Dat's - CJC-1295 & GHRP-6 (Basic Guides)

DatBtrue · Mar 24, 2009

Once again I'm really enjoying your post.

BigTex; said:
However,, there is still considerable evidence to support recommendations that athletes should ingest CHO and PRO following exercise in order to optimize glycogen resynthesis, promote an anabolic hormonal environment, and increase PRO synthesis [1-5]. Further, CHO and PRO ingestion following exercise significantly influences glucose and insulin responses without significantly altering markers of anabolism, catabolism or immunity during the first two hours of recovery [1-5]. Granted all of these studies were done without the aid synthetic HGH, peptides or AAS.

...

* 3. Tipton KD, Rasmussen BB, Miller SL, Wolf SE, Owens-Stovall SK, Petrini BE, Wolfe RR, Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise, Am J Physiol Endocrinol Metab 2001, 281(2):E197-206.

What you didn't think I wasn't going to spot check your references by pulling them and reading them?

This Tipton study * is a good one but doesn't support what you claim...i.e. the superiority of ingesting post-exercise.

In fact the conclusion is just the opposite... that ingestion needs to occur BEFORE and during as well.

QUOTES:

From the INTRO

During an exercise bout, there may be a net loss of muscle protein, because protein synthesis is either decreased (8) or unchanged (9), whereas protein breakdown is generally considered to be elevated (22). Although muscle protein synthesis is increased after exercise, it appears that this response is not stimulated until some time after the exercise bout (17). Hyperaminoacidemia from ingestion of amino acids during the exercise bout, as opposed to after exercise, may counter the net loss of muscle protein, thereby creating a more favorable situation for muscle growth. The purpose of the present study was to determine whether ingesting a combination of amino acid and carbohydrate before exercise is more effective in stimulating net muscle protein synthesis than ingesting the mixture after exercise.

ABSTRACT CONCLUSION

These results indicate that the response of net muscle protein synthesis to consumption of an EAC solution immediately before resistance exercise is greater than that when the solution is consumed after exercise, primarily because of an increase in muscle protein synthesis as a result of increased delivery of amino acids to the leg.

FULL TEXT CONCLUSION

The stimulation of net muscle protein synthesis when EAC is consumed before exercise is superior to that when EAC is consumed after exercise. The combination of increased amino acid levels at a time when blood flow is increased appears to offer the maximum stimulation of muscle protein synthesis by increasing amino acid delivery to the muscle and thus amino acid availability.

DatBtrue · Mar 24, 2009

Here is a study you missed BT which found increased muscle protein synthesis (in a fed state) only when carbs & protein were taken in during exercise.

Coingestion of Carbohydrate and Protein Hydrolysate Stimulates Muscle Protein Synthesis during Exercise in Young Men, with No Further Increase during Subsequent Overnight Recovery, Milou Beelen, Journal of Nutrition Vol. 138, No. 11, 2198-2204, November 2008

We conclude that, even in a fed state, protein and carbohydrate supplementation stimulates muscle protein synthesis during exercise. Ingestion of protein with carbohydrate during and immediately after exercise improves whole-body protein synthesis but does not further augment muscle protein synthesis rates during 9 h of subsequent overnight recovery.

BigTex · Mar 24, 2009

DatBtrue said:
Once again I'm really enjoying your post.

Thanks! I have really enjoyed being challenged to find the studies.

What you didn't think I wasn't going to spot check your references by pulling them and reading them?

Actually I am flattered.

This Tipton study * is a good one but doesn't support what you claim...i.e. the superiority of ingesting post-exercise.

In fact the conclusion is just the opposite... that ingestion needs to occur BEFORE and during as well.

I agree, there seems to be evidence that post-exercise ingestions is good but pre-, during and post- are best.

DatBtrue said:
Here is a study you missed BT which found increased muscle protein synthesis (in a fed state) only when carbs & protein were taken in during exercise.

Coingestion of Carbohydrate and Protein Hydrolysate Stimulates Muscle Protein Synthesis during Exercise in Young Men, with No Further Increase during Subsequent Overnight Recovery, Milou Beelen, Journal of Nutrition Vol. 138, No. 11, 2198-2204, November 2008

We conclude that, even in a fed state, protein and carbohydrate supplementation stimulates muscle protein synthesis during exercise. Ingestion of protein with carbohydrate during and immediately after exercise improves whole-body protein synthesis but does not further augment muscle protein synthesis rates during 9 h of subsequent overnight recovery.

