Sarcoplasmic Protein Synthesis Research Articles

Ethanol‐induced inhibition of ventricular protein synthesis in vivo and the possible role of acetaldehyde

We have determined the extent to which acute ethanol administration perturbs the synthesis of ventricular contractile and non-contractile proteins in vivo. Male Wistar rats were treated with a standard dose of ethanol (75 mmol kg-1 body weight; i.p.). Controls were treated with isovolumetric amounts of saline (0.15 mol l-1 NaCl). Two metabolic inhibitors of ethanol metabolism were also used namely 4-methylpyrazole (alcohol dehydrogenase inhibitor) and cyanamide (acetaldehyde dehydrogenase inhibitor) which in ethanol-dosed rats have been shown to either decrease or increase acetaldehyde formation, respectively. After 2.5 h, fractional rates of protein synthesis (i.e. the percentage of tissue protein renewed each day) were measured with a large (i.e. 'flooding') dose of L-[4-3H]phenylalanine (150 mumol (100 g)-1 body weight into a lateral vein). This dose of phenylalanine effectively floods all endogenous free amino acid pools so that the specific radioactivity of the free amino acid at the site of protein synthesis (i.e. the amino acyl tRNA) is reflected by the specific radioactivity of the free amino acid in acid-soluble portions of cardiac homogenates. The results showed that ethanol alone and ethanol plus 4-methylpyrazole decreased the fractional rates of mixed, myofibrillar (contractile) and sarcoplasmic (non-contractile) protein synthesis to the same extent (by approx. 25 per cent). Profound inhibition (i.e. 80 per cent) in the fractional rates of mixed, myofibrillar and sarcoplasmic protein synthesis occurred when cyanamide was used to increase acetaldehyde formation. There was also a significant decrease in cardiac DNA content. The results suggest that acute ethanol-induced cardiac injury in the rat may be mediated by both acetaldehyde and ethanol.

Comparative Effects of Thermal and Surgical Trauma on Rat Muscle Protein Metabolism

A modified intraperitoneal pool flooding technique, employing L-3H-tyrosine, was developed for measuring muscle protein synthetic rates following traumatic injury. Sufficient radiolabeled tyrosine was injected intraperitoneally to effect a six-fold increase in plasma tyrosine concentration (124-800 microM) resulting in constant, sustained specific radioactivities in plasma- and intracellular-free tyrosine pools. Localized vs systemic effects of thermal and surgical trauma on gastrocnemius muscle protein turnover were assessed 2 and 4 days postinjury. Thermal trauma increased total, myofibrillar, and sarcoplasmic muscle protein synthesis (44%) and protein degradation (300%). Conversely, surgical trauma decreased synthesis of total (24%), myofibrillar (14%), and sarcoplasmic (43%) muscle proteins without altering protein degradation. Short-term restriction of pair-fed controls did not affect either aspect of protein turnover.

Starvation Effects on Protein Synthesis in Red and White Muscle of the Barred Sand Bass,Paralabrax nebulifer

Starvation of the fish Paralabrax nebulifer was accompanied by complex changes in the synthesis rates of different classes of proteins within the white muscle. Synthesis of white-muscle myofibrillar proteins, as measured by incorporation of 14C-leucine, decreased rapidly during starvation, whereas synthesis of total sarcoplasmic proteins was unchanged. Although actin and aldolase label incorporation in white muscle underwent an immediate decrease to approximately 10% of control, lactate dehydrogenase and creatine phosphokinase showed a smaller initial decrease. Relative activities of white-muscle glycolytic enzymes were conserved despite a significant loss in overall glycolytic capacity. Control of specific synthesis rates may be important in maintaining an overall balance of proteins with different half-lives. In red muscle, starvation led to no reductions in the synthesis of any protein examined. Changes in muscle protein synthesis rates were reflected in a larger decrease in RNA/DNA ratio in white muscle than in red muscle during starvation. These results suggest that balanced metabolic function is retained during starvation in fishes, and that starvation may have differential effects on high- and low-speed swimming abilities.

Effects of immobilization on rat hind limb muscles under non-weight-bearing conditions.

