Insulin action on skeletal muscle protein metabolism during catabolic states

Grizard, Jean; Dardevet, Dominique; Balage, Michèle; Larbaud, Daniel; Sinaud, Sandrine; Savary, Isabelle; Grzelkowska, K.; Rochon, Cécile; Tauveron, Igor; Obled, Christiane

doi:10.1051/rnd:19990104

Cited by 24 publications

(14 citation statements)

References 36 publications

(38 reference statements)

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“…Conversely, IGF-I decreased basal levels of protein breakdown, increased total RNA, and, most notably, prevented the Dex-induced increase in overall and myofibrillar protein breakdown and the decrease in protein content. Thus IGF-I is a dominant signal over glucocorticoids in determination of muscle protein balance in vitro, as has been suggested for insulin in vivo (17). Simultaneous administration of IGF-I with glucocorticoids to rats significantly attenuates the glucocorticoid-induced muscle atrophy and myofibrillar protein breakdown as measured by 3-MH excretion (21).…”

Section: Discussionmentioning

confidence: 76%

IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1

Sacheck¹,

Ohtsuka²,

McLary³

et al. 2004

American Journal of Physiology-Endocrinology and Metabolism

536

455

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Section: Discussionmentioning

confidence: 76%

IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1

Sacheck¹,

Ohtsuka²,

McLary³

et al. 2004

American Journal of Physiology-Endocrinology and Metabolism

536

455

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“…In addition, various metabolic disturbances liable to be accompanied by acidosis (diabetes, sepsis) result in a decrease in insulin action on protein synthesis or degradation but, in contrast, the antiproteolytic action of insulin could be improved during hyperthyroidism (Grizard et al 1999).…”

Section: Acid-base Status and Protein Metabolismmentioning

confidence: 99%

Organic anions and potassium salts in nutrition and metabolism

et al. 2004

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The present review examines the importance of dietary organic anions in preventive nutrition. Organic anions are chiefly supplied by plant foods, as partially neutralised K salts such as potassium citrate, potassium malate and, to a lesser extent, oxalate or tartrate salts. Animal products may also supply K anions, essentially as phosphate, but also as lactate as a result of fermentative or maturation processes, but these K salts have little alkalinising significance. Citrate and malate anions are absorbed in the upper digestive tract, while a substantial proportion is probably metabolised in the splanchnic area. Whatever their site of metabolism, these anions finally yield KHCO 3 which is used by the kidneys to neutralise fixed acidity. This acidity essentially reflects the oxidation of excess S amino acids to sulfate ions, which is mainly related to the dietary protein level. Failure to neutralise acidity leads to low-grade metabolic acidosis, with possible long-term deleterious effects on bone Ca status and on protein status. Furthermore, low-grade acidosis is liable to affect other metabolic processes, such as peroxidation of biological structures. These metabolic disturbances could be connected with the relatively high incidence of osteoporosis and muscle-protein wasting problems observed in ageing individuals in Europe and Northern America. Providing a sufficient supply of K organic anions through fruit and vegetable intake should be recommended, fostering the actual motivational campaigns ('five (or ten) per d') already launched to promote the intake of plant foods rich in complex carbohydrates and various micronutrients.

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“…In healthy adult humans, insulin promotes an anabolic state, augmenting cellular glucose uptake and enhancing muscle protein deposition (23,30,41). During experimental sepsis, LPS has been shown to induce pancreatic insulin secretion (28) and to increase circulating insulin levels similar to that observed in naturally occurring sepsis (32,46).…”

mentioning

confidence: 96%

Modulation of muscle protein synthesis by insulin is maintained during neonatal endotoxemia

Orellana¹,

O'Connor²,

Bush³

et al. 2006

American Journal of Physiology-Endocrinology and Metabolism

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motes insulin resistance and reduces protein synthesis in skeletal muscle of adults. The effect of sepsis on insulin-stimulated muscle protein synthesis has not been determined in neonates, a highly anabolic population that is uniquely sensitive to insulin. Overnight fasted neonatal pigs were infused for 8 h with endotoxin [lipopolysaccharide (LPS), 0 and 10 g ⅐ kg Ϫ1 ⅐ h Ϫ1 ]. Glucose and amino acids were maintained at fasting levels, insulin was clamped at either fasting or fed (2 or 10 U/ml) levels, and fractional protein synthesis rates were determined at the end of the infusion. LPS infusion induced a septic-like state, as indicated by a sustained elevation in body temperature, heart rate, and cortisol. At fasting insulin levels, LPS reduced fractional protein synthesis rates in gastrocnemius muscle (Ϫ26%) but had no effect on the masseter and heart. By contrast, LPS stimulated liver protein synthesis (ϩ28%). Increasing insulin to fed levels accelerated protein synthesis rates in gastrocnemius (controls by ϩ38%, LPS by ϩ60%), masseter (controls by ϩ50%, LPS by ϩ43%), heart (controls by ϩ34%, LPS by ϩ40%), and diaphragm (controls by ϩ54%, LPS by ϩ29%), and the response to insulin was similar in LPS and controls. Insulin did not alter protein synthesis in liver, kidney, or jejunum in either group. These findings suggest that acute endotoxemia lowers basal fasting muscle protein synthesis in neonates but does not alter the response of protein synthesis to insulin. growth; amino acids; protein metabolism; insulin resistance; sepsis BACTERIAL ENDOTOXIN [lipopolysaccharide (LPS)] elicits a systemic inflammatory response that has profound consequences on human metabolic homeostasis (1, 45). The physiological response to LPS mimics the metabolic processes triggered by the generalized immune response observed during sepsis, such as insulin resistance for glucose and amino acid metabolism (1,39,46) and the profound reduction of muscle protein synthesis in adult animals (26,29). Hormones and acute-phase reactants that exert and regulate the stress response during sepsis, such as tumor necrosis factor-␣ (TNF-␣), cortisol, insulin, and insulin-like growth factor I (17,44,45), affect the metabolic homeostasis in the normal host, and LPS has been recognized as a potent stimulus that elicits this innate immune response (17,18,44,49).

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Insulin action on skeletal muscle protein metabolism during catabolic states

Cited by 24 publications

References 36 publications

IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1

IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1

Organic anions and potassium salts in nutrition and metabolism

Modulation of muscle protein synthesis by insulin is maintained during neonatal endotoxemia

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