Venom
01-12-2004, 02:36 AM
[ QUOTE ]
Okay, I'll post only the scince behind it
[/ QUOTE ]
Finally!
[ QUOTE ]
oatmeal will give you a significant insulin spike (maybe even more overrall) but in a more stable and longer lasting way.
[/ QUOTE ]
I seriously hope your joking. /forum/images/graemlins/crazy.gif
[ QUOTE ]
And before you say I recommened no insulin, which would be idiotic, oatmeal will give you a significant insulin spike (maybe even more overrall) but in a more stable and longer lasting way.
---
"There are some instances, however, where a food has a low glycemic value but a high insulin index
[/ QUOTE ]
Fair enough. Let’s take a look!
Oatmeal with a GI of 60 in the insulin index--40!
In contrast, white bread (which is as simple as you get) has a GI of 100 and an insulin index of 100.
Once again, you have proven nothing!
Oatmeal has an extremely low GI, and insulin index. And that was the instant kind! Pure oats is about 20 points below that. And I must again refer to my fiber article, concerning its effects on insulin:
[ QUOTE ]
Insulin sensitivity!
Insulin sensitivity is of great value to bodybuilders. Increased sensitivity promotes a much greater anabolic response to food consumption, while insulin resistance leads to elevated fat storage. In addition, insulin resistance can lead to the most common form of a disease, which inflicts more than 8 million people in the United States known as type 2-diabetes. With this in mind, it has been proven that fiber greatly enhances our bodies’ sensitivity to insulin. How this is achieved, will be shown subsequently. For more on the importance of insulin sensitivity, I refer to the following article, 13 Weeks To Hardcore Fat Burning - " The Diet "
But before we move on, lets discuss what diabetes is. Participants who became diabetic developed non-insulin dependent diabetes (also called adult-onset or type 2 diabetes), the most common form of the disease that afflicts 8 million people in the United States. High blood sugar (glucose) levels in type 2 diabetes results from [6,9]:
Decreased effect of insulin on peripheral tissue (insulin resistance),
Inadequate insulin production to control blood sugar (relative insulin deficiency).
A combined effect of the two. Diabetes occurs when the pancreas cannot produce sufficient insulin to manage blood glucose regulation.
Now, lets look how exactly fiber affects insulin production in the human body. To begin, for nutrients to be absorbed, they must move from the lumen (tube) of the small intestine through a glycoprotein water layer lying on top of the enterocytes (intestinal epithelium, which provides better absorption for intestines). The fiber-associated decreased diffusion rate of nutrients through this layer is probably due to an increased thickness of the unstirred water layer. In other words, the unstirred water layer becomes more resistant to nutrient movement, and without this movement nutrients cannot be absorbed into the enterocyte [12,24,25,26,31].
Another mechanism may also be responsible for decreased nutrient diffusion. Gums appear to slow glucose absorption by decreasing the convective movement of glucose within the intestinal lumen. Convective currents induced by peristaltic (wave like movements, caused by muscular contractions) movements are responsible for bringing nutrients from the lumen to the epithelial surface for absorption. Decreasing the solute movement also may help to explain the decreased absorption of amino acids and fatty acids caused by viscous fiber. Ingestion of viscous mucilaginous fibers such as guar gum, but also pectin and psyllium, have been shown to slow transit (transportation, moving through), delay glucose absorption, lower blood glucose concentrations, and affect hormonal response (such as insulin) to the absorbed nutrient. Such results are of great significance to warriors of the iron jungle. This shows that consuming dietary fiber, will promote a slow, and efficient nutrient absorption rate. Which in turn will resists high rapid bursts of insulin, which leads to fat storage, and resistance. This is also beneficial to individuals with diabetes mellitus and reduce postprandial blood glucose concentrations and insulin needs/response [31,35].
A possible explanation for a potential carbohydrate intake-diabetes link relates to the digestion rates of different carbohydrate sources. Low-fiber processed starches (and simple sugars in soft drinks) digest quickly and enter the blood at a relatively rapid rate (high glycemic index). Dietary fiber slows carbohydrate digestion, thus minimizing surges in blood glucose (in-effect lowering glycemic rate). The rapid increase in blood glucose that accompanies refined processed starch consumption (in contrast to the slow-release forms of high fiber, unrefined complex carbohydrates) increases insulin demand, stimulates overproduction of insulin by the pancreas, and accentuates hyperinsulinemial. Consistently eating such foods may eventually reduce the body's sensitivity to insulin (more resistant), thus requiring progressively greater insulin output to control blood sugar levels. Both bodybuilders, and diabetics would greatly benefit from fiber [35,36].
Here is a scary stat; about 25% of the population produces excessive insulin in response to rapidly absorbed carbohydrates. These insulin-resistant individuals may be at increased risk for obesity if they consistently eat carbohydrates that are absorbed rapidly. This increase in weight occurs because abnormal quantities of insulin facilitate glucose conversion to triglyceride (fat) by the liver, which then becomes stored as body fat in adipose tissue. If these observations prove correct, the obese are affected the most. This group shows the greatest insulin resistance and consequently, the greatest insulin response to a blood glucose challenge. Bodybuilders are not as prone to this disease; due to animalistic training sessions, and dedication to a strict diet. Nevertheless, consumption of fiber (especially if you have a family history for this disease) would help athletes avoid this. And as stated above, the anabolic results of muscular insulin sensitivity are invaluable [6].
