Characterization of in vitro immunoselected variants from a highly metastatic murine tumor for alterations in malignant behavior in vivo.
Characterization of in vitro immunoselected variants from a highly metastatic murine tumor for alterations in malignant behavior in vivo.
复制标题
来自高度转移性小鼠肿瘤的体外免疫选择变体的表征，用于改变体内恶性行为。
DOI：
10.1002/ijc.2910330518
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发表时间：
1984
影响因子：
6.4
通讯作者：
Kerbel,RS
中科院分区：
文献类型：
--
作者：
Liteplo,RG;Frost,P;Donaghue,TP;Kerbel,RS
在体外免疫选择技术中，通过单克隆抗Ly-6.2抗体获得了高转移性DBA/2小鼠（Ly-6.2+）MDAY-D2肿瘤的一种新的Ly-6.2−抗原缺失变体（称为L 61-MI）。尽管L 61-MI在皮下接种到同基因宿主中时生长较差，但当接种到免疫抑制的无胸腺裸鼠中时，其生长和转移方式与亲本MDAY-D2肿瘤相似。L 61-MI以及同一MDAY-D2肿瘤的另一种Ly-6.2-变体（称为L 61）在同基因宿主中转移性较差，将外源性岩藻糖回收为糖蛋白和糖脂的速率是亲本MDAY-D2系的5.5和7.8倍。相比之下，Ly-6.2-变体在将外源甘露糖掺入糖蛋白和糖脂中时表现出50-70%的减少。L 61-MI和L 61还表现出与细胞表面糖蛋白和/或糖脂连接的寡糖部分结构的改变。因此，体外免疫选择技术可用于获得一组在其生长和转移能力中具有稳定表型改变的变体。这样的突变体，像以前描述的凝集素抗性突变体，是有用的研究细胞表面糖蛋白和糖脂的肿瘤发生和转移的贡献。
A new Ly‐6.2−antigen‐loss variant (called L61‐MI) of the highly metastatic DBA/2 mouse (Ly‐6.2+) MDAY‐D2 tumor has been obtained by means of a monoclonal anti‐Ly‐6.2 antibody in anin vitroimmunoselection technique. Whereas L61‐MI grew poorly when inoculated subcutaneously into the syngeneic host, it grew and metastasized in a similar way to the parental MDAY‐D2 tumor when inoculated into immunosuppressed, athymic nude mice. L61‐MI as well as another Ly‐6.2−variant of the same MDAY‐D2 tumor (called L61) which is poorly metastatic in the syngeneic host salvaged exogenous fucose into glycoproteins and glycolipids at rates 5.5 and 7.8 times that of the parental MDAY‐D2 line. In contrast, the Ly‐6.2−variants exhibited a 50–70% decrease in the incorporation of exogenous mannose into glycoproteins and glycolipids. L61‐MI and L61 also exhibited alterations in the structures of the oligosaccharide moieties linked to the cell surface glycoproteins and/or glycolipids. Thus, thein vitroimmunoselection technique can be used to obtain a panel of variants with stable phenotypic alterations in their growth and metastatic capacities. Such mutants may, like previously described lectin‐resistant mutants, be useful in studying the contribution of cell surface glycoproteins and glycolipids to tumorigenicity and metastasis.