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The perfect postworkout protein protocol

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    The perfect postworkout protein protocol


    The Perfect Post Workout Protein Protocol

    Its common knowledge that PWO protein intake combined with high glycemic carbohydrates drastically increases recovery and muscle gain. But with all the products out there it’s hard to know if you really getting the most you can out of your PWO nutrition. To get the most out of it, I’m going to explain some general concepts.

    Advantages Of Whey Protein:

    * Helps boost immune system.
    * Whey will absorb 80-90% and isolate will absorb about 90-99% and mixes can offer 100%.
    * Enhances muscle recovery after workouts and helps prevent muscle breakdown.
    * Best source of amino acids next to cooked eggs.
    * Absorbs very quickly in the body.
    * Inexpensive to produce.
    * Easy to flavor.
    * Has a long shelf life.
    * Can be prepared several ways and mixes easily with water.

    Whey comes in several forms: concentrate, isolate, and hydrolyzed whey.
    The most common and least effective form is whey concentrate which has an absorption rate of at best 80-85%. And OK bioavailability

    The next best thing is whey isolate which can absorb up into the 90-99% ranges and better bioavailability.

    The best protein out there i hydrolyzed whey protein. This is essentially the why protein after it has been predigested by enzymes breaking into really small fragments. These small fragments are much easier for the body to absorb and use as building blocks then the larger proteins. Hydrolyzed whey can be found in small amounts in a lot of formulas out there but its important to see what the average size of the proteins are the smaller the better, but usually the more expensive.

    Why is hydro whey so great?
    Your body very rarely actually uses large proteins. The body is constructing different proteins using the protein you digest as building blocks. The protein we eat is usually in the form of large peptides and proteins that were previously constructed by the organism they came from. So our body instead of looking for a place where we need that exact protein digest and breaks down the protein into small pieces which it can use to make its own bigger proteins. The best forms of hydrolyzed whey are broken down into pieces as small as 3-5 amino acids long. So basically imagine trying to construct a building with legos. Hydro whey is like getting stacks of 3 legos together that you can use to from walls etc. for your building. Regular protein would be like trying to build a lego building with a pre-constructed lego car. You have to take it apart before you can actually add to your building.

    So hydro is not only absorbed faster b/c it is smaller, but it is actually able to be used by your body much faster and easier and more completely than sources of full length proteins.

    So what is the best post workout nutrition method?
    Research has shown that protein in combination with high glycemic carbohydrates after exercise in a 2:1 ratio is extremely beneficial. The reason that carbohydrates are need are mainly for digestion of those of those proteins when your body is already starved of carbohydrates from the workout. During your workout your body releases glucose from the stores in the muscles, and when the workout is over the body increases insulin very easily in response to food intake b/c it wants to replenish those levels of glucose in the muscle. This is one reason why you need lots of carbs with your protein b/c most of the carbs are beings stored and used to recover your energy from the workout and remove lactic acid etc.

    By using hydro whey there is less of a carbohydrate demand for protein absorption and construction. There are some supplement companies that fail to realize this and pack 4 times the carbohydrates with hydro whey. This is just extra carbs to be stored as fat.
    When you take a whey concentrate or isolate those carbs are used to digest the protein.

    So here is what IMO would provide the best post workout benefit.
    Immediately following workout.
    15-20g hydro whey with 20-30g of dextrose
    15-20 minutes after the workout
    20-40g whey isolate/concentrate combo mixed with milk with or followed by a low fat med to low glycemic carb meal. Fruit it a great choice here. To have with your shake. And apple or banana works great. Especially if you do vanilla shakes and blend the banana in.

    This gives you the quickest protein available to your muscles, and still utilizes larger slower digest protein to keep the anabolic environment while utilizes the carbohydrates ingested to limit any fat gain.

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    Good post bro!
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    i personally have had much success using scivations methos of 20g BCAA's, 10g glutamine, and 1 scoop whey isolate. i sip this throughout my workout and kill whatever is left before cardio. when i get home, i immediately prepare a whole food meal and eat it soon after. this has proven to work brilliantly for me.
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    Quote Originally Posted by WannaBeHulk
    i personally have had much success using scivations methos of 20g BCAA's, 10g glutamine, and 1 scoop whey isolate. i sip this throughout my workout and kill whatever is left before cardio. when i get home, i immediately prepare a whole food meal and eat it soon after. this has proven to work brilliantly for me.
    Good lord. Why on earth are you using that much in BCAA and glutamine? You do understand the majority of that is just converted via gluconeogensis to glucose right?
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    Quote Originally Posted by TheGame46
    So what is the best post workout nutrition method?
    Research has shown that protein in combination with high glycemic carbohydrates after exercise in a 2:1 ratio is extremely beneficial. The reason that carbohydrates are need are mainly for digestion of those of those proteins when your body is already starved of carbohydrates from the workout. During your workout your body releases glucose from the stores in the muscles, and when the workout is over the body increases insulin very easily in response to food intake b/c it wants to replenish those levels of glucose in the muscle. This is one reason why you need lots of carbs with your protein b/c most of the carbs are beings stored and used to recover your energy from the workout and remove lactic acid etc.
    The body isn't starved of carbohydrates after a workout. Carb depletion isn't achieved in a 60 minute workout, its achieved over long periods of carb restrictions. Weight training utilizes and oxidized FFA's for energy much more than blood glucose.

