Dextrose PWO Bad? read

[dannyboyo]

Post Workout Insulin

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okay basically i'm going to lay down a whole load of quoted stuff some with sources, some without

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"There are some instances, however, where a food has a low glycemic value but a high insulin index value. This applies to dairy foods and to some highly palatable energy-dense "indulgence foods." Some foods (such as meat, fish, and eggs) that contain no carbohydrate, just protein and fat (and essentially have a GI value of zero), still stimulate significant rises in blood insulin."

The New Glucose Revolution (New York: Marlowe and Company, 2003, pages 57-58

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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.

Publication Types:
Review
Review, Tutorial

PMID: 9578375 [PubMed - indexed for MEDLINE]

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Dietary strategies to promote glycogen synthesis after exercise.

Ivy JL.

Exercise Physiology and Metabolism Laboratory, Department of Kinesiology and Health Education, The University of Texas at Austin, Austin, TX, USA.

Muscle glycogen is an essential fuel for prolonged intense exercise, and therefore it is important that the glycogen stores be copious for competition and strenuous training regimens. While early research focused on means of increasing the muscle glycogen stores in preparation for competition and its day-to-day replenishment, recent research has focused on the most effective means of promoting its replenishment during the early hours of recovery. It has been observed that muscle glycogen synthesis is twice as rapid if carbohydrate is consumed immediately after exercise as opposed to waiting several hours, and that a rapid rate of synthesis can be maintained if carbohydrate is consumed on a regular basis. For example, supplementing at 30-min intervals at a rate of 1.2 to 1.5 g CHO x kg(-1) body wt x h(-1) appears to maximize synthesis for a period of 4- to 5-h post exercise. If a lighter carbohydrate supplement is desired, however, glycogen synthesis can be enhanced with the addition of protein and certain amino acids. Furthermore, the combination of carbohydrate and protein has the added benefit of stimulating amino acid transport, protein synthesis and muscle tissue repair. Research suggests that aerobic performance following recovery is related to the degree of muscle glycogen replenishment.

Publication Types:
Review
Review, Tutorial

PMID: 11897899 [PubMed - indexed for MEDLINE]

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Amino acids stimulate translation initiation and protein synthesis through an Akt-independent pathway in human skeletal muscle.

Liu Z, Jahn LA, Wei L, Long W, Barrett EJ.

Division of Endocrinology and Metabolism, Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908, USA. zl3e@virginia.edu

Studies in vitro as well as in vivo in rodents have suggested that amino acids (AA) not only serve as substrates for protein synthesis, but also as nutrient signals to enhance mRNA translation and protein synthesis in skeletal muscle. However, the physiological relevance of these findings to normal humans is uncertain. To examine whether AA regulate the protein synthetic apparatus in human skeletal muscle, we infused an AA mixture (10% Travesol) systemically into 10 young healthy male volunteers for 6 h. Forearm muscle protein synthesis and degradation (phenylalanine tracer method) and the phosphorylation of protein kinase B (or Akt), eukaryotic initiation factor 4E-binding protein 1, and ribosomal protein S6 kinase (p70(S6K)) in vastus lateralis muscle were measured before and after AA infusion. We also examined whether AA affect urinary nitrogen excretion and whole body protein turnover. Postabsorptively all subjects had negative forearm phenylalanine balances. AA infusion significantly improved the net phenylalanine balance at both 3 h (P < 0.002) and 6 h (P < 0.02). This improvement in phenylalanine balance was solely from increased protein synthesis (P = 0.02 at 3 h and P < 0.003 at 6 h), as protein degradation was not changed. AA also significantly decreased whole body phenylalanine flux (P < 0.004). AA did not activate Akt phosphorylation at Ser(473), but significantly increased the phosphorylation of both eukaryotic initiation factor 4E-binding protein 1 (P < 0.04) and p70(S6K) (P < 0.001). We conclude that AA act directly as nutrient signals to stimulate protein synthesis through Akt-independent activation of the protein synthetic apparatus in human skeletal muscle.

