The history of anabolic steroids and a review of clinical experience with anabolic steroids
105
Citation
0
Reference
10
Related Paper
Citation Trend
Abstract:
Metabolism is the term employed to embrace the various physical and chemical processes occurring within the tissues upon which the growth and heat production of the body depend and from which the energy for muscular activity, for the maintenance of vital activity and for the maintenance of vital functions is derived (Best & Taylor 1950). The destructive processes by which complex substances are converted by living cells into more simple compounds are called catabolism. Anabolism denotes the constructive processes by which simple substances are converted by living cells into more complex compounds, especially into living matter. Catabolism and anabolism are part of all metabolic processes, the carbohydrate, fat and protein metabolism. The term anabolic refers only to substances that exert an anabolic effect on protein metabolism and are unlikely to cause adverse androgenic effects. They shift the equilibrium between protein synthesis and degradation in the body as a whole in the direction of synthesis, either by promoting protein synthesis or reducing its breakdown. The protein anabolic effect of anabolic steroids is not restricted to single organs but is the result of stimulated biosynthesis of cellular protein in the whole organism.Keywords:
Catabolism
Anabolic Agents
Protein metabolism
Protein Degradation
Anabolic Agents
Cite
Citations (12)
Amino acid metabolism
Muscle protein
Protein metabolism
Human muscle
Cite
Citations (103)
In healthy active older persons, there is no derangement of muscle protein metabolism. However, there is a major deficit in the ability of older muscles to regulate their maintenance during feeding and exercise. The dose–response relationship between myofibrillar protein synthesis and the availability of essential amino acids (EAA) is shifted down and to the right, and giving extra amino acids is unable to overcome this. There is no sex difference in basal or fed muscle protein metabolism in the young, but postmenopausal women have a greater anabolic resistance than older men. Anabolic resistance is also shown by the decreased phosphorylation in the PKB–mTOR–eIF4BP1 pathway in response to increased EAA. The muscle synthetic system is refractory to EAA provision, irrespective of the availability of insulin, insulin-like growth factor 1, and growth hormone. However, insulin is a major regulator of muscle protein breakdown, and there is a blunting of the ability of older muscle to decrease proteolysis in response to low concentrations of insulin, such as those observed after a light breakfast. Providing more EAA seems not to be useful, and modern N-balance data confirm that the dietary protein requirements of older persons are not increased. The sigmoidal dose–response relationship between muscle protein synthesis and resistance exercise intensity is shifted downward and to the right in older men. Decreased physical activity itself, even in young subjects, can produce anabolic resistance of muscle protein synthesis, which cannot be overcome by increasing amino acid availability. Exercise may retune the amino acid and (or) insulin sensitivity of muscle in older people.
Protein metabolism
Catabolism
Myofibril
Cite
Citations (129)
Protein turnover
Catabolism
Protein Degradation
Protein metabolism
Cite
Citations (34)
Background: Patients with chronic heart failure frequently experience profound wasting during the course of the disease, a condition termed cardiac cachexia. Although protein is the primary structural and functional component of most tissues, few studies have examined the effect of heart failure on protein metabolism. Moreover, no study has assessed the relationship of protein turnover to hormonal alterations thought to promote cachexia. Thus, our goal was to determine if whole‐body protein metabolism is altered in heart failure patients and to assess the relationship of protein kinetics to circulating levels of anabolic and catabolic hormones. Methods: We measured whole‐body protein metabolism using 13 C‐leucine, body composition, and circulating anabolic and catabolic hormone levels in 10 patients with chronic heart failure and 11 elderly controls. Results: No differences in leucine rate of appearance, oxidation, or nonoxidative disposal were noted between heart failure patients and controls. However, in a subgroup of patients characterized by increased resting energy expenditure for their metabolic body size (n = 4; ≥20% above that predicted from fat‐free mass), leucine rate of appearance (mean ± SE; 146 ± 6 μmol/min), an index of protein breakdown, tended to be higher compared with patients with normal resting energy expenditure (n = 5; 120 ± 8 μmol/min) and controls (127± 4 μmol/min; p = .06). Alterations in anabolic/catabolic hormone balance did not explain increased protein breakdown in this subgroup, and no correlations were found between hormone levels and protein breakdown in the heart failure group as a whole. In contrast, increased circulating interleukin‐6 soluble receptor ( r = 0.829; p < .01) and reduced insulin‐like growth factor‐I ( r =–.751; p < .05) levels were related to greater rates of leucine oxidation in heart failure patients. Conclusion: Our results demonstrate that, although increased protein turnover is not a generalized feature of heart failure, there is a subgroup of patients characterized by resting hypermetabolism and increased protein breakdown. Moreover, hormonal alterations related to the heart failure syndrome were related to increased protein oxidation.
