Ito K, Hashimoto K, Kambe N, Van S
Department of Dermatology and Syphilology, Wayne State University School of Medicine, Detroit, Michigan 48201.
J Invest Dermatol. 1987 Oct;89(4):415-8. doi: 10.1111/1523-1747.ep12471778.
Immunoglobulin heavy and light chains and C3 were detected on amyloid deposits in cutaneous nodular amyloidosis (NA) by a direct immunofluorescence method. These immunoglobulin chains and C3 could be removed except lambda (lambda) light chain after treating sections with 0.05% Tween 20 solution, 0.1 M glycine buffer pH 7.4 or 0.5% Triton X solution. Lambda light chain was detected consistently after these treatments. Amyloid filaments were not altered with these treatments. Immunoelectron microscopy demonstrated persistent antigenicity of lambda light chain on amyloid filaments. It was suggested that lambda light chain is an inherent component of amyloid filaments in NA, whereas other chains and complement represent nonessential absorption on amyloid material.
采用直接免疫荧光法在皮肤结节性淀粉样变（NA）的淀粉样沉积物上检测到免疫球蛋白重链和轻链以及C3。在用0.05%吐温20溶液、pH 7.4的0.1M甘氨酸缓冲液或0.5% Triton X溶液处理切片后，除λ（lambda）轻链外，这些免疫球蛋白链和C3均可被去除。经过这些处理后，始终能检测到λ轻链。淀粉样细丝在这些处理后未发生改变。免疫电子显微镜显示λ轻链在淀粉样细丝上具有持续的抗原性。提示λ轻链是NA中淀粉样细丝的固有成分，而其他链和补体则代表淀粉样物质上的非必需吸附。
