Effects of cimaterol on muscle protein metabolism and its actions in hypothyroid and hyperthyroid rats.

Objectives were to examine mechanisms underlying anabolic actions of cimaterol in skeletal muscle and to evaluate cimaterol's actions in hypothyroid and hyperthyroid rats. In the first study growing rats were fed either a control diet or a diet containing cimaterol for 10 days. In a second study sham-thyroidectomized and thyroidectomized (Tx) rats were assigned to one of 5 treatments: control (sham-Tx), Tx, Tx supplemented with cimaterol, Tx injected with triiodothyronine (T3), and Tx rats injected with T3 and supplemented with cimaterol. Effects of treatments on growth, muscle weights and urinary NT-methylhistidine (NMH) excretion were evaluated in both trials. Muscle was also collected for determinations of DNA, RNA, protein and activities of several proteolytic enzymes. Cimaterol caused muscle hypertrophy and increased urinary NMH excretion. Hence, anabolic actions of cimaterol may result from an increase in myofibrillar protein synthesis which exceeds changes in myofibrillar protein degradation. Urinary NMH excretion was reduced by thyroidectomy and increased in hyperthyroid rats and both hypothyroidism and hyperthyroidism were characterized by myopathy. Cimaterol increased muscle weights in hypothyroid but not in hyperthyroid rats. Therefore, cimaterol's anabolic properties are thyroid hormone-independent and antagonized by excess thyroid hormone. Anabolic actions of cimaterol in hypothyroid rat muscle were attributed to an action on protein synthesis because urinary NMH excretion was not affected by cimaterol but muscle RNA concentration was increased. Activities of cathepsins B, D and L and neutral proteinase were dose-related to thyroid status, however, were unrelated to cimaterol-dependent perturbations in NMH excretion. Control of muscle protein balance by thyroid hormones may involve regulation of these enzymes; however, control of muscle protein degradation by cimaterol is likely directed towards other proteolytic mechanisms or to mechanisms which alter susceptibility of myofibrillar proteins to degradation.     

Reduced calcium-dependent proteinase activity in cimaterol-induced muscle hypertrophy in lambs

The purpose of this study was to reveal the possible relationships between total Ca2+-dependent proteinase (CDP) and micromolar-Ca2+-dependent proteinase (microM CDP) activity and cimaterol-induced hypertrophy of skeletal muscle. Dietary administration of 10 ppm cimaterol to finishing lambs reduced microM CDP activity in longissimus muscle (LD) by 55% (P less than .01) and 70% (P less than .02) after 3 and 6 wk of treatment, respectively. Total CDP activity was unaffected by cimaterol at both treatment intervals. The reduced microM CDP activity was not associated with a reduced yield of enzyme extract from the muscle. Cimaterol treatment increased the cross-sectional area of the LD by 23.5% at 3 wk and by 35.6% at 6 wk (P less than .001). Cimaterol also increased (P less than .001) the masses of semitendinosus, semimembranosus and biceps femoris by 26%, 32.4% and 24.5%, respectively. These results suggest that cimaterol-induced muscle hypertrophy may be attained in part by reduction of myofibrillar protein degradation.     

Responses to cimaterol in genetically obese and lean pigs

Twenty-four genetically obese and 24 lean barrows were allotted within genotype to either a 16% CP corn-soybean meal basal diet, the basal + .69 ppm cimaterol or the basal + 1.38 ppm cimaterol. Pigs had ad libitum access to their diets from 59.3 kg to 104.5 kg body weight. No genotype x cimaterol interactions were detected (P greater than .05). Neither genotype nor cimaterol supplementation had any effect (P greater than .05) on average daily weight gain or gain-to-feed ratio. Compared with lean pigs, obese pigs had higher fasting plasma urea nitrogen (BUN), a smaller gastrointestinal tract and a greater dressing percentage with a shorter and fatter carcass (P less than .05). Cimaterol produced a higher fasting plasma BUN, a greater dressing percentage with a leaner carcass and a higher shear force value for loin chops (P less than .05). Cimaterol also tended (P less than .10) to increase heart weight. However, no difference was observed in these measurements between pigs fed .69 or 1.38 ppm cimaterol. In lean pigs fed the basal or .69 ppm cimaterol diet, there was no difference (P greater than .05) in the 8 to 24 h postprandial whole-animal heat production. Cimaterol effectively decreased fat deposition and increased lean accretion both in genetically obese and in lean pigs; there were no differential responses to cimaterol in pigs with different propensities to deposit body fat.     