    The replenishment of glycogen (not glucose) isn't a priority unless you have further activity. The need for high GI or large amounts isn't necessary at all as glut 4 is increased regardless.
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    I was thinking the same of the post-workout high GI stuff. It's just not necessary and just led to extra fat storage for me. I sip on 10 grams BCAA during, gulp down 45 grams whey and 1/2 cup oats post-workout. Works for me! Good info on the whey though.
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    I think Bobo has pointed out before that using lower GI carbs is better post workout for avoiding fat gain.

    Personally I think you can't beat what nature intended for your body - fruit. If you return home after your workout, throw some fruit in the blender with the protein. You can experiment with different fruit for lower or higher GI carbs. Bananas are cheap, mix well, and are at the upper end of moderate on the GI scale.

    I think simple oats are great advice, personally I find fruit easier to choke down.
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    Quote Originally Posted by Bobo
    The need for high GI or large amounts isn't necessary at all as glut 4 is increased regardless.
    What amount (gr/lbs of BW) of low GI carb do you recommend right after workout?
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    Quote Originally Posted by Bobo
    Weight training utilizes and oxidized FFA's for energy much more than blood glucose.
    I didn't know that... that's really interesting (wheee, now I don't have to do my cardio!! ). Mind pointing me out to a pubmed reference so I can read more?

    Also, if glycogen depletion occurs over long periods of time rather than just a 60 minute session, what is the reason for the "wall" that is hit when you train a specific body part until you no longer can work it? Not the lactic acid buildup during a set, but the inability to no longer work out a body part after a particularly volume-heavy workout?
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    Quote Originally Posted by NYhomeboy
    I didn't know that... that's really interesting (wheee, now I don't have to do my cardio!! ). Mind pointing me out to a pubmed reference so I can read more?

    Also, if glycogen depletion occurs over long periods of time rather than just a 60 minute session, what is the reason for the "wall" that is hit when you train a specific body part until you no longer can work it? Not the lactic acid buildup during a set, but the inability to no longer work out a body part after a particularly volume-heavy workout?
    I don't have a pubmed reference for that. I have texts. Cardio is still extremely vital as it won't cause the problems listed below (when done with low intensity).

    Metabolic fatique (increased La, H, Cr, p and K) cause that feeling. If it was just a glucose issue you could drink gatorade for hours upon end and train and not miss a beat. Generally your body is going to fight you and its the reason why you grow in the first place so it doen'st have to go thorugh that condition again (or if it does its less taxing).
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    Quote Originally Posted by Bobo
    The body isn't starved of carbohydrates after a workout. Carb depletion isn't achieved in a 60 minute workout, its achieved over long periods of carb restrictions. Weight training utilizes and oxidized FFA's for energy much more than blood glucose.

    The replenishment of glycogen (not glucose) isn't a priority unless you have further activity. The need for high GI or large amounts isn't necessary at all as glut 4 is increased regardless.
    I should have clarified that blood glucose levels are dropped, resulting in the reslease of glucose from glycogen stores. (the opposite effect of insulin) Post workout we are trying to acheive an insulin type response so that the muscle begins to uptake nutrients once again. The muscle takes up less amino acid content when it is releasing glucose b/c the body thinks its energy is needed for force production not anabolism. This is why reversing this effect immediately PWO when the response will be greatest is key. If not taken within the short time frame you might as well take a whey casein mix I agree.
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    Quote Originally Posted by TheGame46
    I should have clarified that blood glucose levels are dropped, resulting in the reslease of glucose from glycogen stores. (the opposite effect of insulin) Post workout we are trying to acheive an insulin type response so that the muscle begins to uptake nutrients once again. The muscle takes up less amino acid content when it is releasing glucose b/c the body thinks its energy is needed for force production not anabolism. This is why reversing this effect immediately PWO when the response will be greatest is key. If not taken within the short time frame you might as well take a whey casein mix I agree.
    Thats because glucagon is increased but the energy demand during a weight training session ins't that high.

    There really isn't an insulin type response. Its either there or not. GLUT 4 is increased due to energy demand so the condition in which insulin increases GLUT 4 during normal feeding patterns is already present. In other words, the door is already open and the need for carbohydrate to trigger insulin to help shuttle nutrients isn't needed. Exercise alone creates this condition. Unless you have an activity following this (such as a training session then practice) then need to replenish glycogen stores fast isn't needed or warranted. You are under the assumption that insulin actually has an anabolic effect (which it doesn't in normal physiological levels) rather than its actual effect in decreasing protein degradation. Its mainly an anti-catabolic effect which happens if the amount is large or small.

    As for as protein turnover rate and the utilization of amino's acids, all that is needed is to maintain a consistent level during your workout and that is achieved through pre workout nutrition, not post workout.
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    Quote Originally Posted by Bobo
    Thats because glucagon is increased but the energy demand during a weight training session ins't that high.

