粉样纤维经纯化并通过电子显微镜鉴定,其由两种主要的12,000道尔顿和13,000道尔顿以及两种次要的29,000道尔顿和48,000道尔顿的肽组成。蛋白质印迹分析显示一种次要的29,000道尔顿肽与针对免疫球蛋白κ和λ轻链的抗体发生反应。在某些原发性局限性皮肤结节性淀粉样变病例中,淀粉样变的某些成分可能由κ和λ免疫球蛋白轻链组成。