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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 (>/=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 (<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

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Scientists Close In On Trigger Of Insulin Resistance

Extra sugar can cause insulin resistance in cells. Now scientists have an explanation.

In experiments with fat cells, Johns Hopkins scientists have discovered direct evidence that a build-up of sugar on proteins triggers insulin resistance, a key feature of most cases of diabetes.
The results underscore the importance of glycosylation - attachment of a sugar to a protein -- as a way cells control proteins' activities, the scientists report in the April 16 issue of the Proceedings of the National Academy of Sciences. The scientists found that at least two proteins involved in passing along insulin's message were unlikely to work properly when coated in extra sugar.

Type 2 diabetes, the most common form in adults, occurs when muscle, fat and other tissues stop responding to insulin's signals to mop up sugar from the blood. The resulting high blood sugar, if uncontrolled, can lead to blindness, amputation and death. Understanding sugar's precise influence on insulin's activity may help improve treatment and prevention, scientists hope.

"Cells don't respond to insulin itself. Instead, a whole cascade of events, set in motion by insulin, eventually causes cells to take in sugar," explains Gerald Hart, Ph.D., professor and director of biological chemistry in the school's Institute for Basic Biomedical Sciences. "We now have an explanation of how sugar can affect these signals, and even a hypothesis for how high blood sugar could cause tissue damage in diabetes -- by improperly modifying proteins."

Hart's lab discovered 18 years ago that sugar is used routinely inside cells to modify proteins, turning them on and off. The more commonly known protein-controller, phosphate, actually binds to some of the same building blocks of proteins as sugar does. If proteins have too many sugars on them, they can't be controlled properly by the cell and are unlikely to work correctly, suggests Hart.

"We think we've come across a major mechanistic reason for insulin resistance," says Hart. "These cells developed insulin resistance simply because their proteins, and specific proteins in fact, had more than the normal number of sugar tags."

If key proteins laden with sugar are present in patients with diabetes, the findings may provide a target for developing new strategies to deal with this growing public health threat, says Hart. While diabetes can be fairly well controlled by diet and carefully monitoring one's blood sugar levels, finding a way to remove extra sugar tags may help treat or prevent diabetes someday, the researchers suggest.

"Textbooks frequently and incorrectly show glycosylation only happening to proteins on the cell surface," says Hart. "Complex sugars are added only to proteins outside the cell, but simple sugars are used all the time in the nucleus and cytoplasm to modify proteins. It's this glycosylation that happens inside the cell, involving simple sugars, that is the key in insulin resistance."

The "simple sugar" to which he refers is O-linked beta-N-acetylglucosamine, a complex name that condenses to a difficult acronym -- O-GlcNAc -- with an ugly pronunciation -- "oh-gluck-nack." But in many ways, O-GlcNAc is a beautiful and mysterious thing, says Hart.

"O-GlcNAc is a modifier on many proteins, but if you didn't know to look for it, you'd never find it," he says. "Instruments and the usual laboratory methods have a hard time measuring it, so we developed the techniques to detect it."

O-GlcNAc is added to proteins by one enzyme and removed from proteins by another. By selectively blocking that removal, the scientists hoped to load up proteins with sugar without adding extra sugar (the way other scientists have created insulin resistance). "We wanted to see the effect of glycosylation itself, so we used a molecular sledgehammer to increase the amount of sugar bound to proteins," says Hart, whose lab proved the ability of the blocker, a molecule called PUGNAc.

Not only did the blocker increase the amount of O-GlcNAc bound to proteins, but that increase caused the cells to stop responding to insulin, say co-first authors and postdoctoral fellows Lance Wells and Keith Vosseller.

Looking for proteins in the insulin-signaling pathway that were more glycosylated than normal, Vosseller and Wells found two: beta-catenin and insulin receptor substrate-1 (IRS-1). The crucial role these proteins play in passing along insulin's messages is likely to be adversely affected by the extra sugars they carry, the researchers say.

"Our experiments show that increasing O-GlcNAc on proteins is, by itself, a cause of insulin resistance, rather than an effect or a coincidence," says Vosseller.

