Rubin L A, Jay G, Nelson D L
J Immunol. 1986 Dec 15;137(12):3841-4.
The released interleukin 2 receptor (IL 2R) molecule was characterized in order to clarify its biochemical structure and to determine its functional capacity. Enzymatic digestions demonstrated that the released IL 2R, like the cell surface IL 2R, is a complex glycoprotein, modified by the addition of both N- and O-linked carbohydrates and sialic acid residues. It has a peptide backbone that is approximately 10 Kd smaller than that of its membrane-associated counterpart. Affinity chromatography demonstrated that released IL 2R from either an HTLV-I-positive T cell line (HUT-102) or PHA-activated normal peripheral lymphocytes binds efficiently to purified recombinant IL 2. Furthermore, the interaction between the growth factor and the released receptor does not appear to require any accessory molecules. These observations suggest a potentially significant role for the released IL 2R in the regulation of IL 2-dependent lymphocyte functions.
为了阐明其生化结构并确定其功能能力，对释放的白细胞介素2受体（IL-2R）分子进行了表征。酶消化表明，释放的IL-2R与细胞表面IL-2R一样，是一种复杂的糖蛋白，通过添加N-连接和O-连接的碳水化合物以及唾液酸残基进行修饰。它的肽主链比其膜相关对应物的肽主链小约10 Kd。亲和层析表明，来自HTLV-I阳性T细胞系（HUT-102）或PHA激活的正常外周淋巴细胞释放的IL-2R能有效结合纯化的重组IL-2。此外，生长因子与释放的受体之间的相互作用似乎不需要任何辅助分子。这些观察结果表明，释放的IL-2R在调节IL-2依赖性淋巴细胞功能中可能具有重要作用。
