Roesler W J, Nijjar M S, Khandelwal R L
Department of Biochemistry, University of Saskatchewan Saskatoon, Canada.
Mol Cell Biochem. 1989 Jun 1;87(2):147-52. doi: 10.1007/BF00219257.
We have recently demonstrated that the activity of liver glycogen phosphorylase, the rate-limiting enzyme of glycogenolysis, is elevated in genetically diabetic (db/db) mouse and that it is primarily due to the presence of increased amounts of this enzyme. In the present study, we examined the turnover of glycogen phosphorylase in vivo in order to elucidate the mechanism for this specific increase. The rate of phosphorylase synthesis was slightly decreased in the diabetic mouse compared to controls. However, the relative rates of synthesis were similar in these two groups. The rate of degradation of this enzyme was decreased 20% (p less than 0.05) in the diabetic mouse compared to controls. More importantly, the relative rate of degradation of phosphorylase was found to be lower in the diabetic animals. This indicates that the elevated concentration of phosphorylase in the liver of the db/db mouse is likely due to a specific decrease in its rate of degradation.
我们最近证实,糖原分解的限速酶——肝糖原磷酸化酶的活性在遗传性糖尿病(db/db)小鼠中升高,且这主要是由于该酶的量增加所致。在本研究中,我们检测了糖原磷酸化酶在体内的周转情况,以阐明这种特异性增加的机制。与对照组相比,糖尿病小鼠中磷酸化酶的合成速率略有下降。然而,这两组的相对合成速率相似。与对照组相比,糖尿病小鼠中该酶的降解速率降低了20%(p<0.05)。更重要的是,发现糖尿病动物中磷酸化酶的相对降解速率较低。这表明db/db小鼠肝脏中磷酸化酶浓度的升高可能是由于其降解速率的特异性降低。