    There really isn't an insulin type response. Its either there or not. GLUT 4 is increased due to energy demand so the condition in which insulin increases GLUT 4 during normal feeding patterns is already present. In other words, the door is already open and the need for carbohydrate to trigger insulin to help shuttle nutrients isn't needed. Exercise alone creates this condition. Unless you have an activity following this (such as a training session then practice) then need to replenish glycogen stores fast isn't needed or warranted. You are under the assumption that insulin actually has an anabolic effect (which it doesn't in normal physiological levels) rather than its actual effect in decreasing protein degradation. Its mainly an anti-catabolic effect which happens if the amount is large or small.

    As for as protein turnover rate and the utilization of amino's acids, all that is needed is to maintain a consistent level during your workout and that is achieved through pre workout nutrition, not post workout.
    I am agreeing wiht you on almost eery part here but with weight training you say the demand is less. But if you take a look at the way the body uses energy you will see that fat utilization during weight training is essentially non existant b/c of the time fram in which the body uses its energy sources. Weight training is primarily using the glycolytic pathway for evergy.

    Insulin itself is no anabolic, but combined with the phsyiological factors induced by weight training combined with the need to combat the glucagon release it can increase the anabolic effect.

    You have upregulated Test, IGF, lactic acid and HGH levels in response to a complete weight training bout. This means you are primed for maximum anabolism. Anabolism requires energy, which you are currently shuttling out of the muscles stores to be used for mechanical energy instead of protein synthesis within. I can't see how you can then deny that increasing flow of nutrients into the muscle at this time would not be benificial.

    Ask anyone who uses slin.
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    Quote Originally Posted by USPLabs
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    LOL I know its nice to have a good debate with someone intelligant every now and then instead of those goons that follow me on the other boards!!!
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    Quote Originally Posted by Bobo
    I don't have a pubmed reference for that. I have texts. Cardio is still extremely vital as it won't cause the problems listed below (when done with low intensity).

    Metabolic fatique (increased La, H, Cr, p and K) cause that feeling. If it was just a glucose issue you could drink gatorade for hours upon end and train and not miss a beat. Generally your body is going to fight you and its the reason why you grow in the first place so it doen'st have to go thorugh that condition again (or if it does its less taxing).
    If its just La, H, Cr, p and K then why can't you take a 2 minute rest and be completely recovered? Powerlifters rely heavily on some of these for their 1-3 rep sets which is why they rest longer than bodybuilders. This allows these levels to replenish as fully as possible. In the case of a bodybuilder doing sets of 6-15+ with less rest there is a lot more use of glucose for energy during the sets. This is what increases the La, but to remove that lactic acid you need to have oxygen and energy to spare. When you are releasing glucose form the muscle you are not going to be using energy to re-utilize that lactic acid, so it builds up. In the case of bodybuilder this causes an increase in HGH which is a good response for growth. However if you push this to far, you decrease local test and igf levels. This is why you dont get significant hypertrophy from endurance training like you do bodybuilding.

    To answer your ? as you lift you are depleting these levels, and its basically like a computer. Your body starts with the using its fastest available source of ATP. and works its way down. ATP stores are the fastest then it use CTP, then glucose then fat. SO once you start depleting the levels of the fastest ones you are now depending on energy sources that produce fewer molecules of ATP per second. Thus you fatigue faster in the later sets.
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    Quote Originally Posted by TheGame46
    I am agreeing wiht you on almost eery part here but with weight training you say the demand is less. But if you take a look at the way the body uses energy you will see that fat utilization during weight training is essentially non existant b/c of the time fram in which the body uses its energy sources. Weight training is primarily using the glycolytic pathway for evergy.

    Insulin itself is no anabolic, but combined with the phsyiological factors induced by weight training combined with the need to combat the glucagon release it can increase the anabolic effect.

    You have upregulated Test, IGF, lactic acid and HGH levels in response to a complete weight training bout. This means you are primed for maximum anabolism. Anabolism requires energy, which you are currently shuttling out of the muscles stores to be used for mechanical energy instead of protein synthesis within. I can't see how you can then deny that increasing flow of nutrients into the muscle at this time would not be benificial.

    Ask anyone who uses slin.
    You are not making sense here.

    Weight training is one of the most productive ways to break down stored triglycerides to be oxidized. It doesn't pick one or the other. The body uses energy with increased ratios to macronutrients depending on energy demans. The release of oxidation of FFA's during weight training is increased drastically, moreso than almost any training. During low to moderate activity muscle mainly utilize fatty acids for fuel and conserve glycogen. Thats just basic physiology. You can look it up in any text.


    You seem to missing some very basic steps here. Nobody is saying that you aren't shuttling nutrients into muscles. The point is that large amounts of insulin are not needed. Insulin shuttles nutrients by increasing cell permiability and increasing GLUT4, a condition that is ALREADY present BECAUSE of exercise.


    As for your commetn on slin users, I don't think you understand the MAJOR difference that supraphysiological levels of insulin has comapred to normal levels and the cometpely difference cascade of events that happens (or doesn't) because of this. As you can see, its not the same:

    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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    And since I've had this debate for the last 4 years with a million different people, this summed it up nicely before.


    "This entire thread is marred by the simple fact that weight training is not a glycogen-depleting form of exercise. Sure, there will be some loss of glycogen stores, but nowhere near what is found from the type of glycogen-depleting protocols used in refeeding experiments. The type of high-intensity, rest-between-sets of weight lifting taxes the ATP-CP system heavily, but only has a small to moderate effect on glycogen reserves unless training volume is extremely high and/or there is little or no rest between sets and exercises.

