Bulking diet, critique please

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  1. Bulking diet, critique please


    As a quick introduction before everyone starts ripping apart the flaws in my diet -- I'm a college student,
    so bear in mind that sometimes I have difficulty fitting in 8 meals a day, so I had to put together a diet
    that still meets my nutritional needs, but also affords me the time to go to a full time schedule's worth of
    classes and work in between. My stats are 20 years old, 5'11", 190 lbs, approx 9% BF, been lifting natural for about 8
    months. I drink about 1.5 gallons of water a day, supplement with a multi vitamin w/ b complex after I wake
    up and before I go to bed, flax and fish oil, and I try to take some vitamin c before workouts. Anyway I'm sure
    I'm leaving something out, so I'll just post the diet:

    [8:30 am] meal #1
    2 cups (measured uncooked) oats
    whey in milk (50g protein)

    [12:30 pm] meal #2
    turkey sandwich on whole wheat (40g protein)
    glass of skim milk

    [2:30-3:20 pm] lift

    [3:30 pm] meal #3 (post workout)
    whey shake in gatorade (100g dextrose, 50g protein)

    [4:30 pm] meal #4
    roast beef on whole wheat (40g protein)
    glass of skim milk

    [7:30 pm] meal #5
    *breaded chicken fingers (50g or more protein)

    [10:30 pm] meal #6
    whey in no fat no carb milk (50g protein)

    *yeah this meal is kind of difficult to avoid since no other dining halls are open. My only other option here would
    be a greasy calzone with little protein, fried chicken wings, or eating in (which I often do if I have clean food)

    Critique away


  2. for college that aint bad. how are you ding with fat gain? what do you think your body fat % is right now? i would try to switch out some of the bread with oatmeal. oatmeal is real cheap and all you need is hot water. for your post workout - i would cut the gatorade in half at least, if not totally switching it out for oatmeal. before bed, add some flax oil with that shake. whey digests very quickly, so if you can sub that out before bed with either cottage cheese or a slow digesting protein that would e great.
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  3. Quote Originally Posted by goldylight
    for college that aint bad. how are you ding with fat gain? what do you think your body fat % is right now? i would try to switch out some of the bread with oatmeal. oatmeal is real cheap and all you need is hot water. for your post workout - i would cut the gatorade in half at least, if not totally switching it out for oatmeal. before bed, add some flax oil with that shake. whey digests very quickly, so if you can sub that out before bed with either cottage cheese or a slow digesting protein that would e great.
    I gain fat pretty slowly on this diet, usually wont notice a fat increase for a few months. Completely drop gatorade (dextrose) from my post workout shake? Hmm I was always told that it was a critical part of a post workout drink. Any more opinions on this?

  4. yes there has been many debates on this topic at this very board. do a search for it - basically saying low gi will do exactly what you need for post workout without the sugar(sugar=fat).

  5. yeah but dextrose incurs a better/quicker insulin response needed for post workout needs..
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  6. btw looks like you need more cals..

  7. Quote Originally Posted by Kristopher
    yeah but dextrose incurs a better/quicker insulin response needed for post workout needs..
    Post workout "needs" do not require a fast insulin response.
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  8. tattoopierced1
    tattoopierced1's Avatar

    I would add something between meal 1 and meal 2 as well, possibly some turkey bacon for some quick protein and calories.

  9. Quote Originally Posted by Kristopher
    yeah but dextrose incurs a better/quicker insulin response needed for post workout needs..
    you be wrong brudda. especially if pre workout nutrition is up to par.

  10. how about some natty pb and a can of tuna in between meal 1 and 2

  11. Im still trying to figure out how you can stomach whey protein IN gatorade! yuck! Chocolate Tropical Punch!

  12. Quote Originally Posted by Edge
    Im still trying to figure out how you can stomach whey protein IN gatorade! yuck! Chocolate Tropical Punch!
    haha I'll eat / drink anything for gains. I used to drink egg beaters for breakfast until I got sick of them.

  13. natty pb is great for cals. puts too much fat on me personally. banannas are good too. van of tuna, few tbsp of pb and a banana and you are set. add cals whenever\wherever you can.

  14. another good thing for extra cals thats cheap is to try to down btw 1/2 a gallon and a gallon of skim milk if your stomach can handle it. its cheap and works great.

  15. Quote Originally Posted by goldylight
    another good thing for extra cals thats cheap is to try to down btw 1/2 a gallon and a gallon of skim milk if your stomach can handle it. its cheap and works great.
    \
    yeah I worked at a supermarket over the summer and I was drinking quarts of low carb milk everyday, definitely helped. should probably go pick up some skim too for morning hours.

  16. Quote Originally Posted by Bobo
    Post workout "needs" do not require a fast insulin response.
    Wrong. A fast insulin response is CRITICAL to growth, as exercise-induced GH release is very short-lived. He DOES want his GH turned into IGF-1, doesn't he?

  17. I suggest you do a bit more research.



    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.


    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. [email protected]

    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.

    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�min�minus�1�kg�m inus�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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  18. Quote Originally Posted by LunaHotel
    Wrong. A fast insulin response is CRITICAL to growth, as exercise-induced GH release is very short-lived. He DOES want his GH turned into IGF-1, doesn't he?
    GH secretions last up until 60 minutes post exercise. You know what diminishes GH? Insulin. GH is more lipolytic that anything.


    Effect of growth hormone treatment on hormonal parameters, body composition and strength in athletes.

    Deyssig R, Frisch H, Blum WF, Waldhor T.

    Department of Paediatrics, University of Vienna, Austria.

