Muscle protein turnover and tenderness in broiler chickens fed cimaterol.
To investigate the impact of cimaterol (CIM) on muscle protein turnover, carcass and muscle composition, muscle cathepsin B + L activity and meat tenderness, 21-d-old broiler chickens (n = 88) were assigned to dietary treatments of either 0 or 1 ppm CIM. Fractional synthesis rates (FSR), fractional accretion rates (FAR), proximate composition and collagen content were determined in the breast muscle (BM); pectoralis major) and a group of leg muscles (LM; gastrocnemius and peroneous longus) from groups of six birds per treatment within each of two time periods (age = 38 or 56 d). Whole body composition, serum hydroxyproline content and BM cathepsin B + L activity also were measured. Fractional degradation rates (FDR) were calculated as the difference between FSR and FAR. Feeding CIM increased (P less than .01) whole body protein content. Weights of LM and percentage of body weight as BM and LM were increased (P less than .05) when CIM was included in the diet. Although FSR was not significantly reduced by CIM feeding it decreased (P less than .05) with increasing age. Due to decreases in FAR, FDR thereby was reduced by CIM 31.5% and 11.9% in BM and 38.2% and 37.4% in LM at 38 d and 56 d of age, respectively. Cathepsin B + L activities also were reduced 33.6% (P less than .01) and shear forces were increased by 41% (P less than .05) by CIM feeding. For chickens fed CIM, the correlation between cathepsin B + L activity and shear force was -.63 (P less than .01). Feeding CIM improved carcass leanness and muscling due to reductions in FDR and proteolytic enzyme activity. Feeding CIM also reduced meat tenderness.
Morgan
J B
JB
University of Nebraska, Lincoln 68583-0908.
Jones
S J
SJ
Calkins
C R
CR
D000284:Administration, Oral; D000318:Adrenergic beta-Agonists / Q000008:administration & dosage / Q000494:pharmacology*; D000818:Animals; D001835:Body Weight; D002401:Cathepsin B / Q000032:analysis; D056668:Cathepsin L; D002403:Cathepsins; D002645:Chickens / Q000378:metabolism*; D003094:Collagen / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000032:analysis; D004247:DNA / Q000032:analysis; D010450:Endopeptidases; D004983:Ethanolamines / Q000494:pharmacology*; D006909:Hydroxyproline / Q000097:blood; D009124:Muscle Proteins / Q000378:metabolism; D009132:Muscles / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism; D012313:RNA / Q000032:analysis
D000318:Adrenergic beta-Agonists; D004983:Ethanolamines; D009124:Muscle Proteins; D012313:RNA; D003094:Collagen; D004247:DNA; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; D056668:Cathepsin L; D006909:Hydroxyproline; C047411:cimaterol