In the body, sugar (glucose) is changed into glucosamine, which is changed into O-GlcNAc. Other scientists have shown that giving cells or animals excessive amounts of sugar or glucosamine, along with extra insulin, leads to insulin resistance. The new findings provide an explanation for others' experience with animal and laboratory models of insulin resistance.

There has been little study of glucosamine, a commonly used dietary supplement, in people. It is suggested that people taking glucosamine consult their doctors if they are concerned about the possibility of increasing their risk of developing diabetes.

Funding was provided by grants and National Research Service Awards from the National Institutes of Health. Professor of biological chemistry Daniel Lane, Ph.D., is also an author.

Under a licensing agreement between Covance Research Products and The Johns Hopkins University, Hart is entitled to a share of royalty received by the university on sales of the antibody used to detect O-GlcNAc on proteins. The terms of this arrangement are being managed by The Johns Hopkins University in accordance with its conflict of interest policies.

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I think the reason why everyone consumes high GI carbs post workout is to replenish their muscle glycogen levels and to combat the insulin level post workout. U have a small window of opportunity post workout when your body is most primed to absorb nutrients. I think worrying about consuming high vs. low GI carbs post workout is rather trivial. To simplfy it (for those of U unfamiliar) glycogen is in muscle and glucose floats around in the blood (at a very small amount). The glycogen only lasts about 10 min, so like AT said, you should be more concerned about pre-workout complex carbs IMO. They would be much more beneficial.

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Also people think the faster you replenish glycogen stores the faster rate of synthesis will occur and thats just not true.

The oatmeal is not even for the first phase of glycogen replenishment because that phase is insulin independent. It's more for the second insulin dependent stage which is much more prolonged.

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exercise in itself makes you extremely insulin sensitive therefore just about any form of carb will immedietly be put to use

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Catabolism post workout is highly exaggerated. ANY insulin response stops any form of catabolism not to mention GH secretions last up to 60 minutes post exercise.

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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.

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This is where your wrong. Speed is not the key, in terms of glucose. THere is no evidence sating that increased glycogen storage equals a greater rate of synthesis. In fact it states the oppisite in that you can have a large quick spike or a slower spike and the rate stays the same. Its aminos that are the trigger and key to increased rate of synthesis, not insulin.

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Since exercise alone increases a cell's sensitivity to insulin, dextrose isn't neccessary to replace glycogen. Glycogen can be restored via other methods. You've increased insulin sensitivity already via anaerobic exercise; you are increasing the possibility for spillage by introducing dextrose/malto......the rate of glycogen restoration isn't the same as the rate of protein synthesis.

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Conventional thinking helped by numerous marketing ads tell us we need to replenish glycogen as fast as we can and we need to creat a large spike to accomplish this. They are totally wrong. They have zero studies supporting this. The studies they use say there is a greater glycogen replenishent (which DOES NOT increase the RATE)with high GI and that is it. They conclude in no way that the rate of protein synthesis is increased and just recently studies have shown that aminos, NOT insulin, are what triggers protein synthesis. The point is that a large spike, or faster spike, is NOT needed.

Exercise induces sensitivity meaning that a lower GI carb will have a more pronounced insulin spike [than normal] BECAUSE of the sensitivity. A high GI source will have the same effect. Since there is an insulin INDEPENDENT stage and studies clearly show that not all glucose is being utlilized by the exercise (study clearly states that as well) the need for such a large spike is not needed. Insulin, even hyperinsulinemia, post exercise does not cause a significant increase in protein synthesis (study clearly states).

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High G.I. carbs work great and most of what Berardi says is correct. But what he may not understand himself (as he is a writer first and a lifter second), is that low G.I. is the better choice, accomplishing the same goal (anabolism) while leaving rollercoaster ride of up and down blood sugar levels in the past. With a pre-workout meal, steak, chicken, whey protein shake, etc combined with about 50 gms of carbs (oatmeal, sweet potato, etc) your muscles will be supplied with a constant supply of aminos throughout the workout, and will not be "screaming" for a protein fix by workout's end. Thus there is just NO NEED for a huge and dramatic insulin spike here.