    Not that this automatically invalidates everything that's been said, but it seems to me that we may well be comparing apples to oranges here. I know of no published studies which look at the effect of the post-workout meal on protein synthesis/degradation or glycogen synthesis after weight training.

    Janet Rankin did such a study two years ago in our department, and found no effect. Such an "unexciting" finding meant that it didn't get published, unfortunatetly.

    In another thread a while back, we discussed at length a human study which looked at the effects of insulin infusion, both at reast and post-exercise, on muscle protein synthesis. The bottom line was that insulin infusion increased muscle protein syntheses via its effects on vasodilation, which in turn caused a greater rate of amino acid deliver to muscle tissue under resting conditions.

    Post-exercise, when blood flow to muscles was already enhanced, insulin infusion had no further effect on protein synthesis. Thus, the idea that insulin spikes are anabolic in during post-workout conditions appears to be a myth, although there is still room for the anti-catabolic effects of insulin in the post workout state; however, the real-world significance of this for weight trainers is questionable.

    More important for anabolism would seem to be a high level of circulating amino acids both during the workout and post-workout, in addition to a high level of blood flow to the muscles."
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    Quote Originally Posted by Bobo
    You are not making sense here.

    Weight training is one of the most productive ways to break down stored triglycerides to be oxidized. It doesn't pick one or the other. The body uses energy with increased ratios to macronutrients depending on energy demans. The release of oxidation of FFA's during weight training is increased drastically, moreso than almost any training. During low to moderate activity muscle mainly utilize fatty acids for fuel and conserve glycogen. Thats just basic physiology. You can look it up in any text.


    You seem to missing some very basic steps here. Nobody is saying that you aren't shuttling nutrients into muscles. The point is that large amounts of insulin are not needed. Insulin shuttles nutrients by increasing cell permiability and increasing GLUT4, a condition that is ALREADY present BECAUSE of exercise.


    As for your commetn on slin users, I don't think you understand the MAJOR difference that supraphysiological levels of insulin has comapred to normal levels and the cometpely difference cascade of events that happens (or doesn't) because of this. As you can see, its not the same:

    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.
    Tis study isn't applicable b/c its doesnt occur after exercise. The conditions are not the same.
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    Insulin-stimulated insulin receptor substrate-2-associated phosphatidylinositol 3-kinase activity is enhanced in human skeletal muscle after exercise.

    * Howlett KF,
    * Sakamoto K,
    * Yu H,
    * Goodyear LJ,
    * Hargreaves M.

    Center for Physical Activity and Nutrition (C-PAN), School of Exercise and Nutrition Sciences, Deakin University, Burwood, Victoria 3125, Australia. kirsten.howlett@deakin.edu.au

    Exercise increases skeletal muscle insulin action but the underlying mechanisms mediating this are equivocal. In mouse skeletal muscle, prior exercise enhances insulin-stimulated insulin receptor substrate-2 (IRS-2) signaling (Diabetes 2002;51:479-83), but it is unknown if this also occurs in humans. Hyperinsulinemic-euglycemic clamps were performed on 7 untrained males at rest and immediately after 60 minutes of cycling exercise at approximately 75% Vo2peak. Muscle biopsies were obtained at basal, immediately after exercise, and at 30 and 120 minutes of hyperinsulinemia. Insulin infusion increased (P < .05) insulin receptor tyrosine phosphorylation similarly in both the rest and exercise trials. Under resting conditions, insulin infusion resulted in a small, but non-statistically significant increase in IRS-2-associated phosphatidylinositol 3 (PI 3)-kinase activity over basal levels. Exercise per se decreased (P < .05) IRS-2-associated PI 3-kinase activity. After exercise, insulin-stimulated IRS-2-associated PI 3-kinase activity tended to increase at 30 minutes and further increased (P < .05) at 120 minutes when compared with the resting trial. Insulin increased (P < .05) Akt Ser473 and GSK-3alpha/beta Ser21/Ser9 phosphorylation in both trials, with the response tending to be higher in the exercise trial. In conclusion, in the immediate period after an acute bout of exercise, insulin-stimulated IRS-2 signaling is enhanced in human skeletal muscle.
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    Quote Originally Posted by TheGame46
    Tis study isn't applicable b/c its doesnt occur after exercise. The conditions are not the same.
    Then let me get that one.
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    Now lets talk about beyond the glucose/protein up take
    Insulin is going to positively effect IGF-I levels as wel by limiting the IGF binding proteins so that the exercise induced IGF release can have a gerater effect.

    IGF-binding protein-1 levels are related to insulin-mediated glucose disposal and are a potential serum marker of insulin resistance.

    * Maddux BA,
    * Chan A,
    * Mandarino LJ,
    * Goldfine ID.