Thus, To reduce the risks for type 2 diabetes and obesity, consumption of more slowly absorbed, unrefined complex carbohydrate foods (low glycemic index) provides a form of "slow-release" carbohydrate without producing rapid fluctuations in blood sugar. If rice, pasta, and bread remain the carbohydrate sources of choice, they should be consumed in unrefined form as brown rice and whole-grain pastas and breads, which contain higher contents of fiber. Such a dietary modification would greatly benefit bodybuilders, in their goal for obtaining freak, and maintaining a lean physique.
Dietary fiber also slows the rate of carbohydrate digestion causing slower absorption by the intestine. In addition, fiber may also decrease the total number of calories consumed in subsequent meals. Eating a fiber-rich breakfast, for example, decreased the total caloric intake during breakfast and a buffet-type lunch consumed 3.5 hours later. Dietary fiber also contains anabolic micronutrients, particularly magnesium, which may help to control insulin. Magnesium possibly increases the body's sensitivity to insulin, thus reducing the required level of insulin production [28,33,44].
There are many experiments, which show fiber enhances insulin sensitivity. Juntunen KS et al. has this to say [25], “High-fiber rye bread appears to enhance insulin secretion, possibly indicating improvement of b cell function.” McKeown NM et al. states [31], “The association between whole-grain intake and fasting insulin was attenuated after adjustment for dietary fiber and magnesium.” Concerning diabetes, Tabatabai A, Li S. from the results of several tests stated [26]:
“Dietary fiber shows promise in the management of type 2 DM. The inclusion of sufficient dietary fiber in a meal flattens the postprandial glycemic and insulinemic excursions and favorably influences plasma lipid levels in patients with type 2 DM. Water-soluble fiber appears to have a greater potential to reduce postprandial blood glucose, insulin, and serum lipid levels than insoluble fiber. Viscosity of the dietary fiber is important; the greater the viscosity, the greater the effect. Possible mechanisms for metabolic improvements with dietary fiber include delay of glucose absorption, increase in hepatic extraction of insulin, increased insulin sensitivity at the cellular level, and binding of bile acids. Patients with type 2 DM should increase their dietary fiber intake to 20 to 35 g/d and be aware of the considerations when increasing fiber intake.”
As stated above, magnesium shows great promise for improving insulin sensitivity. Here is a quote form Rodriguez-Moran M, and Guerrero-Romero F. on the results of there experiments [35].
”RESULTS:-At the end of the study, subjects who received magnesium supplementation showed significant higher serum magnesium concentration (0.74 +/- 0.10 vs. 0.65 +/- 0.07 mmol/l, P = 0.02) and lower HOMA-IR index (3.8 +/- 1.1 vs. 5.0 +/- 1.3, P = 0.005), fasting glucose levels (8.0 +/- 2.4 vs. 10.3 +/- 2.1 mmol/l, P = 0.01), and HbA(1c) (8.0 +/- 2.4 vs. 10.1 +/- 3.3%, P = 0.04) than control subjects. CONCLUSIONS:-Oral supplementation with MgCl(2) solution restores serum magnesium levels, improving insulin sensitivity and metabolic control in type 2 diabetic patients with decreased serum magnesium levels.”
Therefore, consuming fiber with starchy carbs such as bread, and having more fibrous sources of carbohydrates for instance oatmeal, will greatly reduce high insulin bursts, and promote more efficient use of this anabolic hormone [25,31,33,44].
[/ QUOTE ]
[ QUOTE ]
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.
[/ QUOTE ]
This is entirely false, and I saw no actually scientific study to support this claim, or a reference by this man, only a sentence stating so. Refer to the pre-contest article discussed in this thread.
[ QUOTE ]
THis is why it gets frustrating because I've already posted this yet people still insist insulin is the key, when every study published in the last 6 months say amino's play and much more important part than insulin.
[/ QUOTE ]
This is a complete strawmen. The fact that amino acids play a vital role in protein synthesis adds or subtractes nothing from the anabolism of insulin.
[ QUOTE ]
There was never an argument about High GI carbs being quicker than low GI carbs for glycogen resynthesis ; the argument was about protein synthesis .
[/ QUOTE ]
Let me end the argument then. Consider the following extensive study, which took all factors into account.