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there is no need to spike insulin when glycogen synthesis can occur without it

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Signalling to glucose transport in skeletal muscle during exercise.

Exercise-induced glucose uptake in skeletal muscle is mediated by an insulin-independent mechanism. Although the signalling events that increase glucose transport in response to muscle contraction are not fully elucidated, the aim of the present review is to briefly present the current understanding of the molecular signalling mechanisms involved. Glucose uptake may be regulated by Ca++-sensitive contraction-related mechanisms possibly involving protein kinase C, and by mechanisms that reflect the metabolic status of the muscle and may involve the AMP-activated protein kinase. Furthermore the p38 mitogen activated protein kinase may be involved. Still, the picture is incomplete and a substantial part of the exercise/contraction-induced signalling mechanism to glucose transport remains unknown."

http://www4.infotrieve.com/newmedli...ptake&count=713

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ANY insulin spike eliminates cortisol. It doesn't have to be a big one. Your body is highly responsive to any nutrient taken post workout. Do you think your body sits there and thinks whether it should release insulin or not? Do you think a low GI sources will not produce an insulin response?

[dannyboyo]

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 &lt; .05). Serum creatine kinase (CK) increased for all groups in the 6 hours post-eccentric exercise (p &lt; .01), with the increase tending to be lowest for CHO-PRO (p &lt; .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 &lt; .01). In summary, there were no influences of any post-exercise beverage on muscle glycogen replacement, inflammation, or muscle function.

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Type and timing of protein feeding to optimize anabolism.

Mosoni L, Mirand PP.

PURPOSE OF REVIEW

The delivery rate of amino acids to an organism significantly affects protein anabolism. The rate can be controlled by the type and the timing of feeding. Our aim was to bring new insights to the way they may act.

RECENT FINDINGS

During young and adult ages, when food supply is liberal, subjects can adapt to various modes of protein feeding. However, during food restriction, protein anabolism is favored when the delivery of amino acids is evenly distributed over the day, either with frequent meals, or through the use of slowly absorbed proteins like casein. In contrast, during aging, quickly absorbed protein sources become more efficient. During recovery after exercise, the timing of protein feeding after the end of exercise may or may not influence its anabolic effect, depending on the subject's age and the type of exercise.

SUMMARY

The synchronization of variations in anabolic capability with amino acid supply partly explains the effects of the type and timing of protein feeding. This effect is modulated by the amount of amino acids required to increase whole-body proteins and by the signaling properties of some amino acids to stimulate protein synthesis. Indeed, the anabolic effect of amino acids is determined by their interaction with other anabolic factors (other nutrients or physiological factors, whose efficiency is mainly related to their effect on protein degradation). It is clear that benefits can be obtained from adapted protein feeding patterns.

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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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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.
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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 &lt; 0.05). Infusion of amino acids alone reproduced the effect of feeding. Physiological hyperinsulinemia increased p70S6K (P &lt; 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.

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The use of High GI would be extremely helpful in endurance type training since the object is to fill glycogen stores (both muscle and liver) to account for the energy expenditure that will follow. With resistance training there is no further energy expenditure that will deplete glyocgen stores further so the need for such drastic spikes and quick replenishment is not needed. People also say that you must refill stores quickly to eliminate catabolism. Well GH is produced at high levels well after (50-60minutes) after exercise is completed so the whole catabolism is overrated. It's important but overrated.

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People keep thinking I'm anti-insulin but that would be nuts. I just prefer a more stable release that will coincided with both phases (if it even needed in phase 1) There has been no evidence that a high SPIKE in insulin increases the rate of synthesis. It just increases the glycogen storage quicker.

Amino acids stimulate translation initiation and protein synthesis through an Akt-independent pathway in human skeletal muscle.

Liu Z, Jahn LA, Wei L, Long W, Barrett EJ.

