post workout shake?

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    post workout shake?


    yes i know this thread has been made about a million times on various threads, but here we go. i just ordered some dextrose from 1 fast and decided to add that to my postworkout shake. i usually just drink some Hi C, but would like to try dextrose.
    im 5'9" and about 155 lbs. just curious on what kind of dose i should be taking and is it really that imperative to get the maltodexrin too? i mean it does not ellicit as high of an insulin spike as dextrose does. and i generally eat some simple carbs about 45 minutes after i workout anywas, so i think that would continue to provide the carbs i need.

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    Not to flame but have you tried searching? Like you said there are numerous posts about it, why not come up with a plan and check that with the guys. You know your body better than we do.

    Or ask bobo about hi gi carbs post work out, he'll help you quick hehehe
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    Ask bobo............LOL

    30-50 grams of dextrose and/or maltodextrin is ideal IMO.
    (....of course LBW would factor into exact amounts)

    Maltodextrin has a higher GI and will illicit a slightly higher insulin response.

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    Originally posted by dr.mattdogg
    is it really that imperative to get the maltodexrin too?
    nope
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    yeah i guess i was wrong about the dextrose having a higher GI, its been a whiles since ive lookin into this. guess ill go with 30-50 g of the dextrose, thanks.
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    currently I am on a mass program and I use 50g whey and 100g dextrose, I am 164.5lbs, started at 160lbs about 4 weeks ago, extremely clean mass program, taking in about 3000 cal a day, I recover MUCH better when taking the higher amounts of dextrose. My diet is all about timed nutrition, I eat according to activity to minimize fat gain
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    Originally posted by goes4ever
    currently I am on a mass program and I use 50g whey and 100g dextrose,

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    Originally posted by goes4ever
    currently I am on a mass program and I use 50g whey and 100g dextrose, I am 164.5lbs
    i find that way too much (both protein and carbs). at your current weight, 30g's protein and 55-60 dextrose plenty. Sage
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    Originally posted by sage


    i find that way too much (both protein and carbs). at your current weight, 30g's protein and 55-60 dextrose plenty. Sage
    I think SwoleCat would disagree.
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    Originally posted by sage


    i find that way too much (both protein and carbs). at your current weight, 30g's protein and 55-60 dextrose plenty. Sage
    well at that dose you stated, I just could not gain or properly recover, I am working with swolecat and I am on swoledup, when I was cutting my bodyfat down before I started a bulk, I was using 50-60 dextrose and 35-40 whey, and I was on a cut diet, dropping fat like crazy, My body has never responded before to anything, and the plan swolecat made up for me is the 1st thing that has EVER worked, so I'm sticking to it!
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    Originally posted by Nelson


    I think SwoleCat would disagree.
    I think science would disagree with Swolecat.
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    Originally posted by goes4ever


    well at that dose you stated, I just could not gain or properly recover, I am working with swolecat and I am on swoledup, when I was cutting my bodyfat down before I started a bulk, I was using 50-60 dextrose and 35-40 whey, and I was on a cut diet, dropping fat like crazy, My body has never responded before to anything, and the plan swolecat made up for me is the 1st thing that has EVER worked, so I'm sticking to it!

    Tell me where 100g of dextrose and rpaid glycogen replenishment has anything to do the the rate at which synthesis occurs. Because it you can't, I will show you why its not needed. Actually if you did a search you could find out.

    You basically taking Cell-Tech without the creatine.
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    Originally posted by Bobo



    Tell me where 100g of dextrose and rpaid glycogen replenishment has anything to do the the rate at which synthesis occurs. Because it you can't, I will show you why its not needed. Actually if you did a search you could find out.

    You basically taking Cell-Tech without the creatine.
    The insulin response is what is helpful in this case. You are correct that there is little evidence to support much synthesis because if increased insulin levels. It does inhibit protein breakdown post work out, which is very nice.
    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.

    -------------------------------------


    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.


