Tsuruoka N, Funakoshi K, Kodama S, Tsujimoto M
Suntory Institute for Biomedical Research, Mishima, Osaka, Japan.
Cell Immunol. 1990 Feb;125(2):354-62. doi: 10.1016/0008-8749(90)90090-e.
Interaction of interleukin (IL)-5 with its receptors on murine leukemic cell line, BCL1 cells was examined. 125I-labeled recombinant murine IL-5(rmIL-5) bound specifically to high-affinity receptors on BCL1 cells. rmIL-5, which was about 2500-fold more active than recombinant human IL-5(rhIL-5) in IgM-inducing activity on BCL1 cells, also showed about 5000-fold higher affinity to receptors. These results suggest that the bioactivity of IL-5 correlates with its receptor-binding activity. When disulfide bond formation was blocked, rmIL-5 dissociated into a monomer and lost its biological activity. This monomeric form of rmIL-5 also lost its ability to bind to cells, suggesting that dimer formation is essential for the biological activity of IL-5.
研究了白细胞介素(IL)-5与其在小鼠白血病细胞系BCL1细胞上的受体之间的相互作用。125I标记的重组小鼠IL-5(rmIL-5)特异性结合于BCL1细胞上的高亲和力受体。在诱导BCL1细胞产生IgM的活性方面,rmIL-5比重组人IL-5(rhIL-5)活性高约2500倍,其与受体的亲和力也高约5000倍。这些结果表明IL-5的生物活性与其受体结合活性相关。当二硫键形成被阻断时,rmIL-5解离为单体并失去其生物学活性。rmIL-5的这种单体形式也失去了与细胞结合的能力,这表明二聚体的形成对于IL-5的生物学活性至关重要。