Thanks! Actually I downloaded this one last night but have not had a chance to read it. You really stoked my curiosity and I went back and read two books I have on substrate and exercise metabolism as well as downloading about 30 studies I will read later today.::ction-sm

EasyEJL · Mar 24, 2009

Since we are talking protein synthesis instead of GHR* momentarily, heres a question to toss out. In my research, what i found was very interesting and i'll just paraphrase, but if necessary hunt for the studies. Basically the findings were that although BCAAs and whey isolate did have some of the fastest ingestion, breakdown to individual EAAs and start of protein synthesis, they also showed starting a chain of higher levels of protein oxidation. Whereas although casein took a little longer to digest and break down, stayed in system far longer (8+hrs of elevated EAAs) and had minimal oxidation, so the overall net retained at 24 hours was superior in casein. So i've switched from ever using whey to only using casein or milk isolate/concentrate/in a glass.

I guess my point here was that with me doing this sort of protein "protocol" and knowing that casein/milk's EAAs stay in blood 8+hours, I never really concern myself anymore with PWO protein as I know I already have a decent serum level.

Blade_HST · Mar 24, 2009

Remember that many studies on post-workout nutrient ingestion are performed under fasting conditions, not applicable to most of us who have at least 1-2 meals in us when we go to the gym. Which is why Tipton's study showed pre-workout ingestion to be better, it takes a while for amino acids to show up in the blood stream after a meal.

Now, see the following study:

J Appl Physiol. 2009 Mar 19. [Epub ahead of print]

Resistance exercise with whey protein ingestion affects mTOR signaling pathway and myostatin in men.

Hulmi JJ, Tannerstedt J, Selanne H, Kainulainen H, Kovanen V, Mero AA.

University of Jyväskylä

Signaling pathways sense local and systemic signals and regulate muscle hypertrophy. The effects of whey protein ingestion on acute and long-term signaling responses of resistance exercise are not well known. Previously untrained young men were randomized into protein (n=9), placebo (n=9) and control (n=11) groups. Vastus lateralis (VL) muscle biopsies were taken before, and 1h and 48h after a leg press of 5x10 repetitions (RE) and after 21-wk (2x/wk) resistance training (RT). Protein (15g of whey) or non-energetic placebo was ingested before and after a single RE bout and each RE workout throughout the RT. Protein group increased its body mass and VL muscle thickness (measured by ultrasonography) already at week 10.5 (P<0.05). At week 21, protein and placebo groups had similarly increased their myofiber size. No changes were observed in the non-exercised controls. However, the phosphorylation of p70S6K and rpS6 were increased at 1h post-RE measured by western blotting, the former being the greatest with protein ingestion. mTOR phosphorylation was increased after the RE bout and RT only in the protein group whereas the protein ingestion prevented the post-RE decrease in p-4E-BP1. Akt phosphorylation decreased after RT whereas no change was observed in p-eEF2. A post-RE decrease in muscle myostatin protein occurred only in the placebo group. The results indicate that resistance exercise rapidly increases mTOR signaling and may decrease myostatin protein expression in muscle, and that whey protein increases and prolongs the mTOR signaling response.

Which is interesting but since Leucine has been shown to affect signaling, not all too surprising. Now they need to follow up and use casein and see if there is any clear cut advantage/disadvantage using whey vs. casein. Also, would training experience affect the results? I think so yes, refer to the Cribbs study which showed better results and used trained subjects.

Still though at end of day (rather 21 weeks) the fiber/muscle thickness size increases were not all that dramatic between the two groups:

Fiber size change
Type 1 w/ Pro = +1932 +/-
Type 1 wo/Pro = +1712 +/-
difference of 220

Type II w/Pro = +2578 +/-
Type II wo/Pro = +2334 +/-
difference of 244

Muscle thickness change
W Pro = +.32 cm +/-
WO Pro= +.27 cm +/-
difference of .05 cm about 1/64 inch

As for the leucine, refer to Layne Norton's research and presentation, building upon earlier and concurrent research showing the discreet pulses of BCAA (and/or EAA) separated by troughs gives better overall results (sounds kinda familiar in light of the information of this thread, doesn't it?), whereas continous supply or infusion gives a refractory response where net protein synthesis goes back to zero.