    Department of Medicine, Diabetes Center, University of California, San Francisco, 2200 Post, C415, 94143-1616, USA. bmaddux@itsa.ucsf.edu

    OBJECTIVE: IGF-binding protein (IGFBP)-1 is negatively regulated by insulin. We determined whether the measurement of IGFBP-1 in serum is a useful marker of insulin resistance. RESEARCH DESIGN AND METHODS: Twenty-three subjects underwent a euglycemic insulin clamp. Glucose disposal rates (M) were then correlated with measurements of IGFBP-1, fasting insulin levels, homeostasis model assessment (HOMA), and BMI. RESULTS: IGFBP-1 levels more strongly correlated with M (R = 0.73) than the other parameters such as BMI or HOMA. The level of this protein decreased in individuals who became more insulin sensitive by exercise training. CONCLUSIONS: These studies show a strong correlation between insulin sensitivity and the serum levels of IGFBP-1. These studies suggest, therefore, that measurement of this protein may be valuable in identifying those individuals with insulin resistance and those individuals who respond to interventional strategies.
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    double post sorry
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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.





    THen as a result:



    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
    --------------------------------------------------------------------------------
    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&#215;min&#171;minus&#187;1 &#215;kg&#171;minus&#187;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.
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    Acutally no, because you are skipping a million steps.



    Quote Originally Posted by TheGame46
    Now lets talk about beyond the glucose/protein up take
    Insulin is going to positively effect IGF-I levels as wel by limiting the IGF binding proteins so that the exercise induced IGF release can have a gerater effect.

    IGF-binding protein-1 levels are related to insulin-mediated glucose disposal and are a potential serum marker of insulin resistance.

    * Maddux BA,
    * Chan A,
    * Mandarino LJ,
    * Goldfine ID.

    Department of Medicine, Diabetes Center, University of California, San Francisco, 2200 Post, C415, 94143-1616, USA. bmaddux@itsa.ucsf.edu

    OBJECTIVE: IGF-binding protein (IGFBP)-1 is negatively regulated by insulin. We determined whether the measurement of IGFBP-1 in serum is a useful marker of insulin resistance. RESEARCH DESIGN AND METHODS: Twenty-three subjects underwent a euglycemic insulin clamp. Glucose disposal rates (M) were then correlated with measurements of IGFBP-1, fasting insulin levels, homeostasis model assessment (HOMA), and BMI. RESULTS: IGFBP-1 levels more strongly correlated with M (R = 0.73) than the other parameters such as BMI or HOMA. The level of this protein decreased in individuals who became more insulin sensitive by exercise training. CONCLUSIONS: These studies show a strong correlation between insulin sensitivity and the serum levels of IGFBP-1. These studies suggest, therefore, that measurement of this protein may be valuable in identifying those individuals with insulin resistance and those individuals who respond to interventional strategies.
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    Quote Originally Posted by TheGame46
    Tis study isn't applicable b/c its doesnt occur after exercise. The conditions are not the same.
    Really, are you actually going to sit there and tell me that post wokrout is a condition that is going to have an effect on the differences between injected insulin vs. normal insulin response? Because if you do then this "debate" is pointless beause you arne't even looking at the relevant research.
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    Possible stimuli for strength and power adaptation: acute hormonal responses.

    * Crewther B,
    * Keogh J,
    * Cronin J,
    * Cook C.

    Human Health and Performance Group, HortResearch, Auckland, New Zealand. BCrewther@Hortresearch.co.nz

    The endocrine system plays an important role in strength and power development by mediating the remodelling of muscle protein. Resistance training scheme design regulates muscle protein turnover by modifying the anabolic (testosterone, growth hormone) and catabolic (cortisol) responses to a workout. Although resistance exercise increases the concentrations of insulin-like growth factor 1 in blood following exercise, the effect of scheme design is less clear, most likely due to the different release mechanisms of this growth factor (liver vs muscle). Insulin is non-responsive to the exercise stimulus, but in the presence of appropriate nutritional intake, elevated blood insulin levels combined with resistance exercise promotes protein anabolism. Factors such as sex, age, training status and nutrition also impact upon the acute hormonal environment and, hence, the adaptive response to resistance training. However, gaps within research, as well as inconsistent findings, limit our understanding of the endocrine contribution to adaptation. Research interpretation is also difficult due to problems with experimental design (e.g. sampling errors) and various other issues (e.g. hormone rhythms, biological fluid examined). In addition to the hormonal responses to resistance exercise, the contribution of other acute training factors, particularly those relating to the mechanical stimulus (e.g. forces, work, time under tension) must also be appreciated. Enhancing our understanding in these areas would also improve the prescription of resistance training for stimulating strength and power adaptation.
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    Quote Originally Posted by TheGame46
    Possible stimuli for strength and power adaptation: acute hormonal responses.

    * Crewther B,
    * Keogh J,
    * Cronin J,
    * Cook C.

    Human Health and Performance Group, HortResearch, Auckland, New Zealand. BCrewther@Hortresearch.co.nz

    The endocrine system plays an important role in strength and power development by mediating the remodelling of muscle protein. Resistance training scheme design regulates muscle protein turnover by modifying the anabolic (testosterone, growth hormone) and catabolic (cortisol) responses to a workout. Although resistance exercise increases the concentrations of insulin-like growth factor 1 in blood following exercise, the effect of scheme design is less clear, most likely due to the different release mechanisms of this growth factor (liver vs muscle). Insulin is non-responsive to the exercise stimulus, but in the presence of appropriate nutritional intake, elevated blood insulin levels combined with resistance exercise promotes protein anabolism. Factors such as sex, age, training status and nutrition also impact upon the acute hormonal environment and, hence, the adaptive response to resistance training. However, gaps within research, as well as inconsistent findings, limit our understanding of the endocrine contribution to adaptation. Research interpretation is also difficult due to problems with experimental design (e.g. sampling errors) and various other issues (e.g. hormone rhythms, biological fluid examined). In addition to the hormonal responses to resistance exercise, the contribution of other acute training factors, particularly those relating to the mechanical stimulus (e.g. forces, work, time under tension) must also be appreciated. Enhancing our understanding in these areas would also improve the prescription of resistance training for stimulating strength and power adaptation.

