Ullrich A, Sures I, D'Egidio M, Jallal B, Powell T J, Herbst R, Dreps A, Azam M, Rubinstein M, Natoli C
Department of Molecular Biology, Max-Planck-Institut für Biochemie, Martinsried, Federal Republic of Germany.
J Biol Chem. 1994 Jul 15;269(28):18401-7.
Immunization of mice with conditioned media from human breast cancer cells yielded the monoclonal antibody SP-2, which recognized an antigen of approximately 90-95 kDa. This protein, designated 90K, was found to be present in the serum of healthy individuals and at elevated levels in the serum of subpopulations of patients with various types of cancer and AIDS. Here we report the primary structure of the SP-2 antigen and demonstrate its relationship to a family of proteins which carry a scavenger receptor cysteine-rich domain. Northern blot analysis of normal tissues, primary tumors, and tumor-derived cell lines indicates a broad expression spectrum of the 90K gene at widely varying levels. Functional characterization reveals stimulatory effects of 90K on host defense systems, such as natural killer cell and lymphokine-activated killer cell activity, and indicates that its immunostimulatory effects may be mediated through the induction of interleukin-2 and possibly other cytokines.
用人乳腺癌细胞的条件培养基免疫小鼠产生了单克隆抗体SP-2,该抗体识别一种约90-95 kDa的抗原。这种蛋白质被命名为90K,发现它存在于健康个体的血清中,并且在各类癌症和艾滋病患者亚群的血清中水平升高。在此我们报告SP-2抗原的一级结构,并证明它与一类带有富含半胱氨酸的清道夫受体结构域的蛋白质家族的关系。对正常组织、原发性肿瘤和肿瘤衍生细胞系的Northern印迹分析表明,90K基因在广泛不同的水平上具有广泛的表达谱。功能特性揭示了90K对宿主防御系统的刺激作用,如自然杀伤细胞和淋巴因子激活的杀伤细胞活性,并表明其免疫刺激作用可能通过诱导白细胞介素-2以及可能的其他细胞因子来介导。