monensin and 3-methylhistidine

Urinary 3 methyl-histidine excretion was measured in high yielding dairy cows between 10 and 3 d precalving and between 3 and 9 d postcalving. Cows received a sodium monensin controlled-release capsule or a placebo 3 wk before calving. Monensin did not affect urinary 3 methyl-histidine. Average urinary 3 methyl-histidine excretion was significantly higher postcalving (4.11 mmol d(-1)) than precalving (2.48 mmol d(-1)). This increase is assumed to be predominantly due to the negative nitrogen balance in the postcalving period caused by insufficient nutrient intake to meet nutrient requirements, which necessitates catabolism of mainly myofibrillar protein.

Topics: Animals; Cattle; Delayed-Action Preparations; Energy Metabolism; Female; Ionophores; Labor, Obstetric; Lactation; Methylhistidines; Monensin; Nitrogen; Pregnancy; Proteins

Myofibrillar protein breakdown was evaluated by measuring the release of N tau-methylhistidine by isolated rat skeletal muscles or perfused rat muscles in the presence of a variety of agents known to affect Na+ flux. Total cell proteolysis was evaluated simultaneously by measuring tyrosine release by muscles after the inhibition of protein synthesis with cycloheximide. Treatment of muscles with the Na+ ionophore monensin or inhibitors of Na+-K+ ATPase (ouabain, digoxin or vanadate) decreased N tau-methylhistidine release by muscles by 21-35%. A phorbol ester (phorbol 12-myristate 13-acetate) as well as a synthetic diacylglycerol known to activate protein kinase C and a Na+/H+ antiport also decreased N tau-methylhistidine release by muscles. Removal of extracellular Na+ blocked the ability of these agents to attenuate N tau-methylhistidine release by muscles, suggesting that their effectiveness required a change in Na+ flux. In contrast with N tau-methylhistidine release by muscles, these agents, except for monensin, did not effect the release of tyrosine, suggesting that they attenuate specifically the breakdown of myofibrillar proteins. Overall these results indicate a link between Na+ and the regulation of protein breakdown in rat skeletal muscle, whereby an influx of Na+ can result in a decrease in myofibrillar proteolysis. Left unresolved is whether phospholipid hydrolysis is involved in this scheme.

Topics: Animals; Diglycerides; Digoxin; Male; Methylhistidines; Monensin; Muscle Proteins; Muscles; Myofibrils; Ouabain; Peptides; Rats; Rats, Inbred Strains; Sodium; Tetradecanoylphorbol Acetate; Vanadates