Thompson H L, Matsushima K
Strangeways Research Laboratory, Cambridge, UK.
Clin Exp Immunol. 1992 Nov;90(2):280-5. doi: 10.1111/j.1365-2249.1992.tb07943.x.
The present study demonstrates that tumour necrosis factor (TNF) and FMLP, but not IL-1 or IL-8, enhanced the adherence of polymorphonuclear neutrophil (PMN) to fibronectin, an extracellular matrix protein. The adherence induced by FMLP was very rapid, within 5 min while the induction of adherence by TNF was much slower, reaching maximum at 60 min. TNF also enhanced an adhesion of PMN to other extracellular matrix proteins, such as laminin, collagen IV and gelatin II, but not to human serum albumin. Anti-CD18 MoAb completely inhibited the binding of TNF-stimulated PMN to fibronectin and partially inhibited the binding to laminin. Further investigation showed that adhesion of TNF-stimulated PMN to fibronectin and laminin was inhibited by anti-CD11b MoAb and to a lesser extent by CD11a MoAb. In contrast to TNF-stimulated PMN the binding of unstimulated PMN to fibronectin and laminin was only inhibited by anti-CD11a MoAb. Anti-CD11c had no effect on PMN adherence. These results suggest that unstimulated PMN adhere to extracellular proteins through the CD11a/18, while TNF-stimulated PMN adhere through the CD11b/18. These results suggest that TNF secreted at the site of inflammation may enhance the interaction of PMN with the extravascular environment through the CD11b/18 complex.
本研究表明，肿瘤坏死因子（TNF）和N-甲酰甲硫氨酰-亮氨酰-苯丙氨酸（FMLP），而非白细胞介素-1（IL-1）或白细胞介素-8（IL-8），可增强多形核中性粒细胞（PMN）与细胞外基质蛋白纤连蛋白的黏附。FMLP诱导的黏附非常迅速，在5分钟内即可发生，而TNF诱导的黏附则要慢得多，在60分钟时达到最大值。TNF还增强了PMN与其他细胞外基质蛋白（如层粘连蛋白、IV型胶原和明胶II）的黏附，但对人血清白蛋白无此作用。抗CD18单克隆抗体（MoAb）完全抑制了TNF刺激的PMN与纤连蛋白的结合，并部分抑制了与层粘连蛋白的结合。进一步研究表明，抗CD11b MoAb可抑制TNF刺激的PMN与纤连蛋白和层粘连蛋白的黏附，而抗CD11a MoAb的抑制作用较小。与TNF刺激的PMN不同，未刺激的PMN与纤连蛋白和层粘连蛋白的结合仅被抗CD11a MoAb抑制。抗CD11c对PMN的黏附无影响。这些结果表明，未刺激的PMN通过CD11a/18黏附于细胞外蛋白，而TNF刺激的PMN则通过CD11b/18黏附。这些结果表明，在炎症部位分泌的TNF可能通过CD11b/18复合物增强PMN与血管外环境的相互作用。