[ QUOTE ]
Insulin clearly stimulates skeletal muscle protein synthesis in vitro. Surprisingly, this effect has been difficult to reproduce in vivo. As in vitro studies have typically used much higher insulin concentrations than in vivo studies, we examined whether these concentration differences could explain the discrepancy between in vitro and in vivo observations. In 14 healthy volunteers, we raised forearm insulin concentrations 1,000-fold above basal levels while maintaining euglycemia for 4 h. Amino acids (AA) were given to either maintain basal arterial (n = 4) or venous plasma (n = 6) AA or increment arterial plasma AA by 100% (n = 4) in the forearm. We measured forearm muscle glucose, lactate, oxygen, phenylalanine balance, and [3H]phenylalanine kinetics at baseline and at 4 h of insulin infusion. Extreme hyperinsulinemia strongly reversed postabsorptive muscle's phenylalanine balance from a net release to an uptake (P < 0.001). This marked anabolic effect resulted from a dramatic stimulation of protein synthesis (P < 0.01) and a modest decline in protein degradation. Furthermore, this effect was seen even when basal arterial or venous aminoacidemia was maintained. With marked hyperinsulinemia, protein synthesis increased further when plasma AA concentrations were also increased (P < 0.05). Forearm blood flow rose at least twofold with the combined insulin and AA infusion (P < 0.01), and this was consistent in all groups. These results demonstrate an effect of high concentrations of insulin to markedly stimulate muscle protein synthesis in vivo in adults, even when AA concentrations are not increased. This is similar to prior in vitro reports but distinct from physiological hyperinsulinemia in vivo where stimulation of protein synthesis does not occur. Therefore, the current findings suggest that the differences in insulin concentrations used in prior studies may largely explain the previously reported discrepancy between insulin action on protein synthesis in adult muscle in vivo vs. in vitro.
[/ QUOTE ]
[ QUOTE ]
In this study, the very high insulin concentrations previously shown to stimulate adult skeletal muscle protein synthesis in vitro provoked a similar action in the adult human forearm in vivo. Protein synthesis was strongly stimulated when amino acids were infused at any of the three doses tested. At the lowest dose infused, arterial amino acid concentrations were not changed, but venous amino acid concentrations fell. The latter mimics the cellular concentrations (14), which might also be expected to fall. Despite this, protein synthesis rates doubled (Table 2 and Fig. 2). This contrasts to findings with physiological hyperinsulinemia and euaminoacidemia, which leaves forearm protein synthesis unchanged or even decreased (38, 41). High concentrations of insulin (>1,000 µU/ml) were also achieved in the study by Denne and colleagues (15). They observed that leg muscle proteolysis declined but saw no increase in protein synthesis. However, plasma amino acid concentrations were not maintained in that study, and the decline in amino acid concentrations with hyperinsulinemia may have obscured an effect.
In the present study, steady-state extreme hyperinsulinemia shifted forearm muscle phenylalanine balance from negative to strongly positive. This shift is more marked than reported with physiological hyperinsulinemia in human forearm or leg muscle, where insulin's inhibition of protein degradation accounted for the entire effect (21, 30, 38, 40, 41). In the forearm, raising insulin to four different levels throughout the physiological range (20-125 µU/ml) during euaminoacidemia shifted phenylalanine balance to modestly positive values (~10 nmol • min 1 • 100 ml 1) in all groups, suggesting a plateau effect of physiological hyperinsulinemia to retard proteolysis (38). The greater shift in the current study (even in groups 1 or 2 when plasma amino acid concentrations remained at basal) was primarily due to the marked stimulation of protein synthesis that was not previously seen at physiological insulin concentrations.
In only one human study was muscle protein synthesis reported to increase in response to physiological concentrations of insulin (9). In that study, protein synthesis was measured in leg muscle of six subjects, using both an arterial-venous difference method (as employed here) as well as a tissue biopsy technique. Good internal agreement was obtained between results seen with the arterial-venous difference method and the biopsy technique, both showing an enhancement of muscle protein synthesis by physiological hyperinsulinemia. Contrary to previous (6, 15, 30, 38, 41) or subsequent reports (21), the authors found no evidence for an effect of insulin to restrain proteolysis. No previous human limb balance study (including more than 60 subjects) has seen a stimulation of muscle protein synthesis by physiological hyperinsulinemia using the arterial-venous difference method (21, 27, 38, 41). Most have seen an effect of insulin on whole body and muscle proteolysis. In addition, other studies in both humans (40) and rodents (59) using muscle biopsies and estimating muscle protein synthesis using a variety of methods (including determining the labeling of the aminoacyl-tRNA) have also failed to show an effect of physiological hyperinsulinemia. Thus the results of Biolo and colleagues (9), although internally consistent, are divergent with all other in vivo studies, and we can not currently reconcile their unique findings.
The increases in protein synthesis seen with the higher rates of amino acid infusion (Figs. 2 and 3) indicate that raising plasma amino acid concentrations alone augments protein synthesis. This is in agreement with several previous human studies showing increased rates of whole body (10, 28) or skeletal muscle (7, 8, 46) protein synthesis in response to raised amino acid concentrations with or without added insulin. As these studies augmented amino acid concentrations simultaneously with physiological hyperinsulinemia, it was not possible to assess whether insulin had an independent effect from that of amino acids. We subsequently addressed this experimentally using a double forearm cannulation method. We observed that superimposing local, physiological hyperinsulinemia in one forearm during systemic amino acid infusion did not further stimulate muscle protein synthesis in the insulin-infused arm (21). The amino acid infusion rate (0.015 ml • min 1 • kg 1) in that study was the same as the highest dose used in the present study, and the arterial phenylalanine concentrations were higher than in the present study (113 ± 4 vs. 80 ± 7 µM; see Fig. 3). Therefore, the stimulation of protein synthesis to 90-150% above basal rates with marked hyperinsulinemia in the present study both under basal and hyperaminoacidemic conditions suggests that marked hyperinsulinemia has an effect separate from that of amino acids.
