Kaur P, Welch W J, Saklatvala J
Cytokine Biochemistry Group, Strangeways Research Laboratory, Cambridge, England.
FEBS Lett. 1989 Dec 4;258(2):269-73. doi: 10.1016/0014-5793(89)81671-0.
Interleukin 1 alpha and tumour necrosis factor-alpha stimulated phosphorylation of three 27 kDa phosphoproteins in MRC-5 fibroblasts which was sustained for up to 2 h after adding the cytokines. All three phosphoproteins were immunoprecipitated by a specific antiserum to the small mammalian heat shock protein, hsp 27. The three phosphoproteins from stimulated or control cells contained phosphoserine but not phosphothreonine or phosphotyrosine. Similar increases in phosphorylation of immunoprecipitable 27 kDa proteins were seen in U937 cells stimulated by TNF alpha and Hep G2 cells stimulated by IL1 alpha.
白细胞介素1α和肿瘤坏死因子-α刺激MRC-5成纤维细胞中三种27 kDa磷蛋白的磷酸化，在添加细胞因子后这种磷酸化可持续长达2小时。所有这三种磷蛋白都被针对小哺乳动物热休克蛋白hsp 27的特异性抗血清免疫沉淀。来自受刺激细胞或对照细胞的这三种磷蛋白含有磷酸丝氨酸，但不含磷酸苏氨酸或磷酸酪氨酸。在TNFα刺激的U937细胞和IL1α刺激的Hep G2细胞中，可免疫沉淀的27 kDa蛋白的磷酸化也出现了类似的增加。