Division of Endocrinology and Metabolism, Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908, USA. zl3e@virginia.edu

Studies in vitro as well as in vivo in rodents have suggested that amino acids (AA) not only serve as substrates for protein synthesis, but also as nutrient signals to enhance mRNA translation and protein synthesis in skeletal muscle. However, the physiological relevance of these findings to normal humans is uncertain. To examine whether AA regulate the protein synthetic apparatus in human skeletal muscle, we infused an AA mixture (10% Travesol) systemically into 10 young healthy male volunteers for 6 h. Forearm muscle protein synthesis and degradation (phenylalanine tracer method) and the phosphorylation of protein kinase B (or Akt), eukaryotic initiation factor 4E-binding protein 1, and ribosomal protein S6 kinase (p70(S6K)) in vastus lateralis muscle were measured before and after AA infusion. We also examined whether AA affect urinary nitrogen excretion and whole body protein turnover. Postabsorptively all subjects had negative forearm phenylalanine balances. AA infusion significantly improved the net phenylalanine balance at both 3 h (P &lt; 0.002) and 6 h (P &lt; 0.02). This improvement in phenylalanine balance was solely from increased protein synthesis (P = 0.02 at 3 h and P &lt; 0.003 at 6 h), as protein degradation was not changed. AA also significantly decreased whole body phenylalanine flux (P &lt; 0.004). AA did not activate Akt phosphorylation at Ser(473), but significantly increased the phosphorylation of both eukaryotic initiation factor 4E-binding protein 1 (P &lt; 0.04) and p70(S6K) (P &lt; 0.001). We conclude that AA act directly as nutrient signals to stimulate protein synthesis through Akt-independent activation of the protein synthetic apparatus in human skeletal muscle.

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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.

So what does that mean?
You do NOT need an insulin spike to get the ball rolling, there IS a chance of fat deposition and the rate of absorbtion of High GI carbs may well be limited by the intentine such that a low GI would (and does) work equally as well for MOST people.
Also, the guys that are taking huge amounts of high GI hoping to induce a large insulin spike are just kidding themselves as the intestinal glucose absorption rates will ensure most of it is going to waste.

The arguement has been made that oats are useless PWO due to their slow digestion rate, but if the intestinal absorbtion rate limits the absorbtion of the PWO carbs anyway, then the slow digestion rate may not be as big an issue as they make out.

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.

PMID: 3967778 [PubMed - indexed for MEDLINE]

So a high GI may well ilicite a different blood glucose and insulin response, but in the end it doesnt make any difference.


I did not write this article, was just wondering if anyone could lay some truth uppon it

[Vlad]

[ QUOTE ]

There are some instances, however, where a food has a low glycemic value but a high insulin index value. This applies to dairy foods and to some highly palatable energy-dense "indulgence foods." Some foods (such as meat, fish, and eggs) that contain no carbohydrate, just protein and fat (and essentially have a GI value of zero), still stimulate significant rises in blood insulin.


[/ QUOTE ]

significant is not enough for us.

[ QUOTE ]

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.

Publication Types:
Review
Review, Tutorial

PMID: 9578375 [PubMed - indexed for MEDLINE]


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Of course our CNS activates self-replinishing, it's not breaking news. It takes long time before our muscles will be completely replinished, we are just helping manually with some carbs. Besides, our cortisol levels also go up, that needs to be blocked.

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Dietary strategies to promote glycogen synthesis after exercise.

Ivy JL.

Exercise Physiology and Metabolism Laboratory, Department of Kinesiology and Health Education, The University of Texas at Austin, Austin, TX, USA.

