Maury C P, Teppo A M, Karinemi A L, Koeppen A H
Fourth Department of Medicine, University of Helsinki, Finland.
Am J Clin Pathol. 1988 Mar;89(3):359-64. doi: 10.1093/ajcp/89.3.359.
Immunocytochemical methods were used to study the nature of the amyloid deposits in the Finnish type-familial amyloid polyneuropathy (FAP) type IV, which is characterized by cranial neuropathy and corneal lattice dystrophy. Commercial antisera to human plasma transthyretin (prealbumin) did not stain the amyloid deposits, but in every case a positive staining was obtained with antibodies raised against transthyretin-related amyloid fibril whole protein isolated from the myocardium of a patient with familial amyloid polyneuropathy from the state of New York. The FAP type IV amyloid deposits stained also with antiserum to serum amyloid P component, but did not stain with antisera to retinol-binding protein, amyloid A protein, gamma-trace protein, beta 2-microglobulin, or immunoglobulin light chains. The serum level of serum transthyretin was significantly decreased in FAP type IV patients (256 +/- 75 (SD) mg/L, n = 15) as compared with Finnish control subjects (360 +/- 56 mg/L, n = 30, P less than 0.001), whereas the level of retinol-binding protein was within the normal range. The results of this study strongly suggest that the amyloid fibril protein in FAP type IV amyloidosis is related to transthyretin.
免疫细胞化学方法用于研究IV型芬兰型家族性淀粉样多神经病（FAP）中淀粉样沉积物的性质，该病以颅神经病变和角膜格子状营养不良为特征。针对人血浆转甲状腺素蛋白（前白蛋白）的商业抗血清未使淀粉样沉积物染色，但在每种情况下，用从纽约州一名家族性淀粉样多神经病患者心肌中分离出的与转甲状腺素蛋白相关的淀粉样原纤维全蛋白产生的抗体获得了阳性染色。IV型FAP淀粉样沉积物也用针对血清淀粉样P成分的抗血清染色，但未用针对视黄醇结合蛋白、淀粉样A蛋白、γ-微量蛋白、β2-微球蛋白或免疫球蛋白轻链的抗血清染色。与芬兰对照受试者（360±56mg/L，n = 30，P<0.001）相比，IV型FAP患者的血清转甲状腺素蛋白水平显著降低（256±75（SD）mg/L，n = 15），而视黄醇结合蛋白水平在正常范围内。本研究结果强烈表明，IV型淀粉样变性中的淀粉样原纤维蛋白与转甲状腺素蛋白有关。
