Müllberg J, Schooltink H, Stoyan T, Heinrich P C, Rose-John S
Institut für Biochemie, RWTH Aachen, Germany.
Biochem Biophys Res Commun. 1992 Dec 15;189(2):794-800. doi: 10.1016/0006-291x(92)92272-y.
An analysis of the mechanism of generation of the soluble interleukin-6 receptor (IL-6R) has been performed. The membrane-bound receptor is proteolytically cleaved to release a soluble receptor form which retained its ligand binding capacity. Furthermore, the soluble IL-6R is unique in its ability to induce a biological signal in complex with the ligand interleukin-6 (IL-6) on cells which by themselves do not bind IL-6. Shedding of the IL-6R is strongly activated by PMA and can be inhibited by the protein kinase inhibitor staurosporine. The generation of the IL-6R is not dependent on protein synthesis. The inactive PMA analogue 4-alpha-phorbol-12,13-didecanoate fails to induce shedding of the IL-6R. Transfection of a protein kinase C expression plasmid into IL-6R expressing cells leads to enhanced shedding of the receptor. These experiments clearly show that protein kinase C regulates shedding of the IL-6R.
对可溶性白细胞介素-6受体（IL-6R）的产生机制进行了分析。膜结合受体经蛋白水解切割后释放出一种可溶性受体形式，该形式保留了其配体结合能力。此外，可溶性IL-6R的独特之处在于，它能够与配体白细胞介素-6（IL-6）形成复合物，在自身不结合IL-6的细胞上诱导生物信号。IL-6R的脱落被佛波酯（PMA）强烈激活，并可被蛋白激酶抑制剂星形孢菌素抑制。IL-6R的产生不依赖于蛋白质合成。无活性的PMA类似物4-α-佛波醇-12,13-十二烷酸酯不能诱导IL-6R的脱落。将蛋白激酶C表达质粒转染到表达IL-6R的细胞中会导致受体脱落增加。这些实验清楚地表明蛋白激酶C调节IL-6R的脱落。
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