Bumol T F, Reisfeld R A
Proc Natl Acad Sci U S A. 1982 Feb;79(4):1245-9. doi: 10.1073/pnas.79.4.1245.
A monoclonal antibody, 9.2.27, with a high specificity for human melanoma cell surfaces has been utilized for biosynthetic studies in M21 human melanoma cells to define a unique antigenic complex consisting of a 250-kilodalton N-linked glycoprotein and a high molecular weight proteoglycan component larger than 400 kilodaltons. The 250-kilodalton glycoprotein has endoglycosidase H-sensitive precursors and shows a lower apparent molecular weight after treatment with neuraminidase. The biosynthesis of the proteoglycan component is inhibited by exposure of M21 cells to the monovalent ionophore monensin, this component can be labeled biosynthetically with 35SO4, is sensitive to beta-elimination in dilute base, and is degraded by both chondroitinase AC and ABC lyases, suggesting that it is a chondroitin sulfate proteoglycan. These data demonstrate that the antigenic determinant recognized by monoclonal antibody 9.2.27 is located on a glycoprotein-proteoglycan complex which may have unique implications for the interaction of glycoconjugates at the human melanoma tumor cell surface.
一种对人黑色素瘤细胞表面具有高度特异性的单克隆抗体9.2.27已被用于M21人黑色素瘤细胞的生物合成研究，以确定一种独特的抗原复合物，该复合物由一种250千道尔顿的N-连接糖蛋白和一种大于400千道尔顿的高分子量蛋白聚糖成分组成。250千道尔顿的糖蛋白具有对内切糖苷酶H敏感的前体，并且在用神经氨酸酶处理后显示出较低的表观分子量。M21细胞暴露于单价离子载体莫能菌素会抑制蛋白聚糖成分的生物合成，该成分可用35SO4进行生物合成标记，对稀碱中的β-消除敏感，并被软骨素酶AC和ABC裂解酶降解，表明它是一种硫酸软骨素蛋白聚糖。这些数据表明，单克隆抗体9.2.27识别的抗原决定簇位于糖蛋白-蛋白聚糖复合物上，这可能对人黑色素瘤肿瘤细胞表面糖缀合物的相互作用具有独特的意义。
