Clifford G M, McCormick D K, Londos C, Vernon R G, Yeaman S J
Department of Biochemistry and Genetics, The Medical School, University of Newcastle, Newcastle upon Tyne, UK.
FEBS Lett. 1998 Sep 11;435(1):125-9. doi: 10.1016/s0014-5793(98)01052-7.
By incubating 32P-labelled adipocytes, and extracts from these cells, in the presence or absence of specific inhibitors, we evaluated the contribution of protein phosphatases PP1, PP2A and PP2C, to the dephosphorylation of perilipin, an acutely hormone-regulated adipocyte phosphoprotein. Under conditions to completely inhibit PP2A activity, perilipin phosphatase activity in extracts remain unaffected, but PP1 inhibition results in abolition of perilipin phosphatase activity. Inhibition of PP1 (and 2A) in intact adipocytes stimulated lipolysis and increased phosphorylation of perilipin. No involvement of PP2C was found. Hence, PP1 constitutes the predominant if not sole perilipin phosphatase in adipocytes.
通过在存在或不存在特异性抑制剂的情况下培养32P标记的脂肪细胞及其提取物，我们评估了蛋白磷酸酶PP1、PP2A和PP2C对 perilipin（一种急性激素调节的脂肪细胞磷蛋白）去磷酸化的作用。在完全抑制PP2A活性的条件下，提取物中的perilipin磷酸酶活性不受影响，但抑制PP1会导致perilipin磷酸酶活性丧失。在完整脂肪细胞中抑制PP1（和2A）会刺激脂肪分解并增加perilipin的磷酸化。未发现PP2C参与其中。因此，PP1即使不是脂肪细胞中唯一的perilipin磷酸酶，也是主要的perilipin磷酸酶。
