Ono K, Uchino F
Ono Geka Clinic, Fukuoka, Japan.
Nephron. 1994;66(4):404-7. doi: 10.1159/000187854.
Although the pathogenesis has yet to be fully understood, beta 2-microglobulin (beta 2m) related amyloidosis is a frequent complication in long-term hemodialysis (HD) patients. In an attempt to clarify the association of two potential candidates with amyloidogenesis from beta 2m in HD patients, human urine-derived beta 2m solution alone or combined with glycosaminoglycans: hyaluronic acid, heparan sulfate, or serum amyloid P component (SAP) were dialyzed against physiological buffered solution (pH 7.4) using a microdialyzer in vitro for 72 h at 4 degrees C. This study demonstrates for the first time that SAP can play a crucial role in the formation of amyloid-like fibrils from beta 2m. This occurs by a direct influence on either the processing of a precursor protein, or protein folding, in vitro, by a short-period dialysis against a physiological buffered solution.
尽管其发病机制尚未完全明确，但β2微球蛋白（β2m）相关的淀粉样变性是长期血液透析（HD）患者常见的并发症。为了阐明HD患者中两种潜在候选物与β2m淀粉样变形成的关联，将单独的人尿源性β2m溶液或与糖胺聚糖（透明质酸、硫酸乙酰肝素）或血清淀粉样蛋白P成分（SAP）混合的溶液，在4℃下使用微透析器在体外与生理缓冲溶液（pH 7.4）进行72小时透析。本研究首次证明，SAP在β2m形成淀粉样纤维的过程中可发挥关键作用。这是通过在体外对生理缓冲溶液进行短期透析，直接影响前体蛋白的加工或蛋白质折叠而发生的。