    Umm...are you going to post anything that is recent and/or by IVY and Tipton?

    "However, gaps within research, as well as inconsistent findings, limit our understanding of the endocrine contribution to adaptation. "


    All you have to do is look a little further.
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    "Both muscle contraction and insulin have been shown to increase the activity of glycogen synthase, the rate-limiting enzyme in glycogen synthesis."

    quote from your first study.
    The 2nd is not in relation to exercise

    No I am not saying that insulin response to digestion of carb is anywhere near that of supraphsyiological levels. That is clear

    And what steps do you think I am missing with the IGF? B/c this is common knowledge IMO.
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    Quote Originally Posted by TheGame46
    "Both muscle contraction and insulin have been shown to increase the activity of glycogen synthase, the rate-limiting enzyme in glycogen synthesis."

    quote from your first study.
    The 2nd is not in relation to exercise

    No I am not saying that insulin response to digestion of carb is anywhere near that of supraphsyiological levels. That is clear

    And what steps do you think I am missing with the IGF? B/c this is common knowledge IMO.
    You already started to try to explain the cascade of events that happens as a results of insulin release without even looking as what levels or amounts of insulin are need to achieve those conditions. Its small. So I really don't care about the IGF-1 aspect because it happens regardless whether I ingest a carbohydrate or amino insulin since both are insulinogenic.



    The 2nd quote doesn't need to be related to exercise. Saying this study isn't relevant because exercise isn't involved is ridiculous. The point of the study is to show that insulin's actions within a normal physiological level are anti-catabolic, not anabolic. Its ALWAYS present whether you consume a carb or protein mix.
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    Exercise Effects on Muscle Insulin Signaling and Action
    Invited Review: Role of insulin in translational control of protein synthesis in skeletal muscle by amino acids or exercise
    Scot R. Kimball1, Peter A. Farrell2, and Leonard S. Jefferson1

    1 Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey 17033; and 2 Noll Physiology Research Center, The Pennsylvania State University, University Park, Pennsylvania 16802

    Protein synthesis in skeletal muscle is modulated in response to a variety of stimuli. Two stimuli receiving a great deal of recent attention are increased amino acid availability and exercise. Both of these effectors stimulate protein synthesis in part through activation of translation initiation. However, the full response of translation initiation and protein synthesis to either effector is not observed in the absence of a minimal concentration of insulin. The combination of insulin and either increased amino acid availability or endurance exercise stimulates translation initiation and protein synthesis in part through activation of the ribosomal protein S6 protein kinase S6K1 as well as through enhanced association of eukaryotic initiation factor eIF4G with eIF4E, an event that promotes binding of mRNA to the ribosome. In contrast, insulin in combination with resistance exercise stimulates translation initiation and protein synthesis through enhanced activity of a guanine nucleotide exchange protein referred to as eIF2B. In both cases, the amount of insulin required for the effects is low, and a concentration of the hormone that approximates that observed in fasting animals is sufficient for maximal stimulation. This review summarizes the results of a number of recent studies that have helped to establish our present understanding of the interactions of insulin, amino acids, and exercise in the regulation of protein synthesis in skeletal muscle.



    In other words, amino acids are much more important post workout and the amounts of insulin needed to achieve the synergism is small.
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    So your saying there is no dose dependcy for those actions? The benefit of decreasing IGF binding to IR's alone is does dependent as well as IGFBP levels are directly propotional to insulin levels according to that study which is why its usful in measuring insulin sensativity.

    Effects of exercise and insulin on insulin signaling proteins in human skeletal muscle.

    * Koval JA,
    * Maezono K,
    * Patti ME,
    * Pendergrass M,
    * DeFronzo RA,
    * Mandarino LJ.

    Department of Medicine, The University of Texas Health Science Center at San Antonio, 78284-7886, USA.

