Preliminary characterization of a heat-stable protein from rat adipose tissue whose phosphorylation is stimulated by insulin.
Preliminary characterization of a heat-stable protein from rat adipose tissue whose phosphorylation is stimulated by insulin.
复制标题
来自大鼠脂肪组织的热稳定蛋白的初步表征，其磷酸化受到胰岛素的刺激。
DOI：
10.1042/bj2040817
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发表时间：
1982
期刊：
影响因子：
--
通讯作者：
Avruch,J
中科院分区：
文献类型：
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作者：
Blackshear,PJ;Nemenoff,RA;Avruch,J
将32p标记的离体大鼠脂肪细胞或附睾脂肪垫暴露于胰岛素中，导致热稳定酸溶性蛋白mr22000的磷酸化增加。在完整细胞中，该蛋白的磷酸化不受异丙肾上腺素（异丙肾上腺素）的影响，体外暴露于环amp依赖性蛋白激酶或平滑肌肌球蛋白轻链激酶也不会催化其磷酸化。mr - 22000蛋白的特性包括：热稳定性；在1%三氯乙酸中的溶解度；π4.9;凝胶过滤以表观Mr 37 500洗脱；它同时含有磷丝氨酸和磷苏氨酸。它可以通过几个标准与脂肪组织的热稳定磷酸酶抑制剂1（抑制剂1A）和脂肪组织肌球蛋白轻链的磷酸化形式区分开来。它的身份，以及胰岛素刺激磷酸化可能的功能意义，仍然是未来研究的问题。
Exposure of 32P-labelled isolated rat adipocytes or epididymal fat-pads to insulin resulted in an increase in the phosphorylation of a heat-stable acid-soluble protein of Mr 22 000. The phosphorylation of this protein was unaffected by isoprenaline (isoproterenol) in intact cells, nor was its phosphorylation catalysed by exposure in vitro to the cyclic AMP-dependent protein kinase or smooth-muscle myosin light-chain kinase. The properties of the Mr-22 000 protein include: heat-stability; solubility in 1% trichloroacetic acid; pI 4.9; elution at apparent Mr 37 500 on gel filtration; and it contains both phosphoserine and phosphothreonine. It can be distinguished from the heat-stable phosphatase inhibitor 1 of adipose tissue (inhibitor 1A) and the phosphorylated form of adipose-tissue myosin light chain by several criteria. Its identity, and the possible functional significance of the insulin-stimulated phosphorylation, remain problems for future study.