HEAT SHOCK PROTEIN & IMMUNOPHILIN IN SQUIRREL MONKEY & HUMAN B LYMPHOBLAST

我们已经分析了热休克蛋白（hsp）和免疫亲素， 松鼠猴和人细胞的胞质溶胶（Abs 2）。 这些是 与糖皮质激素形成异源复合物的蛋白质 并将其调整为高亲和力状态。 20个？克 人和松鼠猴B淋巴母细胞的胞浆蛋白质， 在8%变性凝胶上沉淀，并转移至 硝化纤维素 Western blot检测目的蛋白 分析并通过ECL化学发光系统可视化。 免疫反应带的光密度扫描显示， hsp 90、hsp 70、p60、p48和p23在两组间的表达水平相似 物种 然而，亲免蛋白家族的蛋白质表现出相当的 它们的丰度和明显的物种特异性差异 分子量的 FKBP 52（hsp 56）是一种59 kDa的FK 506结合蛋白， 3-在松鼠猴胞质溶胶中低1倍，而亲环素40 （Cyp 40），一个40 kDa的环孢菌素结合蛋白，是1.7倍低。 对 另一方面，FKBP 51（人54 kDa，松鼠猴52 kDa） 在松鼠猴胞质中的浓度是人胞质的7.5倍。 因此，松鼠猴细胞中的亲免蛋白是 以不同于人类细胞的化学计量比表达。 作为 这些亲免蛋白是HSP 90结合蛋白， 竞争hsp 90上的相同位点，它们在 松鼠猴细胞可改变糖皮质激素受体-异源复合物 组装件. 未来的研究将集中在这些作用 免疫亲素在糖皮质激素敏感性降低， 灵长类动物

We have analyzed heat shock proteins (hsp) and immunophilins in the cytosol of squirrel monkey and human cells (Abs 2). These are proteins which are thought to form a heterocomplex with glucocorticoid receptors and tailor them into a high-affinity state. Twenty ?g of cytosolic protein from human and squirrel monkey B-lymphoblasts were electrophoresed on 8% denaturing gels and transferred to nitrocellulose. Proteins of interest were detected by Western blot analysis and visualized by the ECL chemiluminescence system. Densitometric scanning of the immunoreactive bands showed that the levels of hsp90, hsp70, p60, p48, and p23 were similar between the two species. However, proteins of the immunophilin family showed quite dramatic species-specific differences in their abundance and apparent molecular weight. FKBP52 (hsp56), a 59 kDa FK506 binding protein, was 3-fold lower in squirrel monkey cytosol, whereas cyclophilin 40 (Cyp40), a 40 kDa cyclosporin-binding protein, was 1.7-fold lower. On the other hand, FKBP51 (54 kDa in human, 52 kDa in squirrel monkey) was 7.5-fold higher in squirrel monkey cytosol than in human cytosol. Therefore, immunophilin proteins in squirrel monkey cells are expressed at different stoichiometric ratios than in human cells. As these immunophilins are hsp90-binding proteins and are thought to compete for the same sites on hsp90, their differential expression in squirrel monkey cells may alter glucocorticoid receptor-heterocomplex assembly. Future studies will focus on the role of these immunophilins in the decreased glucocorticoid sensitivity of this primate.