Giedlin M A, Martin W J, Callahan G N
J Natl Cancer Inst. 1983 Oct;71(4):825-34.
Antigens associated with the H-2Kk and I-Ak regions of the major histocompatibility complex have been identified with monoclonal antibodies on an in vivo grown murine alveologenic adenocarcinoma, LT-85. Immunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis demonstrated differences in the molecular structure of I-Ak region-coded antigens between LT-85 and host C3H/HeN mammary tumor virus-negative (MTV-) or autologous C3HfB/HeN splenocytes. Ia antigens derived from LT-85 tumor cells exhibited both an increased heterogeneity in the alpha-chain and a lower apparent molecular weight in the beta-chain. Tryptic peptide mapping of the I-Ak antigen alpha- and beta-chains derived from C3H/HeN MTV- mice and LT-85 tumor cells revealed a single peptide difference in the beta-chains of these antigens. Results obtained with neuraminidase-treated I-Ak beta-chains indicated that this difference was not due to sialic and content. Maintenance of LT-85 in vitro, even for short periods, resulted in the loss of these I-Ak antigens. However, this loss of I-Ak antigen expression was fully reversible with in vivo growth.
利用单克隆抗体,已在体内生长的小鼠肺泡源性腺癌LT-85上鉴定出与主要组织相容性复合体的H-2Kk和I-Ak区域相关的抗原。免疫沉淀和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析表明,LT-85与宿主C3H/HeN乳腺肿瘤病毒阴性(MTV-)或自体C3HfB/HeN脾细胞之间,I-Ak区域编码抗原的分子结构存在差异。源自LT-85肿瘤细胞的Ia抗原在α链上表现出更高的异质性,在β链上表现出更低的表观分子量。对源自C3H/HeN MTV-小鼠和LT-85肿瘤细胞的I-Ak抗原α链和β链进行胰蛋白酶肽图谱分析,发现这些抗原的β链存在一个肽段差异。用神经氨酸酶处理I-Akβ链的结果表明,这种差异不是由于唾液酸含量所致。即使在体外短期培养LT-85,也会导致这些I-Ak抗原的丢失。然而,这种I-Ak抗原表达的丢失在体内生长时是完全可逆的。