I agree with ironmaster that you have to know your reason for using insulin.
BTW, insulin is not as anabolic as some think.
Its effect on suppression of protein breakdown is probably more significant...
It was thought that it only has a permissive role on protein synthesis, where only a little is needed for an increase of protein synthesis caused by hyperaminoacidemia, although some recent studies have shown that extreme hyperinsulinemia can promote anabolism ...
Insulin makes you fat by decreasing lypolisis & increasing lipogenesis, so if you want to minimize fat gain, a short acting insulin is a better option.
For bulking, you might get better results with long acting...
As for the window of opportunity, everyone knows how important it is to consume their postworkout drink after exercise, but the effect of exercise on muscle protein turnover is not as short lasting as some think.
Muscle protein synthesis is elevated >24 hours after exercise, degradation is also elevated quite long also..
Diabetes 1999 May;48(5):949-57 Related Articles, Links
Insulin action on muscle protein kinetics and amino acid transport during recovery after resistance exercise.
Biolo G, Williams BD, Fleming RY, Wolfe RR.
Department of Internal Medicine, University of Texas Medical Branch, and the Shriners Burns Hospital, Galveston, USA.
We have determined the individual and combined effects of insulin and prior exercise on leg muscle protein synthesis and degradation, amino acid transport, glucose uptake, and alanine metabolism. Normal volunteers were studied in the postabsorptive state at rest and about 3 h after a heavy leg resistance exercise routine. The leg arteriovenous balance technique was used in combination with stable isotopic tracers of amino acids and biopsies of the vastus lateralis muscle. Insulin was infused into a femoral artery to increase the leg insulin concentrations to high physiologic levels without substantively affecting the whole-body level. Protein synthesis and degradation were determined as rates of intramuscular phenylalanine utilization and appearance, and muscle fractional synthetic rate (FSR) was also determined. Leg blood flow was greater after exercise than at rest (P<0.05). Insulin accelerated blood flow at rest but not after exercise (P<0.05). The rates of protein synthesis and degradation were greater during the postexercise recovery (65+/-10 and 74+/-10 nmol x min(-1) x 100 ml(-1) leg volume, respectively) than at rest (30+/-7 and 46+/-8 nmol x min(-1) x 100 ml(-1) leg volume, respectively; P<0.05).
Insulin infusion increased protein synthesis at rest (51+/-4 nmol x min(-1) x 100 ml(-1) leg volume) but not during the postexercise recovery (64+/-9 nmol x min(-1) x 100 ml(-1) leg volume; P<0.05). Insulin infusion at rest did not change the rate of protein degradation (48+/-3 nmol x min(-1) 100 ml(-1) leg volume). In contrast, insulin infusion after exercise significantly decreased the rate of protein degradation (52+/-9 nmol x min(-1) x 100 ml(-1) leg volume)....
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J Clin Invest 1995 Oct;96(4):1722-9 Related Articles, Links
Insulin and insulin-like growth factor-I enhance human skeletal muscle protein anabolism during hyperaminoacidemia by different mechanisms.
Fryburg DA, Jahn LA, Hill SA, Oliveras DM, Barrett EJ.
Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville 22908, USA.
Insulin inhibits proteolysis in human muscle thereby increasing protein anabolism. In contrast, IGF-I promotes muscle protein anabolism principally by stimulating protein synthesis. As increases or decreases of plasma amino acids may affect protein turnover in muscle and also alter the muscle's response to insulin and/or IGF-I, this study was designed to examine the effects of insulin and IGF-I on human muscle protein turnover during hyperaminoacidemia. We measured phenylalanine balance and [3H]-phenylalanine kinetics in both forearms of 22 postabsorptive adults during a continuous [3H] phenylalanine infusion. Measurements were made basally and at 3 and 6 h after beginning a systemic infusion of a balanced amino acid mixture that raised arterial phenylalanine concentration about twofold. Throughout the 6 h, 10 subjects received insulin locally (0.035 mU/min per kg) into one brachial artery while 12 other subjects were given intraaterial IGF-I (100 ng/min per kg) to raise insulin or IGF-I concentrations, respectively, in the infused arm. The contralateral arm in each study served as a simultaneous control for the effects of amino acids (aa) alone. Glucose uptake and lactate release increased in the insulin- and IGF-I-infused forearms (P < 0.01) but did not change in the contralateral (aa alone) forearm in either study. In the aa alone arm in both studies, hyperaminoacidemia reversed the postabsorptive net phenylalanine release by muscle to a net uptake (P < 0.025, for each) due to a stimulation of muscle protein synthesis. In the hormone-infused arms, the addition of either insulin or IGF-I promoted greater positive shifts in phenylalanine balance than the aa alone arm (P < 0.01). With insulin, the enhanced anabolism was due to inhibition of protein degradation (P < 0.02), whereas IGF-I augmented anabolism by a further stimulation of protein synthesis above aa alone (P < 0.02).
We conclude that: (a) hyperaminoacidemia specifically stimulates muscle protein synthesis; (b) insulin, even with hyperaminoacidemia, improves muscle protein balance solely by inhibiting proteolysis; and (c) hyperaminoacidemia combined with IGF-I enhances protein synthesis more than either alone...
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Int J Sport Nutr Exerc Metab 2001 Dec;11 Suppl:S164-9 Related Articles, Links
Control of muscle protein breakdown: effects of activity and nutritional states.
Wolfe RR.
Department of Surgery/Metabolism, University of Texas Medical Branch, Shriners Burns Hospital, Galveston 77550, USA.