    -------------------------------------


    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.


    -------------------------------------


    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.

    Stolen fro hhajdo.

    That said I agree that 100g of dextrose is quite excessive. It would seem a mix of fast/medium/slow digesting carbs would be best to take full advantage of natural insulin and MUCH easier on the pancrase. I can see 100g dextrose being quite hard on the natural production of insulin.

    Glad it is working for you brother, perhaps its the placebo effect of working harder because you've paid for the help instead of doing it yourself. Either way if your happy run with it and hope you don't become diabetic
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    Originally posted by elijah_123


    The insulin response is what is helpful in this case. You are correct that there is little evidence to support much synthesis because if increased insulin levels. It does inhibit protein breakdown post work out, which is very nice.
    That said I agree that 100g of dextrose is quite excessive. It would seem a mix of fast/medium/slow digesting carbs would be best to take full advantage of natural insulin and MUCH easier on the pancrase. I can see 100g dextrose being quite hard on the natural production of insulin.

    Glad it is working for you brother, perhaps its the placebo effect of working harder because you've paid for the help instead of doing it yourself. Either way if your happy run with it and hope you don't become diabetic

    Glycogen replenishemnt is biphasic and is insulin independent during the first phase (30-60 minutes). Excess amounts are not needed at all and can contribute to excess glucose circulating.

    Determinants of post-exercise glycogen synthesis during short-term recovery.

    Jentjens R, Jeukendrup A.

    Human Performance Laboratory, School of Sport and Exercise Sciences, University of Birmingham, Edgbaston, Birmingham, UK.

    The pattern of muscle glycogen synthesis following glycogen-depleting exercise occurs in two phases. Initially, there is a period of rapid synthesis of muscle glycogen that does not require the presence of insulin and lasts about 30-60 minutes. This rapid phase of muscle glycogen synthesis is characterised by an exercise-induced translocation of glucose transporter carrier protein-4 to the cell surface, leading to an increased permeability of the muscle membrane to glucose. Following this rapid phase of glycogen synthesis, muscle glycogen synthesis occurs at a much slower rate and this phase can last for several hours. Both muscle contraction and insulin have been shown to increase the activity of glycogen synthase, the rate-limiting enzyme in glycogen synthesis. Furthermore, it has been shown that muscle glycogen concentration is a potent regulator of glycogen synthase. Low muscle glycogen concentrations following exercise are associated with an increased rate of glucose transport and an increased capacity to convert glucose into glycogen.The highest muscle glycogen synthesis rates have been reported when large amounts of carbohydrate (1.0-1.85 g/kg/h) are consumed immediately post-exercise and at 15-60 minute intervals thereafter, for up to 5 hours post-exercise. When carbohydrate ingestion is delayed by several hours, this may lead to ~50% lower rates of muscle glycogen synthesis. The addition of certain amino acids and/or proteins to a carbohydrate supplement can increase muscle glycogen synthesis rates, most probably because of an enhanced insulin response. However, when carbohydrate intake is high (&gt;/=1.2 g/kg/h) and provided at regular intervals, a further increase in insulin concentrations by additional supplementation of protein and/or amino acids does not further increase the rate of muscle glycogen synthesis. Thus, when carbohydrate intake is insufficient (&lt;1.2 g/kg/h), the addition of certain amino acids and/or proteins may be beneficial for muscle glycogen synthesis. Furthermore, ingestion of insulinotropic protein and/or amino acid mixtures might stimulate post-exercise net muscle protein anabolism. Suggestions have been made that carbohydrate availability is the main limiting factor for glycogen synthesis. A large part of the ingested glucose that enters the bloodstream appears to be extracted by tissues other than the exercise muscle (i.e. liver, other muscle groups or fat tissue) and may therefore limit the amount of glucose available to maximise muscle glycogen synthesis rates. Furthermore, intestinal glucose absorption may also be a rate-limiting factor for muscle glycogen synthesis when large quantities (&gt;1 g/min) of glucose are ingested following exercise.

