Dohm G L, Kasperek G J, Tapscott E B, Beecher G R
Biochem J. 1980 Apr 15;188(1):255-62. doi: 10.1042/bj1880255.
Several reports have shown that amino acid utilization via oxidation and gluconeogenesis is increased during exercise. The purpose of this study was to investigate whether these changes are accompanied by alterations in protein synthesis and degradation in the muscle of exercising rats. One group of rats was made in swim for 1h and then protein synthesis and protein degradation were measured in a perfused hemicorpus preparation. Protein synthesis was decreased and protein degradation was increased in exercised rats compared with sedentary control rats. Exercise also decreased amino acid incorporation by isolated polyribosomes from muscle. Measurement of several muscle proteinase activities demonstrated that exercise had no effect on alkaline proteinase or Ca2+-activated proteinase. However, the free (unbound) cathepsin D activity was elevated in muscle of exercised rats, whereas the total activity of catepsin D was unchanged. This increase in the proportion of free cathepsin D activity suggests that lysosomal enzymes may be involved in the increased protein degradation that was observed.
多项报告表明,运动期间通过氧化和糖异生作用的氨基酸利用率会提高。本研究的目的是调查这些变化是否伴随着运动大鼠肌肉中蛋白质合成和降解的改变。一组大鼠进行1小时游泳,然后在灌注半体标本中测量蛋白质合成和蛋白质降解。与久坐不动的对照大鼠相比,运动大鼠的蛋白质合成减少,蛋白质降解增加。运动还降低了从肌肉中分离出的多核糖体的氨基酸掺入量。对几种肌肉蛋白酶活性的测量表明,运动对碱性蛋白酶或Ca2+激活的蛋白酶没有影响。然而,运动大鼠肌肉中游离(未结合)组织蛋白酶D的活性升高,而组织蛋白酶D的总活性不变。游离组织蛋白酶D活性比例的这种增加表明溶酶体酶可能参与了所观察到的蛋白质降解增加过程。