Effects of zeranol on protein turnover in L6 myotubes     

R A Roeder  J M Gunn 《Domestic animal endocrinology》1987,4(1):61-67

Protein synthesis and degradation were measured in cultures of L6 myotubes to determine the direct anabolic activity of zeranol on muscle. Zeranol, dexamethasone, insulin and zeranol-dexamethasone combination, at various concentrations from 10(-8) to 10(-6) M, were added to cultures at either 18 hr prior to or at the beginning of a 6 hr synthesis or degradation measuring period. Protein synthesis was measured by determining the incorporation of radioactivity into trichloraoacetic acid precipitable cell protein following incubation with [3H] leucine. Protein synthesis was expressed as cpm incorporated in 6 hr per mg protein. Protein degradation was measured by a pulse-chase procedure using [3H] leucine. Protein degradation was expressed as the percent labeled protein degraded in 6 hr. Results from the study indicate that zeranol did not stimulate protein synthesis or inhibit proteolysis (P greater than .01). Stimulation of proteolysis observed with 10(-8) M dexamethasone was 13% and 18% (P less than .01) at the 6 hr and 24 hr incubation period, respectively. Dexamethasone-stimulated protein degradation was not altered appreciably by zeranol. In contrast, 10(-6) M insulin significantly (P less than .01) stimulated protein synthesis (16%) and inhibited protein degradation (15%). These results suggest that the anabolic action of zeranol does not occur by directly regulating muscle protein synthesis or degradation, or by altering the glucocorticoid-induced catabolic response in muscle.  相似文献