Carsons S, Lavietes B B, Diamond H S
J Lab Clin Med. 1983 Nov;102(5):722-31.
Methods of synovial fluid collection and processing known to affect cryoprotein formation were examined to investigate the proposed role of fibronectin in synovial fluid cryoprecipitation. Fibronectin, a nonimmunoglobulin, noncomplement synovial fluid protein was present in all resolubilized synovial fluid cryoproteins studied. Radiolabeled fibronectin was precipitated from rheumatoid synovial fluid to a significantly greater extent (10%) than from noninflammatory (osteoarthritic) synovial fluid (2.8%), normal plasma (1.3%), or normal serum (0.5%) (p less than 0.01). Clotting of synovial fluid reduced fibronectin concentration 44% and resulted in a reduction in the amount and percent incorporation of fibronectin into cryoprotein, whereas heparinization and hyaluronidase treatment increased cryoprecipitable fibronectin. Affinity depletion of synovial fluid fibronectin resulted in loss of C1q and reduction in IgG in the cryoprotein; however, fibronectin, C1q, and IgG could not be co-eluted from affinity matrices of gelatin and protein A-Sepharose. Cryoprotein formation from pathologic synovial fluid depends in part on fibronectin and appears to involve interactions between fibronectin and fibrinogen as well as immunoglobulin complexes and complement components.
为了研究纤连蛋白在滑膜液冷沉淀中的假定作用，对已知会影响冷球蛋白形成的滑膜液采集和处理方法进行了研究。纤连蛋白是一种非免疫球蛋白、非补体的滑膜液蛋白，在所研究的所有重新溶解的滑膜液冷沉淀物中均存在。与非炎性（骨关节炎）滑膜液（2.8%）、正常血浆（1.3%）或正常血清（0.5%）相比，放射性标记的纤连蛋白从类风湿性滑膜液中的沉淀程度明显更高（10%）（p小于0.01）。滑膜液的凝血使纤连蛋白浓度降低了44%，并导致纤连蛋白掺入冷球蛋白的量和百分比减少，而肝素化和透明质酸酶处理则增加了可冷沉淀的纤连蛋白。滑膜液纤连蛋白的亲和去除导致冷沉淀物中C1q丢失和IgG减少；然而，纤连蛋白、C1q和IgG不能从明胶和蛋白A-琼脂糖亲和基质上共同洗脱。病理性滑膜液中冷球蛋白的形成部分取决于纤连蛋白，似乎涉及纤连蛋白与纤维蛋白原以及免疫球蛋白复合物和补体成分之间的相互作用。
