Activation of MAP kinase in Swiss 3T3 fibroblasts by insulin-like growth factor-I.

Activation of MAP kinase in Swiss 3T3 fibroblasts by insulin-like growth factor-I.
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胰岛素样生长因子-I 激活 Swiss 3T3 成纤维细胞中的 MAP 激酶。

DOI:
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发表时间:
1995
期刊:
Growth regulation
影响因子:
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通讯作者:
M. Thorén
M. Thorén
中科院分区:
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文献类型:
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作者:
A. Hansson;M. Thorén

文献摘要

被引文献

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向 Swiss 3T3 成纤维细胞添加 10 nM 胰岛素样生长因子-I (IGF-I) 后 2-5 分钟观察到胞浆髓磷脂碱性蛋白激酶活性达到峰值。通过色谱、免疫检测和原位激酶测定对诱导的激酶活性进行的分析表明,这代表 p42 丝裂原激活蛋白激酶的活性增加了 1.8 至 3.5 倍。添加 10 nM 胰岛素也导致这些方面的激酶活性增加,但仅达到 IGF-I 诱导的激酶活性的约 60%。发现胰岛素和IGF-I对于诱导[14C-(U)]-D-葡萄糖的脂质和糖原合成的作用之间存在类似的定量关系。然而,两种试剂对 3H-L-亮氨酸掺入蛋白质的刺激程度相同。通过四唑染料还原测量,10 nM 胰岛素对增殖的影响仅为 10 nM IGF-I 诱导的增殖影响的 18%。获得的数据表明,细胞质丝裂原激活的蛋白激酶激活可能构成胰岛素超家族肽诱导的葡萄糖代谢,特别是糖原合成的信号传导途径。
A peak of cytosolic myelin basic protein kinase activity was observed at 2-5 min after addition of 10 nM insulin-like growth factor-I (IGF-I) to Swiss 3T3 fibroblasts. Analysis of the induced kinase activity by chromatography, immunodetection and in situ kinase assay suggests that this represents a 1.8- to 3.5-fold increase in the activity of p42 mitogen-activated protein kinase. Addition of insulin at 10 nM also resulted in an increased kinase activity in these respects, however, only to approximately 60% of that induced by IGF-I. A similar quantitative relation between the effects of insulin and IGF-I was found for induction of lipid and glycogen synthesis from [14C- (U)]-D-glucose. However, incorporation of 3H-L-leucine into protein was stimulated to the same extent by the two agents. The effect of 10 nM insulin on proliferation, measured as tetrazolium dye reduction, was only 18% of that induced by 10 nM IGF-I. The obtained data suggest that cytosolic mitogen-activated protein kinase activation may constitute a signalling pathway for glucose metabolism, and especially glycogen synthesis, induced by peptides of the insulin superfamily.