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目的:分析老年性关节病组织内是否存在淀粉样变沉积,为解析导致淀粉样变形成机制奠定基础。方法选择骨关节病进行手术治疗患者88例,男46例,50~74岁,女42例,53~72岁;同时作为对照组筛选外伤关节手术患者14例,男8例,年龄58~75岁,女6例,年龄57~77岁。留取关节组织进行刚果红染色,结合偏振光观察组织内是否存在淀粉样变。另外,利用组织标本进行immunoglobulin light chain (AL -kappa)、immunoglobulin light chain(AL -lambda)、transthyretin (TTR)、2-microglobulin (2-M)和serum amyloid A (SAA)五种抗体免疫组织化学染色。利用Matrix -assisted laser desorption -ioniza‐ton/time of flight mass spectrometry (MALDI-TOF MS)系统分析 TTR基因突变型。结果在骨关节病患者关节组织内发现Congo Red染色阳性并且可见偏振光显微镜绿色荧光,阳性率为26.1%(23/88),利用TTR、SAA、免疫球蛋白轻链等五种抗体进行免疫组织化学染色,发现有 TTR和AL -kappa两种淀粉样变蛋白,其发生率为T T R 22.7%,A L -kappa为3.4%,且 T T R基于型均未发现有突变型。结论发现老年性骨关节病组织内出现淀粉样变,免疫组织化学方法发现 T T R和A L -kappa两种类型相关淀粉样变。“,”Objective To comprehensively investigate the expresssion of amyloid protein in joint tissues of patients with osteoarthritis(OA) ,and the frequency and subtypes of amyloid deposition in OA were ana‐lyzed as well .Methods All joint sections were recruited from 88 patients with end-stage OA who under‐went joint replacement surgery .The diagnosis of amyloidosis was identified by Congo red staining ,which demonstrate typical apple-green birefringence under polarized microscope .Immunohistochemically ,amy‐loid joint specimens were characterized by the expressions of immunoglobulin light chain (AL -κ,AL -λ) , transthyretin (TTR) ,2-microglobulin ( 2-M) and serum amyloid A (SAA) in patients with OA .Ma‐trix -assisted laser desorption -ionizaton/time of flight mass spectrometry (MALDI-TOF MS) was used to analyze TTR variants .Results The Congo Red Staining was found to be positive in 26 .1% (23/88) pa‐tients with OA .However ,two cases were shown to be Congo red -positive without the appearance of ap‐ple green birefringence under polarized microscope ,which may indicate the phenomenon of pre -amyloid deposition .Then ,the expressions of five precursor proteins in 88 amyloid joint tissues of OA patients wereevaluated by immunohistochemical methods .Among them ,twenty cases (22 .7% ) were anti-TTR posi‐tive ,and three tissue sections (3 .4% ) were shown to be anti -AL -kappa immunoreactive in our cohort . Besides ,there was no co -existence for both TTR and AL -kappa in any tissues involved ,while AL -lambda ,2-M and SAA were not expressed in joint tissues of OA patients .Finally ,using a combination of immunoprecipitation and the subsequent MALDI -TOF -MS ,TTR could be determined as the wild -type ,TTR-Cys10-S -S-Cys and TTR-Cys10-S-S-CysGly .Conclusion According to our knowl‐edge by far ,this is the first report about two types of amyloid deposition in joint tissues of OA patients with majority of TTR(native ,S -Cys and S -CysGly) followed by AL -kappa type .