Aston W P, Ward T L, Cooke T D
Clin Exp Immunol. 1983 May;52(2):280-6.
Porcine hyaline articular cartilage (HAC) has been used to investigate the interaction of bovine serum albumin (BSA) and anti-BSA with articular collagenous tissues in vitro. There was a marked retention of 125I-labelled BSA by plugs of HAC (a) exposed to rabbit anti-BSA for 1-2 h at 37 degrees C prior to a similar incubation with the antigen, or (b) exposed to the antigen and then to antibody. The specifically retained radiolabelled BSA was localized in or at the articular surface of the plugs. In the absence of specific antibody a relatively small amount of the antigen was retained. Exposure of HAC to multiple cycles of antibody and antigen treatment resulted in an increased retention of the 125I-BSA. There was a concomitant increase in the retention of the anti-BSA and the capacity of the treated plugs to fix complement. The forces that maintained the labelled antigen in the tissue were not readily reversed by excess unlabelled BSA. Pre-formed, soluble BSA/anti-BSA complexes did not appear to penetrate the tissue unless the HAC was first exposed to anti-BSA. The results suggest that the antibody-mediated, surface oriented retention of 125I-BSA results from the formation of immune complexes in the tissue.
猪透明关节软骨（HAC）已被用于体外研究牛血清白蛋白（BSA）及抗BSA与关节胶原组织的相互作用。HAC小块对125I标记的BSA有显著保留：（a）在与抗原进行类似孵育之前，于37℃下与兔抗BSA孵育1 - 2小时；或（b）先与抗原接触，然后再与抗体接触。特异性保留的放射性标记BSA定位于小块的关节表面或其表面。在没有特异性抗体时，仅保留相对少量的抗原。HAC经多次抗体和抗原处理循环后，对125I - BSA的保留增加。同时，抗BSA的保留以及处理后的小块固定补体的能力也增加。维持组织中标记抗原的力不易被过量未标记的BSA逆转。预先形成的可溶性BSA/抗BSA复合物似乎不会穿透组织，除非HAC先接触抗BSA。结果表明，抗体介导的、表面定向的125I - BSA保留是由于组织中免疫复合物的形成。
