负责分离的大鼠脂肪细胞中激素敏感脂肪酶去磷酸化的蛋白质磷酸酶。
The protein phosphatases responsible for dephosphorylation of hormone-sensitive lipase in isolated rat adipocytes.
作者信息
Wood S L, Emmison N, Borthwick A C, Yeaman S J
机构信息
Department of Biochemistry and Genetics, Medical School, University of Newcastle upon Tyne U.K.
出版信息
Biochem J. 1993 Oct 15;295 ( Pt 2)(Pt 2):531-5. doi: 10.1042/bj2950531.
Abstract
The levels of the cytosolic serine/threonine protein phosphatases (PP) in rat adipocyte extracts have been determined, by using both reference substrates and hormone-sensitive lipase (HSL) as substrates. Adipocytes contain significant levels of both PP1 and 2A (1.6 and 2.0 m-units/ml of packed cells respectively), with lower levels of PP2C and virtually no PP2B activity. PP2A and 2C exhibit similar degrees of activity against HSL phosphorylated at site 1, together accounting for 92% of the total. In contrast, site 2 is dephosphorylated predominantly by PP2A (over 50% of total activity), whereas PP1 and PP2C contribute approx. 20% and 30% respectively to the total phosphatase activity against that site. Total phosphatase activity in the adipocyte extracts was 2-3-fold higher against site 2 than against site 1. The possible significance of these findings to the regulation of HSL activity in adipose tissue in vivo is discussed.
摘要
利用参考底物和激素敏感脂肪酶（HSL）作为底物，测定了大鼠脂肪细胞提取物中胞质丝氨酸/苏氨酸蛋白磷酸酶（PP）的水平。脂肪细胞中PP1和PP2A的含量都很高（分别为每毫升压实细胞1.6和2.0 m单位），PP2C含量较低，几乎没有PP2B活性。PP2A和PP2C对位点1磷酸化的HSL表现出相似程度的活性，二者共占总活性的92%。相比之下，位点2的去磷酸化主要由PP2A完成（超过总活性的50%），而PP1和PP2C分别约占针对该位点的总磷酸酶活性的20%和30%。脂肪细胞提取物中针对位点2的总磷酸酶活性比对位点1的活性高2至3倍。本文讨论了这些发现对体内脂肪组织中HSL活性调节的可能意义。
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