Protein degradation declined modestly in each of the three study groups in the current study (Fig. 2). This change (~20% decline overall) was statistically significant when observations for all three groups were pooled. In the previous human forearm studies, insulin was found to retard proteolysis by 25-40%. As proteolysis is estimated from the dilution of phenylalanine specific activity across the muscle bed, the high blood flows (vide infra) seen during the very high insulin infusion used here likely added variability to this measurement. That protein synthesis, the primary outcome variable, and net phenylalanine balance were significantly stimulated in each of the three study groups attests to a quantitatively greater (~100%) effect on synthesis with the use of high insulin concentrations.
Although the relative change in protein kinetics was similar in all three groups in the current study, the absolute rates of basal protein synthesis and degradation were lower in the 0.004 ml • min 1 • kg 1 group. Gender differences could partially explain this, as all four subjects were female in the 0.004 group, whereas the 0.007 and 0.015 ml • min 1 • kg 1 groups had a mix of male and female subjects.1 However, each subject was compared with his/her own baseline value, and a consistent and significant effect on protein synthesis was still observed in all three groups. If anything, our results may underestimate the effect of marked hyperinsulinemia to stimulate protein synthesis with euaminoacidemic conditions because of the large proportion of females in two of the groups.
It has been suggested that a stimulation of protein synthesis in vivo has been difficult to demonstrate in humans because basal insulin has already maximally stimulated protein synthesis. Three observations suggest that this may not be the case. First, in the current study, very high insulin concentrations do further stimulate protein synthesis. Second, as infusion of growth hormone (20) or of insulin-like growth factor I (IGF-I; see Refs. 19 and 21) acutely increases forearm muscle protein synthesis, synthesis rates are clearly not at a maximum. Third, in studies of insulin-deficient diabetic humans, acute replacement of insulin did not increase whole body or muscle protein synthesis (44, 47). Collectively, these data suggest that physiological increments in insulin do not augment bulk protein synthesis in humans.
In insulin-withdrawn streptozotocin diabetic rats, replacement of insulin rapidly restores protein synthetic rates in both heart and skeletal muscle (1, 2). Before treatment, these animals are severely catabolic (insulin withdrawn for up to 5 days), and it is quite possible that restoring basal insulin does affect protein synthesis in this setting. This may be a direct effect of insulin or an indirect effect achieved by restoring sensitivity to other growth factors such as IGF-I (31).
Marked hyperinsulinemia combined with amino acid infusion stimulated blood flow more than twofold (100-160%) in each of the three groups in the current study. Both insulin (4) and amino acids likely contributed to this, as generalized hyperaminoacidemia (21) or infusion of arginine (29) increases forearm blood flow. Importantly, physiological hyperinsulinemia in the presence of hyperaminoacidemia does not stimulate blood flow more than hyperaminoacidemia alone (21).
The reported stimulation of limb blood flow with physiological hyperinsulinemia ranges from 10 to 125% (5, 13, 30, 36, 38, 45, 52, 54). This variability involves many factors such as insulin infusion (local vs. systemic and single dose vs. sequential increments in insulin infusion dose), methodology (capacitance plethysmography vs. thermodilution used as well as variability between laboratories in employing a particular method), locale (forearm vs. leg), and muscle content of the limb studied (4, 54). Most studies reporting a stimulation of blood flow above 50% with physiological hyperinsulinemia have used a sequential increase of insulin infusion in the same subject (5, 36, 52).
As our previous studies have extensively used the same procedure of capacitance plethysmography in the forearm, it seems most logical to contrast our current blood flow results with our past results. We previously observed that insulin at five different concentrations within the physiological range did not stimulate blood flow >25%, and this was only in the high physiological range (27). Additionally, we studied the effects of hyperaminoacidemia (0.015 ml • kg 1 • min 1 balanced amino acid infusion) with or without insulin on forearm flow. Physiological hyperinsulinemia did not stimulate blood flow beyond hyperaminoacidemia alone. Of interest, in that study and several others, we noted that local IGF-I strongly stimulated flow when amino acids were elevated or remained at basal levels (21). Thus the two- to threefold stimulation of blood flow in the current study with extreme hyperinsulinemia even when amino acids remained at basal levels is unlike physiological hyperinsulinemia and similar to flow changes provoked by local forearm IGF-I infusion (19, 21).
