Schwaber J F, Rosen F S
J Immunol. 1979 May;122(5):1849-54.
Somatic cell hybrid clones were isolated from the fusion of RPC5.4 mouse myeloma cells and B lymphocytes from a patient with common varied agammaglobuinemia. The patient has B lymphocytes that synthesize immunoglobulin but fail to secrete immunoglobulin. The hybrid character of the six clones was established by examination of metaphase chromosome spreads. Most of the hybrid clones expressed mouse and human surface immunoglobulin. All of the clones synthesized immunoglobulin of mouse and human parental origin. Mouse parental immunoglobulin was secreted, whereas the human parental immunoglobulin was not secreted. Human light chain molecules were secreted as part of hybrid H2L2 molecules formed with mouse heavy chains. Human heavy chains had a reduced m.w. in comparison to the mouse heavy chains. Kinetic experiments indicated that human Ig was synthesized in amounts that were comparable to the mouse Ig. Pulse-chase experiments showed that that the intracellular human Ig was removed from the cytoplasm, probably by degradation. These experiments demonstrate that the hybrid cells are an in vitro model of naturally occurring failure of immunoglobulin secretion from agammaglobulinemia. The failure of fusion with mouse myeloma cells to complement the secretion defect suggests that these B cells produce an altered immunoglobulin molecule that is not programmed for secretion.
从RPC5.4小鼠骨髓瘤细胞与一名普通变异型无丙种球蛋白血症患者的B淋巴细胞融合物中分离出体细胞杂交克隆。该患者的B淋巴细胞能合成免疫球蛋白，但无法分泌免疫球蛋白。通过检查中期染色体铺展确定了六个克隆的杂交特性。大多数杂交克隆表达小鼠和人类表面免疫球蛋白。所有克隆都合成了源自小鼠和人类亲本的免疫球蛋白。小鼠亲本免疫球蛋白被分泌，而人类亲本免疫球蛋白未被分泌。人类轻链分子作为与小鼠重链形成的杂交H2L2分子的一部分被分泌。与小鼠重链相比，人类重链的分子量降低。动力学实验表明，人类Ig的合成量与小鼠Ig相当。脉冲追踪实验表明，细胞内的人类Ig可能通过降解从细胞质中去除。这些实验证明，杂交细胞是无丙种球蛋白血症中自然发生的免疫球蛋白分泌失败的体外模型。与小鼠骨髓瘤细胞融合未能弥补分泌缺陷表明，这些B细胞产生了一种未被编程用于分泌的改变的免疫球蛋白分子。
