Rabourdin-Combe C, Dorf M E, Guimezanes A, Fridman W H
Eur J Immunol. 1979 Mar;9(3):237-42. doi: 10.1002/eji.1830090313.
An immunoglobulin binding factor (IBF) produced by in vivo alloantigen-activated T cells suppresses in vitro antibody production to sheep red blood cells (SRBC) and probably represents the soluble form of the T cell Fc receptor. To study the relationship between IBF and the major histocompatibility complex (MHC), two types of experiments were undertaken. First, different IBF were prepared by injecting thymocytes from mice of H-2k, H-2b and H-2d haplotypes into irradiated, allogeneic recipient mice. Cells recovered in the spleens five days later were incubated for 2 h at 37 degrees C, and IBF was purified by affinity chromatography on insolubilized IgG. Purified IBF was then applied to immunosorbents prepared with anti-H-2 and anti-Ia anti sera. Acid eluates were then tested for their suppressive activity on in vitro antibody production to SRBC. Under these conditions, IBF was found to react with antisera raised against products of the whole MHC and of the I region of the MHC, but not with anti-H-2 D antisera. These data indicate that IBF bears, or is associated with Ia determinants. Second, IBF preparations from mice of H-2k, H-2b, H-2d haplotypes were tested for their capacity to suppress the in vitro antibody production to SRBC by spleen cells of a series of mouse strains. The data indicate that IBF is not genetically restricted in its function.
体内同种异体抗原激活的T细胞产生的一种免疫球蛋白结合因子(IBF)可抑制体外针对绵羊红细胞(SRBC)的抗体产生,它可能代表T细胞Fc受体的可溶性形式。为了研究IBF与主要组织相容性复合体(MHC)之间的关系,进行了两类实验。首先,通过将H-2k、H-2b和H-2d单倍型小鼠的胸腺细胞注射到经辐照的同种异体受体小鼠体内来制备不同的IBF。五天后从脾脏中回收的细胞在37℃孵育2小时,然后通过在不溶性IgG上进行亲和层析来纯化IBF。接着将纯化的IBF应用于用抗H-2和抗Ia抗体制备的免疫吸附剂。然后检测酸性洗脱液对体外针对SRBC的抗体产生的抑制活性。在这些条件下,发现IBF与针对整个MHC产物和MHC I区产物产生的抗血清发生反应,但不与抗H-2 D抗血清发生反应。这些数据表明IBF带有或与Ia决定簇相关。其次,检测来自H-2k、H-2b、H-2d单倍型小鼠的IBF制剂抑制一系列小鼠品系的脾细胞体外针对SRBC的抗体产生的能力。数据表明IBF在功能上不受基因限制。