The conclusion was that meals should probably be separate by at least 3-4hrs, and provide a maximum of about 3.5g of leucine corresponding to about 30-40g of whey or 50g or so of protein from chicken/meat etc. Some other research shows that glucose+EAA in between these separate pulses, i.e. 2hrs following a meal, is capable of providing another protein synthesis elevation, giving more evidence in favor of discreet pulses instead of continous elevated amino acid levels.

Still, further research will hopefully elucidate dose/response and which amino acids are required in each case...or if it really matters at all in the long run...

BigTex · Mar 24, 2009

EasyEJL said:
Since we are talking protein synthesis instead of GHR* momentarily, heres a question to toss out. In my research, what i found was very interesting and i'll just paraphrase, but if necessary hunt for the studies. Basically the findings were that although BCAAs and whey isolate did have some of the fastest ingestion, breakdown to individual EAAs and start of protein synthesis, they also showed starting a chain of higher levels of protein oxidation. Whereas although casein took a little longer to digest and break down, stayed in system far longer (8+hrs of elevated EAAs) and had minimal oxidation, so the overall net retained at 24 hours was superior in casein. So i've switched from ever using whey to only using casein or milk isolate/concentrate/in a glass.

I guess my point here was that with me doing this sort of protein "protocol" and knowing that casein/milk's EAAs stay in blood 8+hours, I never really concern myself anymore with PWO protein as I know I already have a decent serum level.

Very interesting theory. I would guess that the use of different proteins could be useful almost like the use of CHO with different GI's.

I am a fan of egg white protein but it looks like I have been using too much. Here is a good study I found on the effects of different doses and how they effect protein synthesis rates.

To examine the effect of how different dosages of egg protein powder affected protein synthesis rates; researchers had young healthy men who had previous resistance training experience perform intense resistance exercise and consume a egg protein drink that contained either 5, 10, 20, or 40 grams of egg protein. Interestingly, they found that increasing protein intake stimulated protein synthesis in a dose dependent manner up to 20 g of dietary protein, after which there was no further increase in protein synthesis (40 grams did not stimulate protein synthesis greater than 20 grams). This data suggest that there is a maximal rate at which dietary Amino Acids can be incorporated into muscle tissue and that with increasingly higher concentrations of Amino Acids, there is no further stimulation of muscle protein synthesis. So how many times in a day could someone consume such a dose (20 grams) to stimulate muscle anabolism that would ultimately translate into muscle growth? The researchers speculated that 5-6 times daily of small 20 grams of protein would be the optimal measure to increase anabolism and increase muscle mass. Whether this study applies to whey protein is not known.

Moore DR, Robinson MJ, Fry JL, Tang JE, Glover EI, Wilkinson SB, Prior T,Tarnopolsky MA, Phillips SM. Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men. Am J Clin Nutr.

So instead of taking my usual 50g. 3xd I will try 20g, 5-6xd.

Blade_HST said:
Remember that many studies on post-workout nutrient ingestion are performed under fasting conditions, not applicable to most of us who have at least 1-2 meals in us when we go to the gym. Which is why Tipton's study showed pre-workout ingestion to be better, it takes a while for amino acids to show up in the blood stream after a meal.

I think most all of the studies were done under fasting conditions. So I have to agree with you.....how applicable is this to those of us who eat two meals plus supplement with protein in between meals before we train? IMHO ingesting whey protein 20-30m pre-exercise, a CHO during exercise, and eating CHO and protein (or BCCA'S) post-exercise is probably a good idea.

Yoshiharu Shimomura, Taro Murakami, Naoya Nakai, Masaru Nagasaki, and Robert A. Harris. Exercise Promotes BCAA Catabolism: Effects of BCAA Supplementation on Skeletal Muscle during Exercise. The American Society for Nutritional Sciences J. Nutr. 134:1583S-1587S, June 2004.

Conclusion: BCAA supplementation before and after exercise has beneficial effects for decreasing exercise-induced muscle damage and promoting muscle-protein synthesis.