Muscle glycogen is an essential fuel for prolonged intense exercise, and therefore it is important that the glycogen stores be copious for competition and strenuous training regimens. While early research focused on means of increasing the muscle glycogen stores in preparation for competition and its day-to-day replenishment, recent research has focused on the most effective means of promoting its replenishment during the early hours of recovery. It has been observed that muscle glycogen synthesis is twice as rapid if carbohydrate is consumed immediately after exercise as opposed to waiting several hours, and that a rapid rate of synthesis can be maintained if carbohydrate is consumed on a regular basis. For example, supplementing at 30-min intervals at a rate of 1.2 to 1.5 g CHO x kg(-1) body wt x h(-1) appears to maximize synthesis for a period of 4- to 5-h post exercise. If a lighter carbohydrate supplement is desired, however, glycogen synthesis can be enhanced with the addition of protein and certain amino acids. Furthermore, the combination of carbohydrate and protein has the added benefit of stimulating amino acid transport, protein synthesis and muscle tissue repair. Research suggests that aerobic performance following recovery is related to the degree of muscle glycogen replenishment.

Publication Types:
Review
Review, Tutorial

PMID: 11897899 [PubMed - indexed for MEDLINE]


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Nothing new here.


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Amino acids stimulate translation initiation and protein synthesis through an Akt-independent pathway in human skeletal muscle.

Liu Z, Jahn LA, Wei L, Long W, Barrett EJ.

Division of Endocrinology and Metabolism, Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908, USA. zl3e@virginia.edu

Studies in vitro as well as in vivo in rodents have suggested that amino acids (AA) not only serve as substrates for protein synthesis, but also as nutrient signals to enhance mRNA translation and protein synthesis in skeletal muscle. However, the physiological relevance of these findings to normal humans is uncertain. To examine whether AA regulate the protein synthetic apparatus in human skeletal muscle, we infused an AA mixture (10% Travesol) systemically into 10 young healthy male volunteers for 6 h. Forearm muscle protein synthesis and degradation (phenylalanine tracer method) and the phosphorylation of protein kinase B (or Akt), eukaryotic initiation factor 4E-binding protein 1, and ribosomal protein S6 kinase (p70(S6K)) in vastus lateralis muscle were measured before and after AA infusion. We also examined whether AA affect urinary nitrogen excretion and whole body protein turnover. Postabsorptively all subjects had negative forearm phenylalanine balances. AA infusion significantly improved the net phenylalanine balance at both 3 h (P &lt; 0.002) and 6 h (P &lt; 0.02). This improvement in phenylalanine balance was solely from increased protein synthesis (P = 0.02 at 3 h and P &lt; 0.003 at 6 h), as protein degradation was not changed. AA also significantly decreased whole body phenylalanine flux (P &lt; 0.004). AA did not activate Akt phosphorylation at Ser(473), but significantly increased the phosphorylation of both eukaryotic initiation factor 4E-binding protein 1 (P &lt; 0.04) and p70(S6K) (P &lt; 0.001). We conclude that AA act directly as nutrient signals to stimulate protein synthesis through Akt-independent activation of the protein synthetic apparatus in human skeletal muscle.


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How many can get ahold of Travesol? Not many I believe.


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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


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Again, they are only looking at one variable - glycogen replinishment. We have more variables to think about in post workout nutrition.


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Scientists Close In On Trigger Of Insulin Resistance

Extra sugar can cause insulin resistance in cells. Now scientists have an explanation.

In experiments with fat cells, Johns Hopkins scientists have discovered direct evidence that a build-up of sugar on proteins triggers insulin resistance, a key feature of most cases of diabetes.
The results underscore the importance of glycosylation - attachment of a sugar to a protein -- as a way cells control proteins' activities, the scientists report in the April 16 issue of the Proceedings of the National Academy of Sciences. The scientists found that at least two proteins involved in passing along insulin's message were unlikely to work properly when coated in extra sugar.

Type 2 diabetes, the most common form in adults, occurs when muscle, fat and other tissues stop responding to insulin's signals to mop up sugar from the blood. The resulting high blood sugar, if uncontrolled, can lead to blindness, amputation and death. Understanding sugar's precise influence on insulin's activity may help improve treatment and prevention, scientists hope.

"Cells don't respond to insulin itself. Instead, a whole cascade of events, set in motion by insulin, eventually causes cells to take in sugar," explains Gerald Hart, Ph.D., professor and director of biological chemistry in the school's Institute for Basic Biomedical Sciences. "We now have an explanation of how sugar can affect these signals, and even a hypothesis for how high blood sugar could cause tissue damage in diabetes -- by improperly modifying proteins."