    I'd don't see a reason for any High Gi carbs post exercise if:

    1. The first phase is insulin independemnt

    2. The insulin dependent phase is a slow release.
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    Regulation of GLUT4 protein and glycogen synthase during muscle glycogen synthesis after exercise.

    Ivy JL, Kuo CH.

    Department of Kinesiology, The University of Texas at Austin, 78712, USA.

    The pattern of muscle glycogen synthesis following its depletion by exercise is biphasic. Initially, there is a rapid, insulin independent increase in the muscle glycogen stores. This is then followed by a slower insulin dependent rate of synthesis. Contributing to the rapid phase of glycogen synthesis is an increase in muscle cell membrane permeability to glucose, which serves to increase the intracellular concentration of glucose-6-phosphate (G6P) and activate glycogen synthase. Stimulation of glucose transport by muscle contraction as well as insulin is largely mediated by translocation of the glucose transporter isoform GLUT4 from intracellular sites to the plasma membrane. Thus, the increase in membrane permeability to glucose following exercise most likely reflects an increase in GLUT4 protein associated with the plasma membrane. This insulin-like effect on muscle glucose transport induced by muscle contraction, however, reverses rapidly after exercise is stopped. As this direct effect on transport is lost, it is replaced by a marked increase in the sensitivity of muscle glucose transport and glycogen synthesis to insulin. Thus, the second phase of glycogen synthesis appears to be related to an increased muscle insulin sensitivity. Although the cellular modifications responsible for the increase in insulin sensitivity are unknown, it apparently helps maintain an increased number of GLUT4 transporters associated with the plasma membrane once the contraction-stimulated effect on translocation has reversed. It is also possible that an increase in GLUT4 protein expression plays a role during the insulin dependent phase.


    Comparison of carbohydrate and milk-based beverages on muscle damage and glycogen following exercise.

    Wojcik JR, Walber-Rankin J, Smith LL, Gwazdauskas FC.

    Department of Human Nutrition, Foods, and Exercise at Virginia Polytechnic Institute and State University, Blacksburg 24061, USA.

    This study examined effects of carbohydrate (CHO), milk-based carbohydrate-protein (CHO-PRO), or placebo (P) beverages on glycogen resynthesis, muscle damage, inflammation, and muscle function following eccentric resistance exercise. Untrained males performed a cycling exercise to reduce muscle glycogen 12 hours prior to performance of 100 eccentric quadriceps contractions at 120% of 1-RM (day 1) and drank CHO (n = 8), CHO-PRO (n = 9; 5 kcal/kg), or P (n = 9) immediately and 2 hours post-exercise. At 3 hours post-eccentric exercise, serum insulin was four times higher for CHO-PRO and CHO than P (p < .05). Serum creatine kinase (CK) increased for all groups in the 6 hours post-eccentric exercise (p < .01), with the increase tending to be lowest for CHO-PRO (p < .08) during this period. Glycogen was low post-exercise (33+/-3.7 mmol/kg ww), increased 225% at 24 hours, and tripled by 72 hours, with no group differences. The eccentric exercise increased muscle protein breakdown as indicated by urinary 3-methylhistidine and increased IL-6 with no effect of beverage. Quadriceps isokinetic peak torque was depressed similarly for all groups by 24% 24 hours post-exercise and remained 21% lower at 72 hours (p < .01). In summary, there were no influences of any post-exercise beverage on muscle glycogen replacement, inflammation, or muscle function.



    Carbohydrate nutrition before, during, and after exercise.

    Costill DL.

