MacLean I L, Lowdell M W, Blake D R, Lunec J, Archer J R
Inflammation Group, London Hospital Medical College, United Kingdom.
Ann Rheum Dis. 1992 Aug;51(8):963-4. doi: 10.1136/ard.51.8.963.
The spondylitis associated HLA-B27 epitope includes a characteristic unpaired cysteine at amino acid position 67. On some B27 molecules the thiol (-SH) side chain of this residue seems to be available for chemical interactions. The possibility that free radicals produced during inflammation might specifically affect this group was investigated in this work. Cells bearing HLA-B27 were exposed to free radicals generated by ultraviolet irradiation or hydrogen peroxide, and HLA antigens were then measured by flow cytometry. Binding of monoclonal antibodies to B27 was not affected. These results do not support a specific susceptibility of HLA-B27 to damage by free radicals, despite its apparently vulnerable structure.
与脊柱炎相关的HLA - B27表位在氨基酸位置67处包含一个特征性的未配对半胱氨酸。在一些B27分子上,该残基的硫醇(-SH)侧链似乎可用于化学相互作用。本研究探讨了炎症过程中产生的自由基是否可能特异性影响该基团。将携带HLA - B27的细胞暴露于紫外线照射或过氧化氢产生的自由基中,然后通过流式细胞术检测HLA抗原。单克隆抗体与B27的结合不受影响。尽管HLA - B27结构明显易损,但这些结果并不支持其对自由基损伤具有特异性易感性。