Hester R B, Kubo R T, Grey H M
Scand J Immunol. 1979;9(2):125-34. doi: 10.1111/j.1365-3083.1979.tb02714.x.
The mechanism by which exogenously added beta2m binds to lymphoid cells has been explored. In the mouse it has been shown that beta2m remains associated with plasma membrane macromolecules following solubilization with NP-40 and that approximately 25-30% of the binding could be accounted for by binding to H-2 antigens. No binding to mouse immunoglobulin or Ia antigens could be detected. The sites for binding of the remainder of the cell-bound beta2m were not determined. Whereas normal human lymphocytes showed little or no capacity to bind exogenously added beta2m, it was found that phytohaemagglutinin (PHA)-stimulated cells could bind beta2m. This binding occurred optimally 2 days after PHA stimulation. Approximately half of the binding could be accounted for by binding to HLA antigens. The possible significance of these findings with respect to cellular interactions involving major histocompatibility complex gene products in the immune response is discussed.
已对体外添加的β2微球蛋白（β2m）与淋巴细胞结合的机制进行了探索。在小鼠中，研究表明，用NP - 40溶解后，β2m仍与质膜大分子结合，并且约25 - 30%的结合可归因于与H - 2抗原的结合。未检测到与小鼠免疫球蛋白或Ia抗原的结合。细胞结合的β2m其余部分的结合位点尚未确定。正常人类淋巴细胞对外源添加的β2m几乎没有或没有结合能力，而发现植物血凝素（PHA）刺激的细胞能够结合β2m。这种结合在PHA刺激后2天达到最佳。约一半的结合可归因于与HLA抗原的结合。讨论了这些发现对于免疫反应中涉及主要组织相容性复合体基因产物的细胞相互作用的可能意义。