Protein metabolism in chicken muscle cell cultures treated with cimaterol

Primary muscle cell cultures were prepared from the leg muscle of 12-d broiler chicken embryos. The partitioning agent cimaterol (10(-6) to 10(-10) M) was added on d 1 and each day thereafter, and cells were studied after 7 d in culture. Cimaterol had no effect at any level either on the percentage of nuclei within multinucleated myotubes or on the total number of nuclei within myotubes. At 10(-7) M cimaterol, the quantity of the myofibrillar protein fraction was increased by 25.1 +/- 8.0% (P less than .05) and the quantity of myosin heavy chain was increased by 30.9 +/- 4.5% (P less than .05). To understand the basis for the increase in myofibrillar protein, the incorporation rate of [3H]Leu was measured in pulse labeling experiments. The apparent synthesis rate of the soluble protein fraction and the crude myofibrillar fraction was not significantly increased by cimaterol; however, cimaterol levels greater than 10(-8) M caused a 10 to 12% increase (P less than .05) in the incorporation rate of [3H]Leu into myosin heavy chain. The effect of cimaterol on release of [3H]Leu from prelabeled protein also was assessed in pulse-chase experiments; the apparent rate of protein degradation was inhibited by 10 to 15% (P less than .05) at the higher levels of cimaterol. Dot blot analysis indicated that the quantity of myosin heavy chain mRNA was elevated in cimaterol-treated cultures. Thus, the increased quantity of myofibrillar proteins in embryonic broiler muscle cell cultures is the combined result of a stimulation in the rate of protein synthesis and an inhibition in the rate of protein degradation.     

Effects of age and castration on activities of calpains and calpastatin in sheep skeletal muscle.

The objectives of this experiment were to assess effects of animal age and castration on activities of calpain I, calpain II, and calpastatin in sheep skeletal muscle. Ten newborn male lambs (2.9 kg), six weaned wethers (23.2 kg), six weaned rams (22.2 kg), six market wethers (55.4 kg), and six market rams (60.2 kg) were slaughtered and samples of biceps femoris were taken for assay of calpain I (micromolar calcium-dependent proteinase), calpain II (millimolar calcium-dependent proteinase), and calpastatin. Preweaning weight gain was similar for rams and wethers; however, postweaning ram growth exceeded (P less than .05) that of wethers. Ram biceps femoris weights at market were greater than those of wethers (P less than .05). Irrespective of age or gender, activity of calpain II was two- to threefold greater than that of calpain I. Muscle calpastatin activity was severa fold higher than calpain I and II activities. Activities of calpains and calpastatin declined (P less than .05) between birth and weaning. A portion of these losses were due to a dilution effect caused by accumulation of muscle proteins. Neonatal attenuation of calpain activities may underlie age-related attenuation of fractional rates of muscle protein degradation. Although ram muscle growth exceeded that of wethers, no differences (P greater than .05) in activities of muscle calpains or calpastatin were detected between these two groups at weaning or at market weight. Hence, castration did not influence lamb muscle growth by altering muscle calpain or calpastatin activities.     

Cimaterol reduces beta-adrenergic receptor density in rat skeletal muscles.