Catabolism
Protein turnover
Protein metabolism
Protein Degradation
Anabolic steroid
Cite
Citations (19)
Abstract Background Treatment with glucocorticosteroids causes a negative nitrogen balance, but the kinetic mechanisms responsible for this catabolic effect are controversial. We investigated the effects of 60 mg day −1 prednisolone on protein synthesis and degradation in human skeletal muscle. Materials and methods Healthy adults ( n = 9) were studied in the postabsorptive state, before and after 3 days of prednisolone treatment. The L‐[ring 2,6 ‐3 H 5 ]‐phenylalanine tracer technique, concentration and size distribution of the ribosomes, mRNA content of the ubiquitin‐proteasome pathway components in muscle, phenylalanine flux across the leg, and the free amino acid concentrations in skeletal muscle were used to study muscle protein metabolism. Results The concentrations of most amino acids in arterial blood increased after prednisolone. There were also increased effluxes of phenylalanine, asparagine, arginine, alanine, methionine and isoleucine from the leg. The rate of protein degradation, as measured by the appearance rate (Ra) of phenylalanine, increased by 67% ( P = 0·023) which, together with a doubling of the net release of phenylalanine from the leg ( P = 0·007), indicated accelerated protein degradation. The pathway was not identified but there was no significant increase in mRNAs’ encoding components of the ubiquitin‐proteasome pathway. There was a 6% reduction in polyribosomes ( P = 0·007), suggesting a decrease in the capacity for protein synthesis, although there was no measured decrease in the rate of protein synthesis. Conclusions These findings indicate that high doses of prednisolone lead to a sharp increase in net protein catabolism, which depends more on enhanced protein breakdown, and an uncertain effect on protein synthesis. The mechanisms stimulating proteolysis and the pathway stimulated to increase muscle protein degradation should be explored.
Protein turnover
Human muscle
Turnover
Cite
Citations (126)
Metabolism is the term employed to embrace the various physical and chemical processes occurring within the tissues upon which the growth and heat production of the body depend and from which the energy for muscular activity, for the maintenance of vital activity and for the maintenance of vital functions is derived (Best & Taylor 1950). The destructive processes by which complex substances are converted by living cells into more simple compounds are called catabolism. Anabolism denotes the constructive processes by which simple substances are converted by living cells into more complex compounds, especially into living matter. Catabolism and anabolism are part of all metabolic processes, the carbohydrate, fat and protein metabolism. The term anabolic refers only to substances that exert an anabolic effect on protein metabolism and are unlikely to cause adverse androgenic effects. They shift the equilibrium between protein synthesis and degradation in the body as a whole in the direction of synthesis, either by promoting protein synthesis or reducing its breakdown. The protein anabolic effect of anabolic steroids is not restricted to single organs but is the result of stimulated biosynthesis of cellular protein in the whole organism.
Catabolism
Anabolic Agents
Protein metabolism
Protein Degradation
Cite
Citations (105)
The recovery of approximately 40% of the total liver protein during the first day after partial hepatectomy was shown to be due to the near cessation of protein breakdown rather than to an increase in protein synthesis. The decrease in degradation of total protein was less if rats were adrenalectomized or protein-depleted prior to partial hepatectomy. The effect of these treatments originally suggested that changes in free amino acid levels in liver might be related to the rate of protein degradation. However, no correlation was found between levels of total free amino acids and rates of breakdown. Measurements of individual amino acids during liver regeneration suggested that levels of free methionine and phenylalanine, amino acids that have been found to lower rates of protein degradation in vitro, are not correlated with rates of breakdown in vivo. The difference between the fractional rate of ornithine aminotransferase degradation (0.68/day and 0.28/day in sham-hepatectomized and partially hepatectomized rats, respectively) was sufficient to account for the higher level of this protein 3 days after surgery in the latter group.
Protein Degradation
Liver Regeneration
Protein metabolism
Protein turnover
Cite
Citations (13)
Nutrients regulate protein metabolism both in an acute fashion and on a long‐term basis. The ingestion of meals is associated with a dramatic switch from an overall catabolic state to a state of net protein anabolism. The acute response of protein metabolism to meal ingestion is mediated, in part, by an increase in insulin secretion, itself a consequence of glucose absorption. Whereas insulin may primarily suppress rates of proteolysis, amino acids are responsible for the stimulation of protein synthesis that follows food intake. In the long run, the effects of nutrition on protein metabolism depend on the energy supply, the source of the energy (carbohydrate versus fat) and dietary protein intake. Finally, specific amino acids, such as glutamine, may play an additional role as protein anabolic agents.
Catabolism
Protein metabolism
Proteolysis
Protein Degradation
Carbohydrate Metabolism
Protein turnover
Federal state
Cite
Citations (14)
Most patients who are critically ill lose muscle as a result of an inability to maintain rates of protein synthesis above those of protein breakdown. In addition to the effects of a procatabolic hormonal and cytokine milieu, which accelerate protein breakdown, age and immobility also influence the ability of muscle to maintain itself. Although the basal rates of protein turnover are not altered with aging, age is associated with a smaller ability to capture blood-borne amino acids as protein, the results of a decreased capacity for protein synthesis (total RNA/DNA) and decreased sensitivity and capacity of signaling proteins to indicate the availability of amino acids. Furthermore, muscle of older individuals is resistant to the effects of insulin in decreasing muscle proteolysis. Both of these effects are part of "anabolic resistance"—the inability of muscle to maintain its protein mass by appropriate stimulation of muscle protein turnover and inhibition of protein breakdown. Overlain on the effects of age are the effects of immobility, which has some of the characteristics of anabolic resistance. Immobility per se causes a decrease in muscle protein synthesis with no apparent stimulation of muscle protein breakdown; furthermore, muscle of immobilized legs is unable to stimulate muscle protein synthesis to the same extent as that of nonimmobilized legs when amino acids are infused, even at high rates.
Cite
Citations (90)