DatBtrue · Mar 24, 2009

Blade_HST said:
As for the leucine, refer to Layne Norton's research and presentation, building upon earlier and concurrent research showing the discreet pulses of BCAA (and/or EAA) separated by troughs gives better overall results (sounds kinda familiar in light of the information of this thread, doesn't it?), whereas continous supply or infusion gives a refractory response where net protein synthesis goes back to zero.

Awesome post! Well that is just extremely interesting...

I just went and pulled Lane Norton's pdf on protein frequency. Unfortunately his study Norton LE, Layman DK, Garlick PJ, Brana D, Anthony TG, Zhao L, Devkota S, Walker DA. Translational controls of skeletal muscle protein synthesis are delayed and prolonged associated with ingestion of a complete meal. 2007 Experimental Biology meeting abstracts [on CD-ROM], Abstract #694.6. isn't available to read.

Now the one study he mentions in support of pulsation Arnal MA, Mosoni L, Boirie Y, Houlier ML, Morin L, Verdier E, Ritz P, Antoine JM, Prugnaud J, Beaufrere B, Mirand PP. Pulse feeding improves protein retention in elderly women, Am J Clin Nutr. 1999 Jun;69(6):1202-8 is interesting but the study does mention the results weren't duplicated in the few similar studies using young people.

"Feeding frequency (number of daily meals) was shown to modulate body composition and nitrogen retention (32), but the effects of protein feeding patterns on protein metabolism remain poorly studied and have given conflicting results. In young women, nitrogen balance was higher when the daily protein intake was spread fairly evenly over 3 meals than when spread over 2 meals, with 1 meal containing no protein (33); in young men, the same conditions resulted in no significant changes in nitrogen balance (34). Several differences between these studies, such as sex and age of the subjects, daily protein intake, and methods used, might explain the discrepancies. The present study provides the first evidence that at least in the short term in this group of elderly women, protein retention was more efficiently improved by a protein pulse feeding pattern than a spread feeding pattern."

Still this topic fascinates me deeply. Lane mentioned one study that really caught my attention, Latency and duration of stimulation of human muscle protein synthesis during continuous infusion of amino acids, Julien Bohé, J Physiol Volume 532, Number 2, 575-579, April 15, 2001

Lane uses it to support his own findings:

"Thus, it appears that the signal to maintain elevated protein synthesis is still being transmitted but for some reason protein synthesis is becoming refractory after a certain period of time. This is also supported by data from Bohe et. al. which showed that the duration of protein synthesis in response to an infusion of essential amino acids was only 2 hours long even though the essential amino acids were infused for six hours."

Lanes chart:

In the brief Bohe et. al. found:

"The results suggest that muscle protein synthesis (MPS) responds rapidly to increased availability of AAs but is then inhibited, despite continued AA availability. These results suggest that the fed state accretion of muscle protein may be limited by a metabolic mechanism whenever the requirement for substrate for protein synthesis is exceeded."

But they also mention that insulin rose & fell ...which could account for the protein synthesis rise & fall.

"Our data showed that there was a marked rise in the availability of plasma insulin during the early part of the amino acid infusion but that plasma insulin concentration fell thereafter. The rise and fall of plasma insulin are somewhat similar in their extent and duration to the rise and fall of the rate of muscle protein synthesis, consistent with there being a causal link."

Now the authors interpretation though dismisses insulin and hypothesize that the protein synthesis pulse might come from "signalling pathways initially stimulated by increased amino acid availability are later turned off or inhibited."

This seems likely to me as well. What I wonder about though is the extent to which factors such as insulin, gh & androgens administered exogenously, positively effect both the amplitude & length of protein synthesis pulsation.

I believe they are on to something with signalling pathways being on & then off. I am going to assume that our hormone cocktail contributes to stronger protein synthesis pulses (thats really no stretch) and I am going to highlight the crux of it all.

GH, Insulin & androgens only contribute to protein synthesis (breakdown is another matter) during specific periods or pulsed protein ingestion.

I like this statement from Bohe et. al. :

"Overfeeding protein does not increase the size of the lean body mass, and amino acids supplied in excess of the requirements of protein synthesis are simply oxidized (Motil et al. 1981; Price et al. 1994) and their carbon skeletons used for fuel or stored as fat."