The stimulation of protein synthesis in the current study is consistent with previous in vitro studies of isolated muscle incubated with insulin at high concentrations. As comparable effects of insulin have generally not been seen in vivo with physiological insulin concentrations (27, 30, 38, 41, 40, 59), our results suggest that very high insulin concentrations may be required. An exception is in young rats in which in vivo studies have demonstrated a stimulatory action of physiological insulin concentrations on muscle protein synthesis (25, 26). However, these effects are not seen in older animals (3, 11, 39) or, with one exception (9), in adult humans. Thus the muscle's sensitivity to insulin's stimulatory action on protein synthesis may decline with aging.
In the current study, the effects of extreme hyperinsulinemia to stimulate protein synthesis, enhance oxygen consumption, markedly increase blood flow, and induce a strongly positive phenylalanine balance are each similar to the actions of locally infused IGF-I in human forearm (19, 21) and differ from the effects seen with physiological hyperinsulinemia concentrations (27, 30, 38, 41). As the insulin concentrations achieved in the current study were 4-7 × 10 8 M (100-fold above the physiological range), stimulation of the IGF-I receptor by insulin is entirely plausible [dissociation constant (Kd) of insulin for the IGF-I receptor ~10 8 compared with Kd 10 10 for IGF-I (58)]. Furthermore, as the mitogenic effect of insulin (10 6) in vitro is mediated via the IGF-I receptor rather than the insulin receptor (55), an analogous effect with protein synthesis is possible. If this is the case, our results introduce a necessary caution to the interpretation of the many in vitro studies documenting an effect of high concentrations of insulin to increase bulk protein synthesis in adult animals (see Refs. 31 and 35 for reviews). With few exceptions (18, 50, 51), the insulin concentrations used in these studies (generally 2 mU/ml) are in a range in which effects of insulin mediated by the IGF-I receptor or hybrid IGF-I/insulin receptors (48, 49) could complicate data interpretation. As the current study's aim was only to determine if extreme hyperinsulinemia could reproduce in vivo the stimulation of protein synthesis seen with similar concentrations in vitro, further research is needed to elucidate if protein synthesis is indeed being stimulated via IGF-I signaling pathways.
In summary, these results indicate that insulin at high concentrations strongly stimulates muscle protein synthesis in the human forearm. This effect is quite consistent with the action of insulin described in a number of in vitro studies using similar concentrations of insulin but distinct from what is observed with physiological hyperinsulinemia. Therefore, much of the discrepancy previously reported between insulin action on protein synthesis in vivo vs. in vitro may result directly from differences in insulin concentrations used. In addition to stimulating protein synthesis, high-dose insulin resembles the action of IGF-I observed previously (19, 21). As IGF-I receptors can be stimulated by high concentrations of insulin, the present results together with findings from in vitro studies raise the possibility that some or all of insulin's action to stimulate protein synthesis may be mediated by pathways other than the insulin receptor.
[/ QUOTE ]
Note that this was in 'Vivo' and demonstrated that high insulin levels were needed to get the job done.
And here are some references to keep your buddies busy (there are plenty more if needed):
1. Ashford, A. J., and V. M. Pain. Effect of diabetes on the rates of synthesis and degradation of ribosomes in rat muscle and liver in vivo. J. Biol. Chem. 261: 4059-4065, 1986[Abstract/Free Full Text].
2. Ashford, A. J., and V. M. Pain. Insulin stimulation of growth in diabetic rats: synthesis and degradation of ribosomes and total tissue protein in skeletal muscle and heart. J. Biol. Chem. 261: 4066-4070, 1986[Abstract/Free Full Text].
3. Baillie, A. G. S., and P. J. Garlick. Attenuated responses of muscle protein synthesis to fasting and insulin in adult female rats. Am. J. Physiol. 262 (Endocrinol. Metab. 25): E1-E5, 1992[Abstract/Free Full Text].
4. Baron, A. D. Hemodynamic actions of insulin. Am. J. Physiol. 267 (Endocrinol. Metab. 30): E187-E202, 1994[Abstract/Free Full Text].
5. Baron, A. D., H. O. Steinberg, H. Chaker, R. Leaming, A. Johnson, and G. Brechtel. Insulin-mediated vasodilation contributes to both insulin sensitivity and responsiveness in lean humans. J. Clin. Invest. 96: 786-792, 1995[Medline].
6. Barrett, E. J., J. H. Revkin, L. H. Young, B. L. Zaret, R. Jacob, and R. A. Gelfand. An isotopic method for in vivo measurement of muscle protein synthesis and degradation. Biochem. J. 245: 223-228, 1987[Medline].
7. Bennet, W. M., A. A. Connacher, C. M. Scrimgeour, R. T. Jung, and M. J. Rennie. Euglycemic hyperinsulinemia augments amino acid uptake by leg tissues during hyperaminoacidemia. Am. J. Physiol. 259 (Endocrinol. Metab. 22): E185-E194, 1990[Abstract/Free Full Text].
8. Bennet, W. M., A. A. Connacher, C. M. Scrimgeour, and M. J. Rennie. The effect of amino-acid infusion on leg protein turnover assessed by L-[15N]phenylalanine and L-[1-13C]leucine exchange. Eur. J. Clin. Invest. 20: 37-46, 1990.
