Westermark P, Sletten K, Pitkänen P, Natvig J B, Lindholm C E
Mol Immunol. 1982 Mar;19(3):447-50. doi: 10.1016/0161-5890(82)90210-3.
Amyloid fibrils were extracted from a patient Wr with more than 10 yr history of localized laryngeal amyloidosis. Degraded amyloid fibrils reacted in immunodiffusion with an antiserum against an amyloid protein of immunoglobulin kappa light chain origin, showing a line of identity with a kappa I amyloid protein. The protein Wr had a blocked aminoterminal, previously only reported in lambda chains. Amino acid sequence analysis of a fragment of the protein showed it to be an immunoglobulin light chain protein of V kappa I or V kappa III subgroup. The protein had a few unusual amino acid residues as compared to other kappa light chains. The findings support the view that the fibrils in localized, tumour-like amyloidosis are composed by homogeneous immunoglobulin light chain proteins in the same way as is seen in primary and myeloma associated systemic amyloidosis. It is possible that unusual light chains are over-represented in amyloid fibrils.
淀粉样纤维取自一位患有局限性喉淀粉样变性病史超过10年的Wr患者。降解后的淀粉样纤维在免疫扩散中与抗免疫球蛋白κ轻链来源的淀粉样蛋白抗血清发生反应，显示出与κI淀粉样蛋白的一条同一性沉淀线。Wr蛋白的氨基末端被封闭，此前仅在λ链中报道过。该蛋白片段的氨基酸序列分析表明它是VκI或VκIII亚组的免疫球蛋白轻链蛋白。与其他κ轻链相比，该蛋白有一些不寻常的氨基酸残基。这些发现支持了这样一种观点，即局限性、肿瘤样淀粉样变性中的纤维与原发性和骨髓瘤相关的系统性淀粉样变性一样，由同质的免疫球蛋白轻链蛋白组成。淀粉样纤维中不寻常的轻链可能占比过高。
