Human T-cell leukemia-associated cell surface glycoprotein GP37: studies with three monoclonal antibodies and a rabbit antiserum.
Human T-cell leukemia-associated cell surface glycoprotein GP37: studies with three monoclonal antibodies and a rabbit antiserum.
复制标题
人 T 细胞白血病相关细胞表面糖蛋白 GP37：使用三种单克隆抗体和兔抗血清进行的研究。
DOI：
10.1016/0161-5890(86)90093-3
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发表时间：
1986
影响因子：
3.6
通讯作者：
Matsuzaki,H
中科院分区：
文献类型：
--
作者：
Seon,BK;Fukukawa,T;Jackson,AL;Chervinsky,D;Tebbi,CK;Freeman,AI;Matsuzaki,H
用三种单抗(SN2、SN2a和SN2b)研究了人T细胞白血病相关细胞表面糖蛋白GP37。放射免疫分析和流式细胞仪分析表明，SN2、SN2a和SN2b单抗对T白血病细胞具有较强的特异性。正常人外周血淋巴细胞、纯化的正常T细胞、正常胸腺细胞和正常骨髓细胞均未检测到GP37。此外，在植物血凝素(PHA)和刀豆蛋白A(ConA)激活的T细胞上几乎检测不到GP37。结果表明，这些单抗具有一定的临床应用价值。竞争结合实验表明，SN2和SN2a识别的表位距离足够近，可以完全相互抑制结合，而SN2和SN2b识别的表位距离较小，只允许部分相互抑制。用胰酶、胰凝乳酶、热裂解酶、神经氨酸酶和混合糖苷酶处理T白血病细胞，研究了这些单抗所确定的抗原决定簇的生化性质。结果表明，这些单抗所定义的抗原决定簇均由糖蛋白GP37的蛋白部分组成。当T白血病细胞与SN2反应时，未观察到明显的抗原调节。在序贯免疫沉淀实验中，首先用兔抗T白血病抗血清处理125I标记的白血病抗原制剂。后者是用部分纯化的人T白血病抗原免疫兔制备的，对T白血病细胞具有良好的特异性。随后用SN2处理标记的抗原制剂，表明SN2抗原已被预先清除。因此，小鼠单抗SN2和兔抗T白血病抗血清都与同一个GP37分子反应。
Three monoclonal antibodies (mAbs), termed SN2, SN2a and SN2b, were used in the present work to study a human T-cell leukemia-associated cell surface glycoprotein, GP37. Strong specificity of mAbs SN2, SN2a and SN2b for T leukemia cells was demonstrated by radioimmunoassay and fluorescence-activated cell sorter (FACS) analysis. GP37 was not detected on normal human peripheral blood lymphocytes, purified normal T-cells, normal thymocytes nor normal bone marrow cells. Furthermore, GP37 was barely detectable on phytohemagglutinin (PHA)- and Concanavalin A (Con A)-activated T-cells. The results indicate clinical utility of these mAbs. Competitive binding experiments show that the epitopes recognized by SN2 and SN2a are sufficiently close to each other to allow complete reciprocal inhibition of binding whereas the epitopes recognized by SN2 and SN2b are less close to allow only partial reciprocal binding inhibition. The biochemical nature of antigenic determinants defined by these mAbs was studied by treating T leukemia cells with trypsin, chymotrypsin, thermolysin, neuraminidase and mixed glycosidases. The results suggest that the antigenic determinants defined by these mAbs all consist of the protein moiety of the glycoprotein GP37. No significant antigenic modulation was observed when T leukemia cells were reacted with SN2. In a sequential immunoprecipitation experiment, a125I-labeled leukemia antigen preparation was first treated with a rabbit anti-T leukemia antiserum. The latter had been prepared by immunizing a rabbit with a partially purified human T leukemia antigen preparation and showed a good specificity for T leukemia cells. Subsequent treatment of the labeled antigen preparation with SN2 showed that SN2 antigen had been precleared. Thus, both mouse mAb SN2 and the rabbit anti-T leukemia antiserum react with the same GP37 molecule.