    Insulin and exercise independently increase glucose metabolism in muscle. Moreover, exercise training or a prior bout of exercise increases insulin-stimulated glucose uptake in resting skeletal muscle. The present study was undertaken to compare how physiological hyperinsulinemia and moderate intensity aerobic exercise affect the tyrosine phosphorylation state and activity of insulin signaling molecules in healthy, physically inactive volunteers. Subjects had biopsies of the vastus lateralis muscle before and immediately after 30 min of either hyperinsulinemia (euglycemic insulin clamp) or moderate-intensity exercise on a cycle ergometer (approximately 60% of VO2max). Insulin receptor and IRS-1 tyrosine phosphorylation, association of the p85 regulatory subunit of PI 3-kinase with IRS-1, IRS-1 associated PI 3-kinase activity, and glycogen synthase activity were determined in muscle biopsy specimens taken from healthy subjects before and after insulin or exercise. Physiological hyperinsulinemia increased the rate of glucose disposal from 11.4 +/- 1.5 to 25.6 +/- 6.7 micromol x kg(-1) x min(-1) (P < 0.01), insulin receptor and IRS-1 tyrosine phosphorylation (173 +/- 19% and 159 +/- 35% of basal values, respectively, P < 0.05), association of the p85 regulatory subunit of PI 3-kinase with IRS-1 (159 +/- 10%, P < 0.05), and glycogen synthase fractional velocity (136 +/- 11%, P < 0.01). Exercise also increased glucose disposal, from 10.4 +/- 0.5 to 15.6 +/- 1.7 micromol x kg(-1) x min(-1) (P < 0.01) and glycogen synthase fractional velocity (253 +/- 35% of basal, P < 0.01). The exercise-induced increase in glycogen synthase was greater than that due to insulin (P < 0.05). In contrast to insulin, exercise decreased tyrosine phosphorylation of the insulin receptor to 72 +/- 10% of basal values (P < 0.05 vs basal and P < 0.05 vs insulin) and had no effect on IRS-1 tyrosine phosphorylation, or association of p85 with IRS-1. The exercise-induced decreased insulin receptor tyrosine phosphorylation could explain the well-known effect of exercise to enhance the sensitivity of muscle to insulin.
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    Quote Originally Posted by Bobo
    Exercise Effects on Muscle Insulin Signaling and Action
    Invited Review: Role of insulin in translational control of protein synthesis in skeletal muscle by amino acids or exercise
    Scot R. Kimball1, Peter A. Farrell2, and Leonard S. Jefferson1

    1 Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey 17033; and 2 Noll Physiology Research Center, The Pennsylvania State University, University Park, Pennsylvania 16802

    Protein synthesis in skeletal muscle is modulated in response to a variety of stimuli. Two stimuli receiving a great deal of recent attention are increased amino acid availability and exercise. Both of these effectors stimulate protein synthesis in part through activation of translation initiation. However, the full response of translation initiation and protein synthesis to either effector is not observed in the absence of a minimal concentration of insulin. The combination of insulin and either increased amino acid availability or endurance exercise stimulates translation initiation and protein synthesis in part through activation of the ribosomal protein S6 protein kinase S6K1 as well as through enhanced association of eukaryotic initiation factor eIF4G with eIF4E, an event that promotes binding of mRNA to the ribosome. In contrast, insulin in combination with resistance exercise stimulates translation initiation and protein synthesis through enhanced activity of a guanine nucleotide exchange protein referred to as eIF2B. In both cases, the amount of insulin required for the effects is low, and a concentration of the hormone that approximates that observed in fasting animals is sufficient for maximal stimulation. This review summarizes the results of a number of recent studies that have helped to establish our present understanding of the interactions of insulin, amino acids, and exercise in the regulation of protein synthesis in skeletal muscle.



    In other words, amino acids are much more important post workout and the amounts of insulin needed to achieve the synergism is small.

    Ok this gets you passed absorbtion. But synthesis takes a lot of energy. Would it not then benefit to have an excess of nutrient available?
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    Serisouly are you even reading what I post or does everything with you relate back to IGF-1 and your research for IBE?




    Quote Originally Posted by TheGame46
    So your saying there is no dose dependcy for those actions? The benefit of decreasing IGF binding to IR's alone is does dependent as well as IGFBP levels are directly propotional to insulin levels according to that study which is why its usful in measuring insulin sensativity.

    Effects of exercise and insulin on insulin signaling proteins in human skeletal muscle.

    * Koval JA,
    * Maezono K,
    * Patti ME,
    * Pendergrass M,
    * DeFronzo RA,
    * Mandarino LJ.

    Department of Medicine, The University of Texas Health Science Center at San Antonio, 78284-7886, USA.

