Kaur P, Saklatvala J
Strangeways Research Laboratory, Worts' Causeway, Cambridge, England.
FEBS Lett. 1988 Dec 5;241(1-2):6-10. doi: 10.1016/0014-5793(88)81019-6.
Interleukin 1 (IL1) or tumour necrosis factor (TNF) stimulated phosphorylation of a triad of 27 kDa phosphoproteins (pI 6.0, 5.7 and 5.5) in human dermal fibroblasts. The change was dependent on the dose of cytokine in the range 0.1-20 ng, was detectable between 3 and 5 min after stimulation and was maximal by 10 min. The proteins were found in the cytosol after subcellular fractionation. The 32P was removed from them by alkali, indicating the presence of phosphoserine and/or phosphothreonine. The results suggest that early changes in serine/threonine protein kinase activity may be involved in responses of fibroblasts to IL1 and TNF.
白细胞介素1（IL1）或肿瘤坏死因子（TNF）可刺激人皮肤成纤维细胞中一组27 kDa磷蛋白（等电点分别为6.0、5.7和5.5）发生磷酸化。这种变化取决于细胞因子的剂量，范围为0.1 - 20 ng，在刺激后3至5分钟可检测到，10分钟时达到最大值。亚细胞分级分离后发现这些蛋白质存在于胞质溶胶中。通过碱处理可去除它们上面的32P，表明存在磷酸丝氨酸和/或磷酸苏氨酸。结果表明，丝氨酸/苏氨酸蛋白激酶活性的早期变化可能参与成纤维细胞对IL1和TNF的反应。