Hart's lab discovered 18 years ago that sugar is used routinely inside cells to modify proteins, turning them on and off. The more commonly known protein-controller, phosphate, actually binds to some of the same building blocks of proteins as sugar does. If proteins have too many sugars on them, they can't be controlled properly by the cell and are unlikely to work correctly, suggests Hart.

"We think we've come across a major mechanistic reason for insulin resistance," says Hart. "These cells developed insulin resistance simply because their proteins, and specific proteins in fact, had more than the normal number of sugar tags."

If key proteins laden with sugar are present in patients with diabetes, the findings may provide a target for developing new strategies to deal with this growing public health threat, says Hart. While diabetes can be fairly well controlled by diet and carefully monitoring one's blood sugar levels, finding a way to remove extra sugar tags may help treat or prevent diabetes someday, the researchers suggest.

"Textbooks frequently and incorrectly show glycosylation only happening to proteins on the cell surface," says Hart. "Complex sugars are added only to proteins outside the cell, but simple sugars are used all the time in the nucleus and cytoplasm to modify proteins. It's this glycosylation that happens inside the cell, involving simple sugars, that is the key in insulin resistance."

The "simple sugar" to which he refers is O-linked beta-N-acetylglucosamine, a complex name that condenses to a difficult acronym -- O-GlcNAc -- with an ugly pronunciation -- "oh-gluck-nack." But in many ways, O-GlcNAc is a beautiful and mysterious thing, says Hart.

"O-GlcNAc is a modifier on many proteins, but if you didn't know to look for it, you'd never find it," he says. "Instruments and the usual laboratory methods have a hard time measuring it, so we developed the techniques to detect it."

O-GlcNAc is added to proteins by one enzyme and removed from proteins by another. By selectively blocking that removal, the scientists hoped to load up proteins with sugar without adding extra sugar (the way other scientists have created insulin resistance). "We wanted to see the effect of glycosylation itself, so we used a molecular sledgehammer to increase the amount of sugar bound to proteins," says Hart, whose lab proved the ability of the blocker, a molecule called PUGNAc.

Not only did the blocker increase the amount of O-GlcNAc bound to proteins, but that increase caused the cells to stop responding to insulin, say co-first authors and postdoctoral fellows Lance Wells and Keith Vosseller.

Looking for proteins in the insulin-signaling pathway that were more glycosylated than normal, Vosseller and Wells found two: beta-catenin and insulin receptor substrate-1 (IRS-1). The crucial role these proteins play in passing along insulin's messages is likely to be adversely affected by the extra sugars they carry, the researchers say.

"Our experiments show that increasing O-GlcNAc on proteins is, by itself, a cause of insulin resistance, rather than an effect or a coincidence," says Vosseller.

In the body, sugar (glucose) is changed into glucosamine, which is changed into O-GlcNAc. Other scientists have shown that giving cells or animals excessive amounts of sugar or glucosamine, along with extra insulin, leads to insulin resistance. The new findings provide an explanation for others' experience with animal and laboratory models of insulin resistance.

There has been little study of glucosamine, a commonly used dietary supplement, in people. It is suggested that people taking glucosamine consult their doctors if they are concerned about the possibility of increasing their risk of developing diabetes.

Funding was provided by grants and National Research Service Awards from the National Institutes of Health. Professor of biological chemistry Daniel Lane, Ph.D., is also an author.

Under a licensing agreement between Covance Research Products and The Johns Hopkins University, Hart is entitled to a share of royalty received by the university on sales of the antibody used to detect O-GlcNAc on proteins. The terms of this arrangement are being managed by The Johns Hopkins University in accordance with its conflict of interest policies.


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Did I miss something or they don't mention a squat about training? I don't see how it applies to trainies.