    Insulin and exercise independently increase glucose metabolism in muscle. Moreover, exercise training or a prior bout of exercise increases insulin-stimulated glucose uptake in resting skeletal muscle. The present study was undertaken to compare how physiological hyperinsulinemia and moderate intensity aerobic exercise affect the tyrosine phosphorylation state and activity of insulin signaling molecules in healthy, physically inactive volunteers. Subjects had biopsies of the vastus lateralis muscle before and immediately after 30 min of either hyperinsulinemia (euglycemic insulin clamp) or moderate-intensity exercise on a cycle ergometer (approximately 60% of VO2max). Insulin receptor and IRS-1 tyrosine phosphorylation, association of the p85 regulatory subunit of PI 3-kinase with IRS-1, IRS-1 associated PI 3-kinase activity, and glycogen synthase activity were determined in muscle biopsy specimens taken from healthy subjects before and after insulin or exercise. Physiological hyperinsulinemia increased the rate of glucose disposal from 11.4 +/- 1.5 to 25.6 +/- 6.7 micromol x kg(-1) x min(-1) (P < 0.01), insulin receptor and IRS-1 tyrosine phosphorylation (173 +/- 19% and 159 +/- 35% of basal values, respectively, P < 0.05), association of the p85 regulatory subunit of PI 3-kinase with IRS-1 (159 +/- 10%, P < 0.05), and glycogen synthase fractional velocity (136 +/- 11%, P < 0.01). Exercise also increased glucose disposal, from 10.4 +/- 0.5 to 15.6 +/- 1.7 micromol x kg(-1) x min(-1) (P < 0.01) and glycogen synthase fractional velocity (253 +/- 35% of basal, P < 0.01). The exercise-induced increase in glycogen synthase was greater than that due to insulin (P < 0.05). In contrast to insulin, exercise decreased tyrosine phosphorylation of the insulin receptor to 72 +/- 10% of basal values (P < 0.05 vs basal and P < 0.05 vs insulin) and had no effect on IRS-1 tyrosine phosphorylation, or association of p85 with IRS-1. The exercise-induced decreased insulin receptor tyrosine phosphorylation could explain the well-known effect of exercise to enhance the sensitivity of muscle to insulin.
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    Quote Originally Posted by TheGame46
    Ok this gets you passed absorbtion. But synthesis takes a lot of energy. Would it not then benefit to have an excess of nutrient available?
    Who says there isn't? Amino acids are by FAR more important for protein synthesis.
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    Quote Originally Posted by Bobo
    Who says there isn't? Amino acids are by FAR more important for protein synthesis.
    Yes they are the bricks, but you have no mottar without readily available glucose and ATP. Peptide bonds dont form via fairy dust.
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    Quote Originally Posted by TheGame46
    Yes they are the bricks, but you have no mottar without readily available glucose and ATP. Peptide bonds dont form via fairy dust.
    What are you talking about?!?! Are we not eating?!?!?!
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    Quote Originally Posted by Bobo
    What are you talking about?!?! Are we not eating?!?!?!
    during ur workout prob not lol. And i know most not within 20 minutes after.

    This has gotten kind of off topic. Let me make a few closing remarks before I move on. PWO carbohydrates are going to benfit beyond that of upregulating insulin. It is going to help increase glucose uptake via glut4 and insulin mechanisms. Provide an anti catabolic environment. Provide ample energy for absorption and synthesis creating the optimal anabolic environment.

    You can argue the limitations of certain factors. But the bottom line is if there is a small benefit, its still a benefit. And when you combine every possible small token you can. that is when you acheive the optimum effect combined with amino acids and peptides.

    Keep in mind this is article is only on PWO. I will not argue that pre, and during workout amino acids and carbohydrates arnt benficial b/c they are very much so.
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    Quote Originally Posted by TheGame46
    during ur workout prob not lol. And i know most not within 20 minutes after.

    This has gotten kind of off topic. Let me make a few closing remarks before I move on. PWO carbohydrates are going to benfit beyond that of upregulating insulin. It is going to help increase glucose uptake via glut4 and insulin mehcanisms. Provide an anti catabolic environment. Provide ample energy for absorption and synthesis creating the optimal anabolic environment.

    You can argue the limitations of certain factors. But the bottom line is if there is a small benefit, its still a benefit. And when you combine every possible small token you can. that is when you acheive the optimum effect.

    Keep in mind this is article is only on PWO. I will not argue that pre, and during workout amino acids and carbohydrates arnt benficial b/c they are very much so.

    There is a concept that is called pre-during-post workout nutrition that almost eliminates any problems you can bring up.

    Exercise already increases glut4 receptors. I already covered that. Its like trying to kick in a door that already open. Its pointless. Increases energy demands increase nutrient uptake because it's a the natural response of the body to re-achieve homeostasis. You don't need to cram 50g of dextrose to achieve it. More is NOT better.

    The single most important aspect of post workout nutrition is amino acid availability. You don't need high GI carbs, you don't need large amount of carbs and all the research is finally concluding the same thing Tipton said years ago.

    Pretty much every benefit you can name is achieved with much less than what you prescribe or what most companies want you to believe. Instead of worrying about what effects certain macros have you should focus on the amounts needed to achieve it. More isn't better and there are plenty of insulin infusion studies out there that show this.
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    Quote Originally Posted by Bobo
    There is a concept that is called pre-during-post workout nutrition that almost eliminates any problems you can bring up.

    Exercise already increases glut4 receptors. I already covered that. Its like trying to kick in a door that already open. Its pointless. Increases energy demands increase nutrient uptake because it's a the natural response of the body to re-achieve homeostasis. You don't need to cram 50g of dextrose to achieve it. More is NOT better.

    The single most important aspect of post workout nutrition is amino acid availability. You don't need high GI carbs, you don't need large amount of carbs and all the research is finally concluding the same thing Tipton said years ago.

    Pretty much every benefit you can name is achieved with much less than what you prescribe or what most companies want you to believe. Instead of worrying about what effects certain macros have you should focus on the amounts needed to achieve it. More isn't better and there are plenty of insulin infusion studies out there that show this.
    Very well put. when I do my shakes pre mid post. I use about 25g dextrose through the whole thing vs when I cant I used about 40g at the end and then my post workout meal come a lil later b/c I am wating for the shake to digest.
    Unfortunantly this is the case a lot of the time for folks b/c you can't have a shake in the gym. When I'm lifting at a gym wiht lockers close by I will sip my shake on the way to gym, hit it in the locker about 20 minutes into it, and then when I'm done on. But I cant do that a lot of places.
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