Interactions between the beta-adrenoceptor agonist cimaterol and beta-adrenoceptors on rat skeletal muscle membranes were examined in two studies. In Exp. 1, muscle samples from eight Sprague-Dawley rats (female, approximately 200 g) were used for competition binding and autoradiographic studies using [125I]cyanopindolol (ICYP) as a radioligand. The affinities or dissociation constants for binding (KD values) for cimaterol in plantaris and soleus muscles were .68 and .92 microM, respectively. Muscle areas stained for succinic dehydrogenase had propranolol-resistant ICYP binding sites; cimaterol did not seem to compete for these sites. In Exp. 2, 60 Sprague-Dawley rats (female, approximately 218 g) were fed 0 or 10 ppm of cimaterol in rat diet that was ground. Groups were killed after 1, 3, 7, 14, or 28 d of treatment. Cimaterol increased BW gain up to 14 d after commencement of treatment, with little or no improvement thereafter. Enhanced weight gain in skeletal muscles also occurred up to 14 d of cimaterol treatment. Densities of beta-adrenoceptors in plantaris and soleus muscle membrane homogenates were estimated using a radioligand binding assay with ICYP. A significant reduction in the number of binding sites (Bmax) was observed after 3 d of cimaterol treatment in plantaris muscle without a change in the KD of ICYP binding. The percentage reductions in Bmax were 26.8, 42.2, 37.7, and 37.8% at 3, 7, 14, and 28 d after cimaterol administration, respectively. In the soleus muscle, significant reductions (44.1 and 29.8%) in Bmax were observed after 3 and 14 d of cimaterol treatment.(ABSTRACT TRUNCATED AT 250 WORDS)     

Effects of cimaterol on energetics and carcass characteristics of Suffolk ewe lambs.

The effects of cimaterol, a beta agonist, on basal metabolic rate, heat increment, maintenance requirements and carcass characteristics were determined using six treated and six control Suffolk ewe lambs. The lambs were fed a pelleted diet (18.7% CP, 2.64 Mcal ME/kg) with or without .5 mg cimaterol/kg BW.75 daily for 70 d. Heat production was monitored for 2 d on each animal at three levels of intake by respiration calorimetry. A 7-d total collection digestion trial was conducted on each animal at both high and low levels of intake. Cimaterol-fed lambs gained more (P less than .05) weight (174 vs 107 g/d) and had a higher (P less than .01) gain/feed ratio (151 vs 90 g/kg) than controls. Cimaterol did not affect diet digestibility or methane production. It reduced (P less than .01) urinary N excretion by 12% and improved (P less than .001) N retention by 18%. Cimaterol also increased carcass weight (26.9 vs 22.1 kg), dressing percentage (57.2 vs 53.9), longissimus muscle area (22.5 vs 15.0 cm2) and leg score (14.3 vs 12.2). Heat production was, on the average, elevated 7 to 10% on d 1 to 4 of cimaterol feeding but reverted to control levels by d 10. Cimaterol did not have any long-term thermogenic effects, either expressed as partial efficiency of ME use for growth (.48 vs .49), as maintenance ME requirements (76 vs 75 kcal/kg BW.75) or as fasting heat production (84 vs 80 kcal/kg BW.75) for treated vs control lambs, respectively. Results indicate little long-term thermogenic effect of cimaterol, even though growth rate and protein deposition were increased.     

Effect of dietary cimaterol on Na(+)-K+ ATPase activity in rabbit tissues.

Cimaterol, a catecholamine analog that acts as a beta-adrenergic agonist, has been shown to have a growth promoting effect in rabbits. Catecholamines are also known to stimulate ion transport in many tissues. The objective of this study was to determine the effect of dietary cimaterol on rabbit tissue Na(+)-K+ ATPase activity. Twelve New Zealand White rabbits, fed either control diet or cimaterol-supplemented diet, were killed at the end of a 35-d feeding trial. Heart, kidney, and liver were weighed, and total ATPase and Na(+)-K+ ATPase activities of these tissues were determined. Cimaterol did not affect liver and kidney weights, but heart weight was significantly increased. Cimaterol increased both total and Na(+)-K+ ATPase activities in heart and kidney but had no effect in liver. These data indicate that increased dietary energy intake and body energy expenditure in cimaterol-fed animals can be attributed, in part, to elevated Na(+)-K+ ATPase activities in heart and kidney.     

