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Thread: new PWO ideas
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01-12-2006, 04:34 PM #41Originally Posted by jdh
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01-12-2006, 05:05 PM #42AR Hall of Fame
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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
(One reason BB'ers shoot slin PWO and use high gi carbs)
~SC~
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01-12-2006, 05:12 PM #43Originally Posted by SwoleCat
Last edited by Giantz11; 01-12-2006 at 05:14 PM.
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01-12-2006, 05:26 PM #44
I think this study giantz sent me today can clear that upp decently. Most of insulins anabolic effects is its ability to shut down degradation of protein and the body is very sensitive to that effect and it peaks out quickly.
Insulin sensitivity of protein and glucose metabolism in human forearm skeletal muscle.
Louard RJ, Fryburg DA, Gelfand RA, Barrett EJ.
Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06510.
Physiologic increases of insulin promote net amino acid uptake and protein anabolism in forearm skeletal muscle by restraining protein degradation. The sensitivity of this process to insulin is not known. Using the forearm perfusion method, we infused insulin locally in the brachial artery at rates of 0.00 (s****e control), 0.01, 0.02, 0.035, or 0.05 mU/min per kg for 150 min to increase local forearm plasma insulin concentration by 0, approximately 20, approximately 35, approximately 60, and approximately 120 microU/ml (n = 35). L-[ring-2,6-3H]phenylalanine and L-[1-14C]leucine were infused systemically, and the net forearm balance, rate of appearance (Ra) and rate of disposal (R(d)) of phenylalanine and leucine, and forearm glucose balance were measured basally and in response to insulin infusion. Compared to s****e, increasing rates of insulin infusion progressively increased net forearm glucose uptake from 0.9 mumol/min per 100 ml (s****e) to 1.0, 1.8, 2.4, and 4.7 mumol/min per 100 ml forearm, respectively. Net forearm balance for phenylalanine and leucine was significantly less negative than basal (P < 0.01 for each) in response to the lowest dose insulin infusion, 0.01 mU/min per kg, and all higher rates of insulin infusion. Phenylalanine and leucine R(a) declined by approximately 38 and 40% with the lowest dose insulin infusion. Higher doses of insulin produced no greater effect (decline in R(a) varied between 26 and 42% for phenylalanine and 30-50% for leucine). In contrast, R(d) for phenylalanine and leucine did not change with insulin. We conclude that even modest increases of plasma insulin can markedly suppress proteolysis, measured by phenylalanine R(a), in human forearm skeletal muscle. Further increments of insulin within the physiologic range augment glucose uptake but have little additional effect on phenylalanine R(a) or balance. These results suggest that proteolysis in human skeletal muscle is more sensitive than glucose uptake to physiologic increments in insulin
Exercise Effects on Muscle Insulin Sign****g 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.Last edited by Kärnfysikern; 01-12-2006 at 05:30 PM.
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01-12-2006, 06:54 PM #45AR Hall of Fame
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Originally Posted by johan
True they use GH as well w/all kinds of anabolics, but slin does make a significant difference in the size of a professional bodybuilder.
~SC~
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01-12-2006, 10:27 PM #46Originally Posted by SwoleCat
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01-13-2006, 06:48 AM #47
Has a pretty intense chest/tri w/o yesterday. Had a premeal of 1 cup oats, 1 scoop of whey about 330......trained at 5-630. Skipped my shake (anxiety set in big time) and went home. Finally ate at 730 4 pieces of ww, eggs, salad and then had a muscle milk prebed about 9:15..........I feel ok now, but we'll see tonight for back/bis.....deads....thats when I feel the lack of throttle.
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01-13-2006, 11:04 AM #48Originally Posted by Giantz11
yeah gosh swolecat you are breaking all the rules!
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