Dorsiflexion of one unloaded hind limb caused hypertrophy of the soleus relative to weight-bearing controls and faster growth of the plantaris and gastrocnemius muscles relative to the contralateral freely moving muscles. Unloading of the soleus muscle diminished primarily myofibrillar proteins whereas stretching increased all proteins. Stretching the soleus increased RNA, accelerated, especially, in vitro synthesis of sarcoplasmic proteins, and diminished in vitro proteolysis. Both in vivo and in vitro results showed slower synthesis and faster degradation in the freely moving than in the weight-bearing soleus muscle, faster synthesis and slower degradation in the stretched than in the freely moving soleus muscle, and faster degradation in the stretched than in the weight-bearing soleus muscle. Hence, stretching of the soleus muscle prevented changes in mass and protein metabolism produced by unloading. Shortening of the extensor digitorum longus muscle produced less muscle growth, slowed in vitro protein synthesis, and lowered RNA relative to the contralateral, freely moving muscle.

Role of glucocorticoids in the response of rat leg muscles to reduced activity.

Adrenalectomy did not prevent atrophy of rat soleus muscle during 6 days of tail cast suspension. Cortisol treatment enhanced this atrophy and caused atrophy of the weight-bearing soleus and both extensor digitorum longus (EDL) muscles. Unloading led to increased sarcoplasmic protein concentration in the soleus, but cortisol administration increased the myofibrillar (+stromal) protein concentration in both muscles. Suspension of hindlimbs of adrenalectomized animals led to faster protein degradation, slower sarcoplasmic protein synthesis, and faster myofibrillar protein synthesis in the isolated soleus, whereas with cortisol-treated animals, the difference in synthesis of myofibrillar proteins was enhanced and that of sarcoplasmic proteins was abolished. Both soleus and EDL of suspended, cortisol-treated animals showed faster protein degradation. It is unlikely that any elevation in circulating glucocorticoids was solely responsible for atrophy of the soleus in this model, but catabolic amounts of glucocorticoids could alter the response of muscle to unloading.

Age-related changes in the incorporation of [14-C] leucine into myofibrillar and sarcoplasmic proteins of red and white muscles of chicks.

Studies on the incorporation of DL-[1- 14-C] leucine into myosin, total myofibrillar protein and total sarcoplasmic protein have shown age-dependent alterations in the rate of synthesis of these protiens in red and white skeletal muscles of chicks. During the early phase of ex ovo development white muscle synthesizes significantly higher amounts of myofibrillar proteins, especially myosin, in comparison with red muscle. The rate of sarcoplasmic protein synthesis in red and white muscles one day after hatching is almost identical. The red muscle shows a markedly higher rate of sarcoplasmic protein synthesis from 10 days after hatching. The incorporation of amino acid into various protein fractions of both the muscle types decreases with advancing age. In adult chicks red muscle displays a higher ability to synthesize sarcoplasmic and myofibrillar proteins.

Protein turnover in skeletal muscle of piglets.

1. Rates of protein synthesis and catabolism were measured in longissimus dorsi and hind-limb muscles of suckling piglets.2. Half-lives for synthesis and catabolism for mixed sarcoplasmic proteins were 4.8 and 9.4 d respectively. The corresponding values for mixed myofibrillar proteins were 5.7 and 16.4 d.3. The half-lives for synthesis of sarcoplasmic proteins were significantly different from those of myofibrillar proteins and were not confounded by contamination of the sarcoplasmic protein fraction with plasma proteins of higher specific activity.4. Individual myofibrillar proteins were synthesized and catabolized at rates which were not statistically significantly different. Intramuscular connective tissue also appeared to turnover rapidly, the half-life for synthesis being 8 d and that for catabolism 20 d.5. Values obtained for the specific radioactivities of aspartate + glutamate in mixed plasma proteins support the view that, in so far as the young of animals larger in mature body size than rats or mice are concerned, muscle assumes a more important role relative to liver in regulating whole body amino acid metabolism.

Effect of insulin on the synthesis of sarcoplasmic and ribosomal proteins of muscle.

RIBOSOMES isolated from skeletal muscle of alloxan diabetic rats are only half as effective as those from normal animals in catalysing the synthesis of protein1–4. Administration of insulin to diabetic animals restores the activity of the ribosomes to normal1. The identity of the proteins the synthesis of which is regulated by insulin, however, is not known. We report here the results of preliminary experiments that bear on the problem.

Unbalanced synthesis of contractile and sarcoplasmic proteins in denervated frog muscle

Unbalanced synthesis of contractile and sarcoplasmic proteins in denervated frog muscle