Evaluation of cimaterol for finishing swine including a drug withdrawal period

One hundred fifty crossbred pigs (55 kg) were allotted by weight, sex and litter to a randomized complete-block design with five dietary treatments, six blocks per treatment and five pigs per pen with sex equalized across treatments. Corn-soybean meal-based diets (.65% lysine) with 0, .25 and .5 mg/kg cimaterol were fed, on an ad libitum basis, to pigs slaughtered at an average pen weight of 104 kg/pig. Drug withdrawal prior to slaughter was 1, 3 and 5 d for pigs fed cimaterol at .25 mg/kg and 1 d for those fed cimaterol at .5 mg/kg of diet. Dietary cimaterol level influenced (quadratic, P less than .01) average daily gain during the first 42 d on test; however, daily feed intake and feed conversion ratio were not affected (P greater than .1). Pigs fed .25 mg/kg cimaterol with a 1-d drug withdrawal had 6.8, 7.7 and 13.5% less 10th rib fat depth and 11.1, 6.1 and 13.3% less P2 fat depth than those subjected to either a 3- or 5-d drug withdrawal or those fed the 0 mg/kg cimaterol diet (control), respectively. Overall, pigs fed cimaterol had 7.9% larger longissimus muscle area and 2.6% more kilograms of muscle than pigs fed the control diet. Cimaterol fed at .5 mg/kg resulted in higher (P less than .05) Warner-Bratzler shear force values and altered the proportion of saturation in some long-chain fatty acids, although the total saturated:unsaturated fat ratio was not affected. Pigs fed no cimaterol had less thaw loss (P less than .05) than did those fed other treatments.(ABSTRACT TRUNCATED AT 250 WORDS)     

钙蛋白酶系统在肌肉生长和肉品嫩化方面的研究

钙蛋白酶系统主要由钙蛋白酶(calpain)及钙蛋白酶抑制蛋白(calpastatin)组成,calpain是存在于细胞质中的依赖于Ca2+的中性蛋白酶,calpastatin是钙蛋白酶的内源抑制蛋白。近年的研究表明,calpain是细胞质中主要的蛋白水解酶,在肌原纤维蛋白降解中起着重要的作用。肌肉增长和宰后嫩度的变化与蛋白质水解程度密切相关。因此,钙蛋白酶系统的活性会影响畜禽肌肉增长和肉的嫩度。文中综述了钙蛋白酶系统各种酶的结构及其如何在肌肉生长和肉的嫩化中起作用。     

Predicting beef-longissimus tenderness from various biochemical and histological muscle traits

Our objective was to determine the predictive value of various biochemical and histological traits for tenderness of the longissimus muscle. Data collected from 27 crossbred cattle included longissimus pH, temperature, sarcomere length, total and percentage of soluble collagen, muscle-fiber type and area, cathepsin B and B + L activities, calcium-dependent protease (CDP)-I, -II and inhibitor activities, myofibril fragmentation indices (MFI), Warner-Bratzler shear (WBS) force, sensory-panel tenderness (SPT) ratings and carcass traits. Stepwise regression analyses were performed among breeds or pooled within breeds with WBS and SPT as dependent variables. When MFI were included in the analysis, MFI at d 7 explained 50% of the variation in WBS and SPT at d 14. An additional 19% of SPT was accounted for by the addition of CDP inhibitor d 1 activity and percentage-area of alpha R fibers to the model. However, because variation in MFI was not significant within breed subclasses and MFI could be classified more as a dependent variable, it was removed from the model. This resulted in CDP inhibitor d 1 activity explaining 44% of the variation in WBS and SPT at d 14. Also, percentage-area of beta R fibers, 6 h pH and cathepsin B + L d 14 activity appeared in the model. In addition, CDP inhibitor activity was the only variable to be significant within breed groups. These data suggest that d 7 MFI could be used as a single predictor of d 14 longissimus muscle tenderness; however, CDP inhibitor d 1 activity (a biological event) also may be useful in predicting tenderness.     