    The role of dietary carbohydrates (CHO) in the resynthesis of muscle and liver glycogen after prolonged, exhaustive exercise has been clearly demonstrated. The mechanisms responsible for optimal glycogen storage are linked to the activation of glycogen synthetase by depletion of glycogen and the subsequent intake of CHO. Although diets rich in CHO may increase the muscle glycogen stores and enhance endurance exercise performance when consumed in the days before the activity, they also increase the rate of CHO oxidation and the use of muscle glycogen. When consumed in the last hour before exercise, the insulin stimulated-uptake of glucose from blood often results in hypoglycemia, greater dependence on muscle glycogen, and an earlier onset of exhaustion than when no CHO is fed. Ingesting CHO during exercise appears to be of minimal value to performance except in events lasting 2 h or longer. The form of CHO (i.e., glucose, fructose, sucrose) ingested may produce different blood glucose and insulin responses, but the rate of muscle glycogen resynthesis is about the same regardless of the structure.


    Effect of different types of high carbohydrate diets on glycogen metabolism in liver and skeletal muscle of endurance-trained rats.

    Garrido G, Guzman M, Odriozola JM.

    Department of Human Performance, National Institute of Physical Education, Madrid, Spain.

    Male Wistar rats were fed ad libitum four different diets containing fructose, sucrose, maltodextrins or starch as the source of carbohydrate (CH). One group was subjected to moderate physical training on a motor-driven treadmill for 10 weeks (trained rats). A second group received no training and acted as a control (sedentary rats). Glycogen metabolism was studied in the liver and skeletal muscle of these animals. In the sedentary rats, liver glycogen concentrations increased by 60%-90% with the administration of simple CH diets compared with complex CH diets, whereas skeletal muscle glycogen stores were not significantly affected by the diet. Physical training induced a marked decrease in the glycogen content in liver (20%-30% of the sedentary rats) and skeletal muscle (50%-80% of the sedentary rats) in animals fed simple (but not complex) CH diets. In liver this was accompanied by a two-fold increase of triacylglycerol concentrations. Compared with simple CH diets, complex CH feeding increased by 50%-150% glycogen synthase (GS) activity in liver, whereas only a slight increase in GS activity was observed in skeletal muscle. In all the animal groups, a direct relationship existed between tissue glucose 6-phosphate concentration and glycogen content (r = 0.9911 in liver, r = 0.7177 in skeletal muscle). In contrast, no relationship was evident between glycogen concentrations and either glycogen phosphorylase activity or adenosine 5'-monophosphate tissue concentration. The results from this study thus suggest that for trained rats diets containing complex CH (compared with diets containing simple CH) improve the glycogenic capacity of liver and skeletal muscle, thus enabling the adequate regeneration of glycogen stores in these two tissues.


    Simple and complex carbohydrate-rich diets and muscle glycogen content of marathon runners.

    Roberts KM, Noble EG, Hayden DB, Taylor AW.

    Faculty of Physical Education, University of Western Ontario, London, Canada.

    The effects of simple-carbohydrate (CHO)- and complex-CHO-rich diets on skeletal muscle glycogen content were compared. Twenty male marathon runners were divided into four equal groups with reference to dietary consumption: depletion/simple, depletion/complex, nondepletion/simple, and nondepletion/complex. Subjects consumed either a low-CHO (15% energy [E] intake), or a mixed diet (50% CHO) for 3 days, immediately followed by a high-CHO diet (70% E intake) predominant in either simple-CHO or in complex-CHO (85% of total CHO intake) for another 3 days. Skeletal muscle biopsies and venous blood samples were obtained one day prior to the start of the low-CHO diet or mixed diet (PRE), and then again one day after the completion of the high-CHO diet (POST). The samples were analysed for skeletal muscle glycogen, serum free fatty acids (FFA), insulin, and lactate and blood glucose. Skeletal muscle glycogen content increased significantly (p less than 0.05) only in the nondepletion/simple group. When groups were combined, according to the type of CHO ingested and/or utilization of a depletion diet, significant increases were observed in glycogen content. Serum FFA decreased significantly (p less than 0.05) for the nondepletion/complex group only, while serum insulin, blood glucose, and serum lactate were not altered. It is concluded that significant increases in skeletal muscle glycogen content can be achieved with a diet high in simple-CHO or complex-CHO, with or without initial consumption of a low-CHO diet.




