Changes in protein degradation in chickens due to an inflammatory challenge.
Tissue-specific changes in protein catabolism were examined in chicks 16 hr following an inflammatory challenge. It was determined that tyrosine was not catabolized or converted to phenylalanine in muscle, thymus, bursa, or spleen. Therefore, rates of tyrosine release from protein were used to estimate rates of protein catabolism in these tissues. Arginine was not catabolized to urea by chick liver; consequently, arginine release from liver protein was used to measure protein catabolism in this tissue. An injection of sheep red blood cells (SRBC) or Escherichia coli did not change rates of protein catabolism in liver or bursa as compared to saline-injected controls. SRBC significantly increased protein catabolism in muscle and spleen by 29 and 15%, respectively. E. coli resulted in significant increases in muscle, spleen, and thymus of 43, 30, and 34%, respectively. These changes in protein catabolism, together with known changes in protein synthesis, suggest that an inflammatory response to SRBC and E. coli result in increased protein accretion in the bursa and liver, and net protein loss from muscle.
D000818:Animals; D001120:Arginine / Q000378:metabolism*; D002060:Bursa of Fabricius / Q000378:metabolism; D002645:Chickens; D004912:Erythrocytes / Q000276:immunology; D004926:Escherichia coli / Q000276:immunology; D007249:Inflammation / Q000276:immunology / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D008297:Male; D009132:Muscles / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D012756:Sheep; D013154:Spleen / Q000378:metabolism; D013950:Thymus Gland / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism*
D011506:Proteins; D014443:Tyrosine; D001120:Arginine