Combined effect of epinephrine and exercise on calpain/calpastatin and cathepsin B and L activity in porcine longissimus muscle.

The objective of the study was to improve the understanding of the relationship between the effect of epinephrine plus exercise and meat tenderness. The calpain, calpastatin, and cathepsin B + L activities and postmortem proteolysis in porcine longissimus muscle were studied. The muscle glycogen stores were depleted in five pigs by s.c. injection of epinephrine (.3 mg/kg) at 15 h antemortem and exercise on a treadmill (5 min, 3.8 km/h) immediately before slaughter. Antemortem injection of epinephrine and treadmill exercise resulted in higher ultimate pH (6.32 vs 5.66 in control) and decreased (P < .05) thaw loss, cooking loss, and shear force values. The muscle energy depletion treatment increased (P < .05) the muscle mu-calpain activity measured 42 min postmortem, and at 24 h mu-calpain activity was still approximately 50% greater in the high ultimate pH group. Also, as the ratio of mu-calpain to calpastatin increased (P < .01), the overall proteolytic potential of the calpain system were greater. These observations suggest that the muscle energy level may influence the activity of the calpain system in the living animal. The high ultimate pH group showed lower (P < .001) cathepsin B + L activity in the myofibrillar and the soluble fractions after 8 d of storage, suggesting that the increased ultimate pH increased the stability of the lysosomal membrane and thereby reduced the release of cathepsins from the lysosomes during storage. The SDS-PAGE showed increased (P < .001) degradation of a 39-kDa band in the epinephrine and exercise-treated samples. Degradation products at 30, 31, and 32 kDa were labeled by troponin-T antibody in western blot. An appearing 24-kDa band was identified as a troponin-I degradation product in western blot. The proteolytic degradation pattern of myofibrillar proteins during storage differed in control and treated samples, supporting the hypothesis that calpain-mediated proteolysis was affected after treatment, resulting in meat with high ultimate pH.     

Effects of cimaterol on nitrogen retention and energy utilization in lambs

Fifty-two weaned lambs were used in a comparative slaughter feeding trial and six lambs in a concurrent digestibility trial to investigate the effects of cimaterol on nitrogen retention and energy utilization. Cimaterol (CIM) was administered in the feed at 10 ppm for 90 and 14 d, respectively, in a comparative slaughter feeding trial and in a digestibility trial. No difference was found in dry matter digestibility. Nitrogen retention in the CIM group (739 mg/Wkg.75/d) was greater (P less than .01) than that of the control group (321 mg/Wkg.75/d). This difference was accounted for primarily by reduced nitrogen loss in urine of the CIM group. Cimaterol improved growth rate and feed/gain ratio, although these improvements were only evident during the first 42 d of the 90-d feeding trial. The improvement in growth performance of the CIM group was associated with increased protein gain in the empty body (40.2 g/d, P less than .01) as well as in carcass (26.9 g/d, P less than .01), compared with 30.1 and 14.5 g/d of the control group. Cimaterol decreased (P less than .01) fat gain (91.4 vs 109.9 g/d), total daily energy gain (1.08 vs 1.22 Mcal) and energy gain/kg gain (4.17 vs 5.11 Mcal) compared with the control. Feeding CIM increased (P less than .01) estimated fasting heat production (73 vs 64 Kcal/Wkg.75) and metabolizable energy requirement for maintenance (110.2 vs 92.7 Kcal/Wkg.75) over the control.(ABSTRACT TRUNCATED AT 250 WORDS)     

A modified procedure for simultaneous extraction and subsequent assay of calcium-dependent and lysosomal protease systems from a skeletal muscle biopsy

