Aruga E, Ozasa H, Teraoka S, Ota K
Department of Surgery, Tokyo Women's Medical College.
Lab Invest. 1993 Aug;69(2):223-30.
Common elements in many different types of amyloid may have important roles in amyloidogenesis. The proteinaceous tissue deposits have a common appearance in polarized light and other similar features. The present investigation describes for the first time the relation between beta 2-microglobulin (beta 2-M)-type amyloidosis and colocalized materials, as demonstrated using specific antibodies and hyaluronan-binding protein.
Amyloid-rich carpal tunnel synovium was obtained surgically from 28 patients who were being treated by maintenance hemodialysis. Serial sections were examined using a hyaluronan (hyaluronic acid)-binding protein and antibodies against heparan sulfate-glycosaminoglycan, chondroitin sulfate-proteoglycan, dermatan sulfate-proteoglycan, alpha 1-antichymotrypsin, alpha 1-antitrypsin, inter-alpha-trypsin inhibitor, haptoglobin, and ubiquitin.
Accumulation of hyaluronan was of three types, namely, localization around beta 2-M deposits, colocalization with deposition of beta 2-M itself and localization at a small distance from beta 2-M deposits. Immunostaining for heparan sulfate glycosaminoglycan was demonstrated at the sites of beta 2-M plaques. Chondroitin sulfate-proteoglycan did not show specific patterns of immunostaining, resembling hyaluronan rather than heparan sulfate. The other materials tested, alpha 1-antichymotrypsin, alpha 1-antitrypsin, inter-alpha-trypsin, haptoglobin and ubiquitin, were not immunostained at sites of beta 2-M plaques. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting revealed that the molecular weight of heparan sulfate-glycosaminoglycan was 16,000.
These results suggest that HS has an important role in hemodialysis-associated amyloidosis as it does in other types of amyloidosis. Moreover, accumulation of hyaluronan may be an indication of inflammation of the carpal synovium.
许多不同类型淀粉样蛋白中的共同成分可能在淀粉样蛋白生成过程中发挥重要作用。蛋白质组织沉积物在偏振光下具有共同外观及其他相似特征。本研究首次描述了β2-微球蛋白（β2-M）型淀粉样变性与共定位物质之间的关系，这是通过使用特异性抗体和透明质酸结合蛋白来证明的。
从28例接受维持性血液透析治疗的患者中手术获取富含淀粉样蛋白的腕管滑膜。使用透明质酸结合蛋白以及针对硫酸乙酰肝素-糖胺聚糖、硫酸软骨素-蛋白聚糖、硫酸皮肤素-蛋白聚糖、α1-抗糜蛋白酶、α1-抗胰蛋白酶、α1-抗胰蛋白酶抑制剂、触珠蛋白和泛素的抗体对连续切片进行检查。
透明质酸的积累有三种类型，即定位于β2-M沉积物周围、与β2-M自身沉积共定位以及定位于距β2-M沉积物有一小段距离处。在β2-M斑块部位显示出硫酸乙酰肝素糖胺聚糖的免疫染色。硫酸软骨素-蛋白聚糖未显示出特异性免疫染色模式，与透明质酸相似而非硫酸乙酰肝素。所检测的其他物质，α1-抗糜蛋白酶、α1-抗胰蛋白酶、α1-抗胰蛋白酶抑制剂、触珠蛋白和泛素，在β2-M斑块部位未被免疫染色。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和免疫印迹显示硫酸乙酰肝素-糖胺聚糖的分子量为16,000。
这些结果表明，硫酸乙酰肝素在血液透析相关淀粉样变性中与在其他类型淀粉样变性中一样发挥重要作用。此外，透明质酸的积累可能是腕关节滑膜炎症的一个指标。