    The effect of recombinant GH on strength, body composition and endocrine parameters in power athletes was investigated in a controlled study. Twenty-two healthy, non-obese males (age 23.4 +/- 0.5 years; ideal body weight 122 +/- 3.1%, body fat 10.1 +/- 1.0%; mean +/- SEM) were included. Probands were assigned in a double-blind manner to either GH treatment (0.09U (kg BW)-1 day-1 sc) or placebo for a period of six weeks. To exclude concurrent treatment with androgenic-anabolic steroids urine specimens were tested at regular intervals for these substances. Serum was assayed for GH, IGF-I, IGF-binding proteins, insulin and thyroxine before the onset of the study and at two-weekly intervals thereafter. Maximal voluntary strength of the biceps and quadriceps muscles was measured on a strength training apparatus. Fat mass and lean body mass were derived from measurements of skinfolds at ten sites with a caliper. For final evaluation only data of those 8 and 10 subjects in the two groups who completed the study were analyzed. GH, IGF-I and IGF-binding protein were in the normal range before therapy and increased significantly in the GH-treated group. Fasting insulin concentrations increased insignificantly and thyroxine levels decreased significantly in the GH-treated probands. There was no effect of GH treatment on maximal strength during concentric contraction of the biceps and quadriceps muscles. Body weight and body fat were not changed significantly during treatment. We conclude that the anabolic, lipolytic effect of GH therapy in adults depends on the degree of fat mass and GH deficiency.(ABSTRACT TRUNCATED AT 250 WORDS)

    Also its not IGF-1 that contributes to increase muscle growth, it is MGF within localized skeletal muscle.
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  19. Might want to read this one too:


    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.
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  20. Forgot this one too:

    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.
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  21. Bobo, i may be wrong but does mean that it is better to not eat carbs before training?
    "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."

    That is what it sounds like to me but like i said i might be wrong.

    DEANO

  22. If the amount is great and the GI is high then yes you could have a negative result (think about taking in a lot of sugar then how you feel 45 minutes later). Thats why a low-mod GI is preferential because it controls blood glucose and insulin much better and will prevent any type of crash from the result of a large amount of high GI carbs.

    And remember the exercise that they are referring to is prolonged exaustive exercise. THe hormonal release is different for that type of exercise than resistant training. In fact it is much worse in terms of catabolic activity so this shows even when you are REALLY depleted the form of CHO really doesn't matter when it comes to glycogen resynthesis.


    Now the other studies show the results of short term recovery and the conlcusion is amino acids are MUCH more important the any physiological insulin release.

    Remember the primary role of insulin it to shuttle nutrients. It does this by increasing GLUT4 receptors and increasing cell permeability. Now during normal feeding patterns this is very true but during exercise the need for it minimal because exercise in itself does this all alone and much moreso than insulin, so there is need for a high spike and large amount at one given time. In fact the study even states the majority of glucose does not get shuttled to the exercised muscle BECAUSE of this.
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  23. That's all well and good, friend, but that's not what I am talking about. Your studies are of course correct, but miss the point completely.

    YOU do a little more research, because you don't seem to know that insulin being released WHILE GH IS HIGH makes the liver turn it into IGF-1 and is the only way to do so. Or maybe you don't know that IGF-1 is anabolic? Or maybe you don't know that weight training releases GH? Or maybe you don't know that glycogen sythesis, protein synthesis, satellite-cell hyperplasia, and merging of those cells are all PART of muscle growth but are NOT equivalent? I don't know which specific things of these you don't know, but do read up, please.

    I know it's not easy to be confronted with such a veritable behemoth of knowledge as I, but it was ever thus : destruction of beliefs causes great anguish, pain and protests. But in the end, whole truth in science prevails.

  24. Quote Originally Posted by LunaHotel
    That's all well and good, friend, but that's not what I am talking about. Your studies are of course correct, but miss the point completely.

    YOU do a little more research, because you don't seem to know that insulin being released WHILE GH IS HIGH makes the liver turn it into IGF-1 and is the only way to do so. Or maybe you don't know that IGF-1 is anabolic? Or maybe you don't know that weight training releases GH? Or maybe you don't know that glycogen sythesis, protein synthesis, satellite-cell hyperplasia, and merging of those cells are all PART of muscle growth but are NOT equivalent? I don't know which specific things of these you don't know, but do read up, please.

    I know it's not easy to be confronted with such a veritable behemoth of knowledge as I, but it was ever thus : destruction of beliefs causes great anguish, pain and protests. But in the end, whole truth in science prevails.

    Hey genius, maybe you should research a bit more because what happens when circulating hepatic IGF-1 is increased? IGFBP3 is increased rendering is USELESS. The body keeps a constant homeostasis between the GH/GF-1 axis. That is why rIGF-1 injected does not work much because the body counteracts it by increasing the binding protein. That is WHY Gropep introduced Long R3 IGF-1 BECAUSE it resists the IGFBP3.


    And this would be confirmed by this statement in a study which you obvisouly didn't read.

    "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."

    MGF causes the increases skleletal muscle not hepatic IGF-1 and this occurs over LONG peroids of time. I suggest you look up the effects of increasing eccentric time and MGF.


    So go hit the books again and stop repeating what every other message board says.
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  25. Quote Originally Posted by LunaHotel
    Or maybe you don't know that glycogen sythesis, protein synthesis, satellite-cell hyperplasia, and merging of those cells are all PART of muscle growth but are NOT equivalent? I don't know which specific things of these you don't know, but do read up, please.
    Satellite cell hypersplasia won't be much of a factor unless supraphysiolgical levels are given exogenously for long peroids of time. There is a reason why in vitro studies show different results than in vivo studies.

    I suggest you learn the difference.
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