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I think the reason why everyone consumes high GI carbs post workout is to replenish their muscle glycogen levels and to combat the insulin level post workout. U have a small window of opportunity post workout when your body is most primed to absorb nutrients. I think worrying about consuming high vs. low GI carbs post workout is rather trivial. To simplfy it (for those of U unfamiliar) glycogen is in muscle and glucose floats around in the blood (at a very small amount). The glycogen only lasts about 10 min, so like AT said, you should be more concerned about pre-workout complex carbs IMO. They would be much more beneficial.


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Again, one variable. He obviously has no idea what he's talking about.

Quote from Jacob from his Muscle Fiber Article:
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Facilitated Diffusion - This is diffusion that is assisted by protein transports. When a needed nutrient is low in the muscle cell environment and it cannot pass through the pores, then it must be transported). This is similar to the above process except that it needs a boat to get across the plasma membrane and into the cell environment. Following a workout, when glucose concentrations are low, and you down a high carb drink, the glucose in your blood stream has a high concentration. Therefore it diffuses to the lower concentration area inside your muscle cells. The green nutrients are insoluble to lipids, they therefore must move across the membrane in a transported manner. The purple protein transporters as you can see take the nutrients, carry them across the membrane and then release them inside of the cell environment


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Also people think the faster you replenish glycogen stores the faster rate of synthesis will occur and thats just not true.

The oatmeal is not even for the first phase of glycogen replenishment because that phase is insulin independent. It's more for the second insulin dependent stage which is much more prolonged.


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This one must have ran away from circus or something. He should seriously consider a career as comedian for bodybuilding scienfitic community.

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exercise in itself makes you extremely insulin sensitive therefore just about any form of carb will immedietly be put to use


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He can be his partner.



Okay, I'm tired of quotting and telling the same thing. Read Window of Opportunity with its new addons. That should answer ALL of your questions.

[Cronus]

[ QUOTE ]

Division of Endocrinology and Metabolism, Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908, USA. zl3e@virginia.edu

Studies in vitro as well as in vivo in rodents have suggested that amino acids (AA) not only serve as substrates for protein synthesis, but also as nutrient signals to enhance mRNA translation and protein synthesis in skeletal muscle. However, the physiological relevance of these findings to normal humans is uncertain. To examine whether AA regulate the protein synthetic apparatus in human skeletal muscle, we infused an AA mixture (10% Travesol) systemically into 10 young healthy male volunteers for 6 h. Forearm muscle protein synthesis and degradation (phenylalanine tracer method) and the phosphorylation of protein kinase B (or Akt), eukaryotic initiation factor 4E-binding protein 1, and ribosomal protein S6 kinase (p70(S6K)) in vastus lateralis muscle were measured before and after AA infusion. We also examined whether AA affect urinary nitrogen excretion and whole body protein turnover. Postabsorptively all subjects had negative forearm phenylalanine balances. AA infusion significantly improved the net phenylalanine balance at both 3 h (P < 0.002) and 6 h (P < 0.02). This improvement in phenylalanine balance was solely from increased protein synthesis (P = 0.02 at 3 h and P < 0.003 at 6 h), as protein degradation was not changed. AA also significantly decreased whole body phenylalanine flux (P < 0.004). AA did not activate Akt phosphorylation at Ser(473), but significantly increased the phosphorylation of both eukaryotic initiation factor 4E-binding protein 1 (P < 0.04) and p70(S6K) (P < 0.001). We conclude that AA act directly as nutrient signals to stimulate protein synthesis through Akt-independent activation of the protein synthetic apparatus in human skeletal muscle.

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I too like pie. [img]/forum/images/graemlins/crazy.gif[/img]

[Johnny Flash]

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This one must have ran away from circus or something.

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Great comment! LOL

[Adam Knowlden]

We've covered all of those a multitude of times.

There really is no need for us to defend Post workout Spiking anymore. Its like argueing whether or not the world is round at this point.

[butcher22]

Just down your maltodextrin and dextrose with whey post workout and stop questioning the unquestionable.

[nothwang]

the earth is round?

[psaturn]

[ QUOTE ]
the earth is round?

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That is shocking ! I see it flat !