An extraction and assay system was developed for quantifying endogenous muscle proteases from a single 5-g sample. A single extraction buffer was developed for simultaneous extraction of both calcium-dependent proteases (CDP) and cathepsins. Protease activity determined by the modified procedure was compared to standard procedures currently used in our laboratory. The successful use of the modified procedure on muscle biopsies was verified. Activities per gram of ovine longissimus muscle of CDP system components for 50-g standard and 5-g modified procedures were not different (P greater than .05) for CDP-I (1.16 vs 1.08), CDP-II (.89 vs 1.03), or CDP inhibitor (2.34 vs 2.32), respectively. Activities of cathepsins per gram of muscle for standard and modified procedures were higher (P less than .05) for the modified procedure (cathepsins B + L, 202.0 vs 309.8), but not different (P greater than .05) for cathepsin B (76.6 vs 98.8). Cystatin-like activity was not different (P greater than .05; 3.4 vs 3.2). To test the effect of location within the longissimus muscle on protease activities, 5 g of longissimus muscle was removed immediately postmortem from each of six locations from each side of three steer carcasses. Location within the longissimus muscle had no effect (P greater than .05) on the protease activities measured. Protease activities determined on bovine longissimus muscle biopsies with the modified procedure were similar to immediate postmortem activities. These data verify that the modified procedure was as able to quantify endogenous muscle proteases as the standard procedures and could be used on muscle biopsies. This procedure should be useful in studying the role of endogenous muscle proteases in muscle growth and postmortem proteolysis.     

Effect of nutrient restriction on calpain and calpastatin content of skeletal muscle from cows and fetuses

Calpains are crucial for the degradation of myofibrillar proteins in muscle. Calpastatin is a specific inhibitor of calpains. The objective of this study was to elucidate the effect of nutrient restriction on the activity of calpains and calpastatin in the skeletal muscle of both cows and fetuses. Beginning 30 d after conception, 20 cows were fed either a control diet consisting of native grass hay fortified with vitamins and minerals at recommendations for a mature cow to gain 0.72 kg/d or half the vitamins and minerals and millet straw at 68.1% of NEm requirements. Cows were slaughtered on d 125 of gestation, and the LM was sampled at the 12th rib for calpain and calpastatin measurement. When comparing the muscle samples from nutrient-restricted and control cows, no difference in the activity of calpain I and II was observed; however, there was a significant difference (P < 0.05) in calpastatin activity. Muscle samples from control cows had greater calpastatin content than those of nutrient-restricted cows (P < 0.05); in contrast, the calpastatin content of fetal muscle was greater in fetuses gestated by nutrient-restricted cows than those of control cows (P < 0.05). Further, there were three calpastatin isoforms of 125, 110, and 70 kD detected in fetal muscle, whereas only the110-kD isoform was detected for cow muscle. These results indicate that the activity of the calpain system in skeletal muscle is mainly controlled through the expression of calpastatin. Alternating the calpastatin content in muscle and thereby modulating calpain activity may provide a mechanism for the maintenance of fetal muscle growth during nutrient restriction, whereas skeletal muscle loss in cows is upregulated.     

Effect of cimaterol on sheep adipose tissue lipid metabolism

Effects of dietary cimaterol (5 mg/kg) on adipose tissue metabolism of wether lambs were studied. Lipogenesis, lipolysis, fatty acid composition and adipocyte size and number were measured. Cimaterol feeding increased lipogenesis; however, this effect was not statistically significant. Insulin (1,000 microU/ml) stimulated lipogenesis of adipose tissue from control sheep. However, this elevated rate was abolished by in vitro cimaterol. Insulin had no stimulatory effect on lipogenesis in cimaterol-fed sheep. Lipolysis was depressed by cimaterol feeding. However, 10(-4) M cimaterol stimulated lipolysis in the adipose tissue from both control and cimaterol-fed sheep. Insulin inhibited stimulated lipolysis in adipose tissue from control sheep but had no effect on the stimulated lipolysis in cimaterol-fed sheep. Mean adipocyte diameter was smaller (from 74 to 70 microns) and adipocyte size distribution also was changed in the cimaterol-fed sheep. Adipocyte number per gram of tissue was not affected by cimaterol. There was a significant increase in percentage of unsaturated fatty acids in adipose tissue from cimaterol-fed sheep. These results indicate that lipogenic and lipolytic responses to insulin and cimaterol in sheep adipose tissue were altered by cimaterol feeding. The carcass fat content decrease in cimaterol-fed sheep may be attributed to the reduction in adipocyte size.     