9. Biolo, G., R. Y. D. Fleming, and R. R. Wolfe. Physiologic hyperinsulinemia stimulates protein synthesis and enhances transport of selected amino acids in human skeletal muscle. J. Clin. Invest. 95: 811-819, 1995[Medline].
10. Castellino, P., L. Luzi, D. C. Simonson, M. Haymond, and R. A. DeFronzo. Effect of insulin and plasma amino acid concentrations on leucine metabolism in man. J. Clin. Invest. 80: 1784-1793, 1987[Medline].
11. Dardevet, D., C. Sornet, D. Attaix, V. E. Baracos, and J. Grizard. Insulin-like growth factor-I and insulin resistance in skeletal muscle of adult and old rats. Endocrinology 134: 1475-1484, 1994[Abstract].
12. DeFronzo, R. A., J. D. Tobin, and R. Andres. Glucose clamp technique, a method for quantifying insulin secretion and resistance. Am. J. Physiol. 237 (Endocrinol. Metab. Gastrointest. Physiol. 6): E214-E223, 1979.
13. De Haan, C. H. A., F. M. H. van Dielen, A. J. H. M. Houben, P. W. de Leeuw, F. C. Huvers, J. G. R. De Mey, B. H. R. Wolffenbuttel, and N. C. Schaper. Peripheral blood flow and noradrenaline responsiveness: the effect of physiologic hyperinsulinemia. Cardiovasc. Res. 34: 192-198, 1997[Medline].
14. Del Prato, S., R. DeFronzo, P. Castellino, J. Wahren, and A. Alvestrand. Regulation of amino acid metabolism by epinephrine. Am. J. Physiol. 258 (Endocrinol. Metab. 21): E878-E887, 1990[Abstract/Free Full Text].
15. Denne, S. C., E. A. Liechty, Y. M. Liu, G. Brechtel, and A. D. Baron. Proteolysis in skeletal muscle and whole body in response to euglycemic hyperinsulinemia in normal adults. Am. J. Physiol. 261 (Endocrinol. Metab. 24): E809-E814, 1991[Abstract/Free Full Text].
16. Flakoll, P. J., M. Kulaylat, M. Frexes-Steed, H. Hourani, L. L. Brown, J. O. Hill, and N. N. Abumrad. Amino acids augment insulin's suppression of whole body proteolysis. Am. J. Physiol. 257 (Endocrinol. Metab. 20): E839-E847, 1989[Abstract/Free Full Text].
17. Fluckey, J. D., T. C. Vary, L. S. Jefferson, W. J. Evans, and P. A. Farrell. Insulin stimulation of protein synthesis in rat skeletal muscle following resistance exercise is maintained with advancing age. J. Gerontol. B Psychol. Sci. Soc. Sci. 51: B323-B330, 1996.
18. Frayn, K. N., and P. F. May****. Regulation of protein metabolism by a physiological concentration of insulin in mouse soleus and extensor digitorum longus muscles. Biochem. J. 184: 323-330, 1979[Medline].
19. Fryburg, D. A. Insulin-like growth factor I exerts growth hormone- and insulin-like actions on human muscle protein metabolism. Am. J. Physiol. 267 (Endocrinol. Metab. 30): E331-E336, 1994[Abstract/Free Full Text].
20. Fryburg, D. A., R. A. Gelfand, and E. J. Barrett. Growth hormone acutely stimulates muscle protein synthesis in normal humans. Am. J. Physiol. 260 (Endocrinol. Metab. 23): E499-E504, 1991[Abstract/Free Full Text].
21. Fryburg, D. A., L. A. Jahn, S. A. Hill, D. M. Oliveras, and E. J. Barrett. Insulin and insulin-like growth factor-I enhance human skeletal muscle protein anabolism during hyperaminoacidemia by different mechanisms. J. Clin. Invest. 96: 1722-1729, 1995[Medline].
22. Fukagawa, N. K., K. L. Minaker, J. W. Rowe, M. N. Googman, D. W. Matthews, D. M. Bier, and V. R. Young. Insulin-mediated reduction of whole body protein breakdown: dose-response effects on leucine metabolism in postabsorptive man. J. Clin. Invest. 76: 2306-2311, 1985[Medline].
23. Fukagawa, N. K., K. L. Minaker, V. R. Young, and J. W. Rowe. Insulin dose-dependent reductions in plasma amino acids in man. Am. J. Physiol. 250 (Endocrinol. Metab. 13): E13-E17, 1986[Abstract/Free Full Text].
24. Fulks, R. M., J. B. Li, and A. L. Goldberg. Effects of insulin, glucose, amino acids on protein turnover in rat diaphragm. J. Biol. Chem. 250: 290-298, 1975[Abstract].
25. Garlick, P. J., and I. Grant. Amino acid infusion increases the sensitivity of muscle protein synthesis in vivo to insulin. Biochem. J. 254: 579-584, 1988[Medline].