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    I agree with you completely about the synthesis bobo. I was only pointing the role insulin plays in preventing muscle degredation.

    This snippets supports both of us (sorry I forgot to bold them in my post):

    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)....


    We conclude that: (a) hyperaminoacidemia specifically stimulates muscle protein synthesis; (b) insulin, even with hyperaminoacidemia, improves muscle protein balance solely by inhibiting proteolysis;

    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.

    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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    Amino acids regulate skeletal muscle PHAS-I and p70 S6-kinase phosphorylation independently of insulin. Long, W., L. Saffer, L. Wei, and E. J. Barrett. Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
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    APStracts 7:0077E, 2000.
    --------------------------------------------------------------------------------
    Refeeding reverses the muscle protein loss seen with fasting. The physiological regulators and cellular control sites responsible for this reversal are incompletely defined. Phosphorylation of phosphorylated heat-acid stabled protein (PHAS-I) frees eukaryotic initiation factor 4E (eIF4E) and stimulates protein synthesis by accelerating translation initiation. Phosphorylation of p70 S6-kinase (p70S6k) is thought to be involved in the regulation of the synthesis of some ribosomsal proteins and other selected proteins with polypyrimidine clusters near the transcription start site. We examined whether phosphorylation of PHAS-I and p70S6k was increased by feeding and determined the separate effects of insulin and amino acids on PHAS-I and p70S6k phosphorylation in rat skeletal muscle in vivo. Muscle was obtained from rats fed ad libitum or fasted overnight (n = 5 each). Other fasted rats were infused with insulin (3 muU×min«minus»1×kg«minus»1, euglycemic clamp), amino acids, or the two combined. Gastrocnemius was freeze-clamped, and PHAS-I and p70S6k phosphorylation was measured by quantifying the several phosphorylated forms of these proteins seen on Western blots. We observed that feeding increased phosphorylation of both PHAS-I and p70S6k (P < 0.05). Infusion of amino acids alone reproduced the effect of feeding. Physiological hyperinsulinemia increased p70S6K (P < 0.05) but not PHAS-I phosphorylation (P = 0.98). Addition of insulin to amino acid infusion was no more effective than amino acids alone in promoting PHAS-I and p70S6k phosphorylation. We conclude that amino acid infusion alone enhances the activation of the protein synthetic pathways in vivo in rat skeletal muscle. This effect is not dependent on increases in plasma insulin and simulates the activation of protein synthesis that accompanies normal feeding.

    Physiological hyperinsulinemia stimulates p70(S6k) phosphorylation in human skeletal muscle.

    Hillier T, Long W, Jahn L, Wei L, Barrett EJ.

    Department of Internal Medicine, Division of Endocrinology, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA.

    Using tracer methods, insulin stimulates muscle protein synthesis in vitro, an effect not seen in vivo with physiological insulin concentrations in adult animals or humans. To examine the action of physiological hyperinsulinemia on protein synthesis using a tracer-independent method in vivo and identify possible explanations for this discrepancy, we measured the phosphorylation of ribosomal protein S6 kinase (P70(S6k)) and eIF4E-binding protein (eIF4E-BP1), two key proteins that regulate messenger ribonucleic acid translation and protein synthesis. Postabsorptive healthy adults received either a 2-h insulin infusion (1 mU/min.kg; euglycemic insulin clamp; n = 6) or a 2-h saline infusion (n = 5). Vastus lateralis muscle was biopsied at baseline and at the end of the infusion period. Phosphorylation of P70(S6k) and eIF4E-BP1 was quantified on Western blots after SDS-PAGE. Physiological increments in plasma insulin (42 +/- 13 to 366 +/- 36 pmol/L; P: = 0.0002) significantly increased p70(S6k) (P: < 0.01), but did not affect eIF4E-BP1 phosphorylation in muscle. Plasma insulin declined slightly during saline infusion (P: = 0.04), and there was no change in the phosphorylation of either p70(S6k) or eIF4E-BP1. These findings indicate an important role of physiological hyperinsulinemia in the regulation of p70(S6k) in human muscle. This finding is consistent with a potential role for insulin in regulating the synthesis of that subset of proteins involved in ribosomal function. The failure to enhance the phosphorylation of eIF4E-BP1 may in part explain the lack of a stimulatory effect of physiological hyperinsulinemia on bulk protein synthesis in skeletal muscle in vivo.