We propose that there is a link between muscle protein synthesis and breakdown that is regulated, in part, through maintenance of the free intracellular pool of essential amino acids. For example, we propose that muscle protein breakdown is paradoxically elevated in the anabolic state following resistance exercise in part because the even greater stimulation of synthesis would otherwise deplete this pool. Thus, factors regulating muscle protein breakdown must be evaluated in the context of the prevailing rate of muscle protein synthesis. Further, the direct effect of factors on breakdown may depend on the physiological state.
For example, local hyperinsulinemia suppresses accelerated muscle protein breakdown after exercise, but not normal resting breakdown. Thus, factors regulating muscle protein breakdown in human subjects are complex and interactive.
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Effect of physiologic hyperinsulinemia on skeletal muscle protein synthesis and breakdown in man.
Gelfand RA, Barrett EJ.
Although insulin stimulates protein synthesis and inhibits protein breakdown in skeletal muscle in vitro, the actual contribution of these actions to its anabolic effects in man remains unknown. Using the forearm perfusion method together with systemic infusion of L-[ring-2,6-3H]phenylalanine and L-[1-14C]leucine, we measured steady state amino acid exchange kinetics across muscle in seven normal males before and in response to a 2-h intraarterial infusion of insulin. Postabsorptively, the muscle disposal (Rd) of phenylalanine (43 +/- 5 nmol/min per 100 ml forearm) and leucine (113 +/- 13) was exceeded by the concomitant muscle production (Ra) of these amino acids (57 +/- 5 and 126 +/- 9 nmol/min per dl, respectively), resulting in their net release from the forearm (-14 +/- 4 and -13 +/- 5 nmol/min per dl, respectively). In response to forearm hyperinsulinemia (124 +/- 11 microU/ml), the net balance of phenylalanine and leucine became positive (9 +/- 3 and 61 +/- 8 nmol/min per dl, respectively (P less than 0.005 vs. basal). Despite the marked increase in net balance, the tissue Rd for both phenylalanine (42 +/- 2) and leucine (124 +/- 9) was unchanged from baseline, while Ra was markedly suppressed (to 33 +/- 5 and 63 +/- 9 nmol/min per dl, respectively, P less than 0.01).
Since phenylalanine is not metabolized in muscle (i.e., its only fates are incorporation into or release from protein) these results strongly suggest that in normal man, physiologic elevations in insulin promote net muscle protein anabolism primarily by inhibiting protein breakdown, rather than by stimulating protein synthesis.
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Int J Sport Nutr Exerc Metab 2001 Mar;11(1):109-32 Related Articles, Links
Exercise, protein metabolism, and muscle growth.
Tipton KD, Wolfe RR.
Metabolism Division, Department of Surgery, University of Texas Medial Branch-Galveston, Galveston, TX 77550-2720, USA.
Exercise has a profound effect on muscle growth, which can occur only if muscle protein synthesis exceeds muscle protein breakdown; there must be a positive muscle protein balance. Resistance exercise improves muscle protein balance, but, in the absence of food intake, the balance remains negative (i.e., catabolic). The response of muscle protein metabolism to a resistance exercise bout lasts for 24-48 hours; thus, the interaction between protein metabolism and any meals consumed in this period will determine the impact of the diet on muscle hypertrophy. Amino acid availability is an important regulator of muscle protein metabolism. The interaction of postexercise metabolic processes and increased amino acid availability maximizes the stimulation of muscle protein synthesis and results in even greater muscle anabolism than when dietary amino acids are not present. Hormones, especially insulin and testosterone, have important roles as regulators of muscle protein synthesis and muscle hypertrophy.
Following exercise, insulin has only a permissive role on muscle protein synthesis, but it appears to inhibit the increase in muscle protein breakdown. Ingestion of only small amounts of amino acids, combined with carbohydrates, can transiently increase muscle protein anabolism, but it has yet to be determined if these transient responses translate into an appreciable increase in muscle mass over a prolonged training period.
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J Nutr 2002 Oct;132(10):3225S-7S Related Articles, Links
Latency, duration and dose response relationships of amino acid effects on human muscle protein synthesis.
Rennie MJ, Bohe J, Wolfe RR.
Division of Molecular Physiology, School of Life Sciences, University of Dundee, Scotland, United Kingdom.
m.j.rennie@dundee.ac.uk
The components of the stimulatory effect of food on net deposition of protein are beginning to be identified and separated. One of the most important of these appears to be the effect of amino acids per se in stimulating muscle anabolism. Amino acids appear to have a linear stimulatory effect within the range of normal diurnal plasma concentrations from postabsorptive to postprandial. Within this range, muscle protein synthesis (measured by incorporation of stable isotope tracers of amino acids into biopsied muscle protein) appears to be stimulated approximately twofold; however, little further increase occurs when very high concentrations of amino acids (>2.5 times the normal postabsorptive plasma concentration) are made available. Amino acids provided in surfeit of the ability of the system to synthesize protein are disposed of by oxidation, ureagenesis and gluconeogenesis. The stimulatory effect of amino acids appears to be time dependent; a square wave increase in the availability of amino acids causes muscle protein synthesis to be stimulated and to fall back to basal values, despite continued amino acid availability.
The relationship between muscle protein synthesis and insulin availability suggests that most of the stimulatory effects occur at low insulin concentrations, with large increases having no effect. These findings may have implications for our understanding of the body's requirements for protein. The maximal capacity for storage of amino acids as muscle protein probably sets an upper value on the extent to which amino acids can be stored after a single meal.