26. Garlick, P. J., V. R. Preedy, and P. J. Reeds. Regulation of protein turnover in vivo by insulin and amino acids. In: Intracellular Protein Catabolism, edited by E. A. Khairallah, J. S. Bond, and J. W. C. Bird. New York: Liss, 1985, p. 555-564.
27. Gelfand, R. A., and E. J. Barrett. Effect of physiologic hyperinsulinemia on skeletal muscle protein synthesis and breakdown in man. J. Clin. Invest. 80: 1-6, 1987[Medline].
28. Gelfand, R. A., M. G. Glickman, R. Jacob, R. S. Sherwin, and R. A. DeFronzo. Removal of infused amino acids by splanchnic leg tissues in man. Am. J. Physiol. 250 (Endocrinol. Metab. 13): E407-E413, 1986[Abstract/Free Full Text].
29. Giugliano, D., R. Marfella, G. Verrazzo, R. Acampora, L. Coppola, D. Cozzolino, and F. D'Onofrio. The vascular effects of L-arginine in humans: the role of endogenous insulin. J. Clin. Invest. 99: 433-438, 1997[Abstract/Free Full Text].
30. Heslin, M. J., E. Newman, R. F. Wolf, P. W. T. Pisters, and M. F. Brennan. Effect of hyperinsulinemia on whole body and skeletal muscle leucine carbon kinetics in humans. Am. J. Physiol. 262 (Endocrinol. Metab. 25): E911-E918, 1992[Abstract/Free Full Text].
31. Jacob, R., X. Hu, D. Niederstock, S. Hasan, P. H. McNulty, R. S. Sherwin, and L. H. Young. IGF-I stimulation of muscle protein synthesis in the awake rat: permissive role of insulin and amino acids. Am. J. Physiol. 270 (Endocrinol. Metab. 33): E60-E66, 1996[Abstract/Free Full Text].
31a. Jahn, L. A., E. J. Barrett, T. Spraggins, M. Genco, L. Im, and D. A. Fryburg. Effect of gender on forearm muscle metabolism (Abstract). Med. Sci. Sports Exercise, Suppl. 5: 93, 1997.
32. Jefferson, L. S., J. O. Koehler, and H. E. Morgan. Effect of insulin on protein synthesis in skeletal muscle of an isolated perfused preparation of rat hemicorpus. Proc. Natl. Acad. Sci. USA 69: 816-820, 1972[Medline].
33. Jefferson, L. S., J. B. Li, and S. R. Rannels. Regulation by insulin of amino acid release and protein turnover in the perfused rat hemicorpus. J. Biol. Chem. 252: 1476-1483, 1977[Abstract].
34. Karinch, A. M., S. R. Kimball, T. C. Vary, and L. S. Jefferson. Regulation of eukaryotic initiation factor-2B activity in muscle of diabetic rats. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E101-E108, 1993[Abstract/Free Full Text].
35. Kimball, S. R., T. C. Vary, and L. S. Jefferson. Regulation of protein synthesis by insulin. Annu. Rev. Physiol. 56: 321-348, 1994[Medline].
36. Laasko, M., S. V. Edelman, G. Brechtel, and A. D. Baron. Decreased effect of insulin to stimulate skeletal muscle blood flow in obese man. J. Clin. Invest. 85: 1844-1852, 1990[Medline].
37. Lin, T. A., X. Kong, T. A. J. Haystead, P. Arnim, G. Belsham, N. Sonenberg, and J. C. Lawrence. PHAS-1 as a link between mitogen-activated protein kinase and translation initiation. Science 266: 653-656, 1994[Medline].
38. Louard, R. J., D. A. Fryburg, R. A. Gelfand, and E. J. Barrett. Insulin sensitivity of protein and glucose metabolism in human forearm skeletal muscle. J. Clin. Invest. 90: 2348-2354, 1992[Medline].
39. McNulty, P. H., L. H. Young, and E. J. Barrett. Response of rat heart and skeletal muscle protein in vivo to insulin and amino acid infusion. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E958-E965, 1993[Abstract/Free Full Text].
40. McNurlan, M. A., P. Essen, A. Thorell, A. G. Calder, S. E. Anderson, O. Ljungquist, A. Sandgren, I. Grant, I. Thader, P. E. Ballmer, J. Wernerman, and P. J. Garlick. Response of protein synthesis in human skeletal muscle to insulin: an investigation with L-[2H5]phenylalanine. Am. J. Physiol. 267 (Endocrinol. Metab. 30): E102-E108, 1994[Abstract/Free Full Text].
41. Moller-Loswick, A. C., H. Zachrisson, A. Hyltander, U. Korner, D. E. Matthews, and K. Lundholm. Insulin selectively attenuates breakdown of nonmyofibrillar proteins in peripheral tissues of normal men. Am. J. Physiol. 266 (Endocrinol. Metab. 29): E645-E652, 1994[Abstract/Free Full Text].
42. Morgan, H. E., L. S. Jefferson, E. B. Wolpert, and D. E. Rannels. Regulation of protein synthesis in heart muscle. II. Effect of amino acid levels and insulin on ribosomal aggregation. J. Biol. Chem. 246: 2163-2170, 1971[Abstract/Free Full Text].