Effect of the beta-adrenergic agonist L644,969 on muscle growth, endogenous proteinase activities, and postmortem proteolysis in wether lambs.

To examine the effect of a beta-adrenergic agonist (BAA) on muscle growth, proteinase activities, and postmortem proteolysis, 16 wether lambs were randomly assigned to receive 0 or 4 ppm of L644,969 in a completely mixed high-concentrate diet for 6 wk. Weight of the biceps femoris was 18.6% heavier in treated lambs. At 0 h after slaughter, treated lambs had higher cathepsin B (35.6%), cathepsins B + L (19.1%), calpastatin (62.8%), and m-calpain (24.6%) than control lambs, but both groups had similar mu-calpain activities. In both longissimus and biceps femoris muscles, treated lambs had higher protein and RNA and lower DNA concentrations. However, total DNA was not affected, indicating that the increase in muscle mass was probably due to muscle hypertrophy rather than to hyperplasia. The pattern of postmortem proteolysis was significantly altered by BAA feeding. In treated lambs, postmortem storage had no effect on the myofibril fragmentation index and degradation of desmin and troponin-T. These results indicate that the ability of the muscle to undergo postmortem proteolysis has been dramatically reduced with BAA feeding. Similar proteolytic systems are thought to be involved in antemortem and postmortem degradation of myofibrillar proteins, so BAA-mediated protein accretion is probably due, at least in part, to reduced protein degradation. To examine whether protein synthesis was altered with BAA feeding, the level of skeletal muscle alpha-actin mRNA was quantified. Longissimus muscle alpha-actin mRNA abundance was 30% greater in BAA-fed lambs. Collectively, these results indicate that dietary administration of BAA increases muscle mass through hypertrophy and that the increase in muscle protein accretion is due to reduced degradation and possibly to increased synthesis of muscle proteins.     

Effect of calpastatin on degradation of myofibrillar proteins by mu-calpain under postmortem conditions.

To improve our understanding of the regulation of mu-calpain activity in situ during postmortem storage of muscle, the effect of different calpastatin levels on proteolysis of myofibrillar proteins by mu-calpain in a system closely mimicking postmortem conditions was studied. Increasing the amount of calpastatin in the incubations limited both the rate and extent of proteolysis of myofibrillar proteins and autolysis of mu-calpain. Excess calpastatin (i.e., a mu-calpain:calpastatin ratio of 1:4) did not inhibit proteolysis completely. Western blot analysis revealed that proteolysis of myofibrillar proteins virtually ceased after 7 d of incubation, despite the presence of partly autolyzed, therefore seemingly active, mu-calpain. A series of incubations of autolyzed mu-calpain revealed that the autolyzed form of this enzyme is unstable at an ionic strength observed in postmortem muscle. The possible significance of these results in terms of the regulation of mu-calpain activity in postmortem muscle is discussed.     

Energy exchanges of broilers, selected for fatness and leanness, on diets with and without a repartitioning agent.

1. Two experiments were undertaken for 3 or 5 d in respiration chambers, on two experimental lines of broiler chickens (aged 25-38 d) selected for leanness and fatness. Diets were without or with 0.4 mg cimaterol per kg. 2. The lean line with sexes combined (experiment 1), or with females only, had a significantly greater heat production than the fat line. Net availability of metabolisable energy for gain (kg) was 0.54 for the lean birds and and 0.84 for the fat birds. 3. Cimaterol did not have an effect on any of the variables examined.