    More evidence
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    Originally posted by Bobo


    I think science would disagree with Swolecat.
    Science isn`t always right.
    This has been proved time & time again.
    For every study in support of your view, there is another against it.
    We could go back & forth posting studies forever.
    I`m not saying you`re wrong & SwoleCat is right, but maybe both methods have their place in a given diet & training regime.
    I can`t go into the specifics of SwoleCat`s diets.
    But maybe if you knew how meals are timed on SwoleGenix or SwoledUp, the macronutrients of those meals, & other factors such as supplements, cardio & workouts you may be in a better position to understand the reason why goes4ever & others are consuming that much dextrose in their post-workout shakes.
    I guess what I`m trying to say is, when you can see the
    whole picture you`re in a better position to be able to see it how it all works.
  19. I am faster than 80% of all snakes
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    Originally posted by Nelson


    Science isn`t always right.
    This has been proved time &amp; time again.
    For every study in support of your view, there is another against it.
    We could go back &amp; forth posting studies forever.
    I`m not saying you`re wrong &amp; SwoleCat is right, but maybe both methods have their place in a given diet &amp; training regime.
    I can`t go into the specifics of SwoleCat`s diets.
    But maybe if you knew how meals are timed on SwoleGenix or SwoledUp, the macronutrients of those meals, &amp; other factors such as supplements, cardio &amp; workouts you may be in a better position to understand the reason why goes4ever &amp; others are consuming that much dextrose in their post-workout shakes.
    I guess what I`m trying to say is, when you can see the
    whole picture you`re in a better position to be able to see it how it all works.
    Nobody said his methods won't work. I'm just saying their is a wiser and better choice supported by case studies and real world results withouth spending money on information that is easily obtained. Ask around and those who have switched see the SAME gains WITHOUT the extra fat that will build up over time. They bought into the whole high GI myths the supp companies have been throwing down your throats for years. 100g of dextrose is NOT healthy at all in the long run and will lead to insulin resistance over time. That has been proven.

    I've seen the big picture and understand what his diet is about. Its nothing new or revolutionary and those that think it is are gravely mistaken. Will it work? Sure it will but when you look at ALL the facts, studies, and real world results there are better options that won't cost you money. If people actually took the time and researched nutrition they wouldn't spend time defending a diet they spent $200 on.
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  20. I am faster than 80% of all snakes
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    Originally posted by Nelson


    Science isn`t always right.
    This has been proved time &amp; time again.
    For every study in support of your view, there is another against it.
    Then would someone post them because I would really like to see how 100g of dextrose leads to increased synthesis rates. Provide one study. I bet you can't because there isnt any yet people follow this theory like its written in stone because someone sells it for $200. Maybe I should do the same because I would make a whole lot of money on people that don't understand nutrition.


    Now I know how Cell-Tech is the #1 seller. At least that has creatine and ALA...
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    I'm no scientist but that much sugar is not good for ME. I gain fat like no other. I keep it simple I drink LAVA from universal 32 carbs,32protein ,5creatine,3glutamine,2taurine . All in gram levels of course I am not saying it is perfect just works for me. To much sugar and I just feel like ass. Plus in the long haul it can't be that healthy.
    Just my opinion though.
  22. I am faster than 80% of all snakes
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    Good opinion!
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    Thank you
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