43. Mosoni, L., M. Houlier, P. P. Mirand, G. Bayle, and J. Grizard. Effect of amino acids alone or with insulin on muscle and liver protein synthesis in adult and old rats. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E614-E620, 1993[Abstract/Free Full Text].
44. Nair, K. S., G. C. Ford, and D. Halliday. Effect of intravenous insulin treatment on in vivo whole body leucine kinetics and oxygen consumption in insulin-deprived type I diabetic patients. Metabolism 36: 491-495, 1987[Medline].
45. Natali, A., G. Buzzigoli, S. Taddei, D. Santoro, M. Cerri, P. Pedrinelli, and E. Ferrannini. Effects of insulin on hemodynamics and metabolism in human forearm. Diabetes 39: 490-500, 1990[Abstract].
46. Newman, E., M. J. Heslin, R. F. Wolf, P. T. W. Pisters, and M. F. Brennan. The effect of systemic hyperinsulinemia with concomitant infusion of amino acids on skeletal muscle protein turnover in the human forearm. Metabolism 43: 70-78, 1994[Medline].
47. Pacy, P. J., K. S. Nair, C. Ford, and D. Halliday. Failure of insulin infusion to stimulate fractional muscle protein synthesis in type I diabetic patients. Diabetes 338: 618-624, 1989.
48. Pessin, J. E., and A. L. Frattali. Molecular dynamics of insulin/IGF-I receptor transmembrane signaling. Mol. Reprod. Dev. 35: 339-345, 1993[Medline].
49. Pessin, J. E., and A. L. Frattali. Structure-function properties of insulin/IGF-I hybrid receptors. In: Molecular Biology of Diabetes, edited by D. LeRoith, and B. Draznin. Totowa, NJ: Humana, 1994, pt. II, p. 413-426.
50. Stirewalt, W. S., R. B. Low, and J. M. Slaiby. Insulin sensitivity and responsiveness of epitrochlearis and soleus muscles from fed and starved rats. Biochem. J. 227: 355-362, 1985[Medline].
51. Sugden, P. H., and S. J. Fuller. Regulation of protein turnover in skeletal and cardiac muscle. Biochem. J. 273: 21-37, 1991[Medline].
52. Tack, C. J. J., A. E. P. Schefman, J. L. Willems, T. Thien, J. A. Lutterman, and P. Smits. Direct vasodilator effects of physiological hyperinsulinemia in human skeletal muscle. Eur. J. Clin. Invest. 26: 772-778, 1996[Medline].
53. Tessari, P., R. Trevisan, S. Inchiostro, G. Bioli, R. Nosadini, S. V. De Kreutzenberg, E. Duner, A. Tiengo, and G. Crepaldi. Dose-response curves of effects of insulin on leucine kinetics in humans. Am. J. Physiol. 251 (Endocrinol. Metab. 14): E334-E342, 1986[Abstract/Free Full Text].
54. Utriainen, T., R. Malmstrom, S. Makimattila, and H. Yki-Jarvinen. Methodological aspects, dose-response characteristics and causes of interindividual variation in insulin stimulation of limb blood flow in normal subjects. Diabetologia 38: 555-564, 1995[Medline].
55. Van Wyk, J., D. Graves, S. Casella, and S. Jacobs. Evidence from monoclonal antibody studies that insulin stimulates deoxyribonucleic acid synthesis through the type I somatomedin receptor. J. Clin. Endocrinol. Metab. 61: 639-643, 1985[Abstract].
56. Watt, P., Y. Lindsay, C. Scrimgeour, P. Chien, J. Gibson, D. Taylor, and M. Rennie. Isolation of aminoacyl-tRNA and its labeling with stable-isotope tracers, use in studies of human tissue protein synthesis. Proc. Natl. Acad. Sci. USA 88: 5892-5896, 1991[Abstract].
57. Watt, P. W., M. E. Corbett, and M. J. Rennie. Stimulation of protein synthesis in pig skeletal muscle by infusion of amino acids during constant insulin availability. Am. J. Physiol. 263 (Endocrinol. Metab. 26): E453-E460, 1992[Abstract/Free Full Text].
58. Werner, H., D. Beitner-Johnson, C. T. Roberts, and D. LeRoith. Molecular comparisons of the insulin and IGF-I receptors. In: Molecular Biology of Diabetes, edited by B. Draznin, and D. LeRoith. Totowa, NJ: Humana, 1994, pt. II, p. 377-392.
59. Young, L. H., W. Stirewalt, P. H. McNulty, J. H. Revkin, and E. J. Barrett. Effect of insulin on rat heart and skeletal muscle phenylalanyl-tRNA labeling and protein synthesis in vivo. Am. J. Physiol. 267 (Endocrinol. Metab. 30): E337-E342, 1994[Abstract/Free Full Text].
vBulletin® v3.7.2, Copyright ©2000-2013, Jelsoft Enterprises Ltd.