DatBtrue · Mar 24, 2009

EasyEJL said:
In my research, what i found was very interesting and i'll just paraphrase, but if necessary hunt for the studies. Basically the findings were that although BCAAs and whey isolate did have some of the fastest ingestion, breakdown to individual EAAs and start of protein synthesis, they also showed starting a chain of higher levels of protein oxidation. Whereas although casein took a little longer to digest and break down, stayed in system far longer (8+hrs of elevated EAAs) and had minimal oxidation, so the overall net retained at 24 hours was superior in casein. So i've switched from ever using whey to only using casein or milk isolate/concentrate/in a glass.

I guess my point here was that with me doing this sort of protein "protocol" and knowing that casein/milk's EAAs stay in blood 8+hours, I never really concern myself anymore with PWO protein as I know I already have a decent serum level.

Great point!!!

I stopped using Whey protein as well years ago because I thought it just contributed to fat gain. My post-workout meals are whole-food proteins.

I posted this quote in my previous post but I like it so much here it is again.

From: Bohe et. al. :

"Overfeeding protein does not increase the size of the lean body mass, and amino acids supplied in excess of the requirements of protein synthesis are simply oxidized (Motil et al. 1981; Price et al. 1994) and their carbon skeletons used for fuel or stored as fat."

EasyEJL · Mar 24, 2009

DatBtrue said:
From: Bohe et. al. :

"Overfeeding protein does not increase the size of the lean body mass, and amino acids supplied in excess of the requirements of protein synthesis are simply oxidized (Motil et al. 1981; Price et al. 1994) and their carbon skeletons used for fuel or stored as fat."

I've tried to explain this time and time again to the "more is better" crowd taking in 2g/lb of bodyweight on protein, but they rarely listen. Funnier yet are the guys trying to do a CKD, but still taking in 60g of whey in a shake PWO - gluconeogenesis will turn much of that excess protein into glucose, and keep you out of ketosis.

I had realized a while back the fallacy of the bodybuilder protein myths just looking into simple facts - a pound of muscle has less than (depending on which particular muscle) 160g of protein in it. Daily maintenance for a 220lb man even with resistance training is still only around 80g-100g. I don't know of any combination of androgens + peptides that will put on more than a pound of muscle a day(i wish), so anything over 250g is likely to be no more use than a potato. And putting on .5lb a day for 15lbs a month (which is still near impossible) of actual muscle tissue means a protein need of around 170g a day. Granted some loss in the synthesis process, but not a huge amount assuming decent quantities of other nutrients.

oh well.

BigTex · Mar 24, 2009

DatBtrue said:
I like this statement from Bohe et. al. :

"Overfeeding protein does not increase the size of the lean body mass, and amino acids supplied in excess of the requirements of protein synthesis are simply oxidized (Motil et al. 1981; Price et al. 1994) and their carbon skeletons used for fuel or stored as fat."

Pretty much the same thing Moore et al. found with the ingestion of egg protein.

EasyEJL said:
I've tried to explain this time and time again to the "more is better" crowd taking in 2g/lb of bodyweight on protein, but they rarely listen.

Fern et al. (1991) found that 2.4 g/kg/d was considered protein overload, thus providing no further increase in protein synthesis for strength and power athletes. When strength athletes increased their protein consumption to 2.4 g/kg/d amino acid oxidation increased, but there was no further protein synthesis. Researchers considered this to clearly indicate a protein overload.

It is interesting to note that Consolazio et al. (1975) Marabel et al. (1979), and Dragan et al. (1985) all reported larger increases in strength, lean body mass (LBM) and nitrogen with much higher protein intakes (3.3, 2.8, and 3.5 g/kg/d respectively). These reports tend to corroborate the more anecdotal beliefs of weight lifters that extremely high dietary protein intakes are essential for optimal muscular development.

However, they still did not prove that higher intakes of more than about 1.76 g/kg/d actually were responsible for improving muscle mass during resistance training. Researchers are not exactly sure what role the extra calories might have provided by consuming that much extra protein, could have had on protein synthesis. It is further suspected that the more calories you take in over energy balance, the less protein you may actually need for optimal protein synthesis (Bucci 1993).

Fern, E.B., Bielinski, R.N., and Schultz, Y. (1991). Effects of exaggerated amino acid and protein supply in man. Experientia. 47: 168.

Consolazio, C.F., Johnson, H.L., Nelson, R.A., Dramise, J.G., and Skala, J.H. (1975). Protein metabolism during intensive physical training in the young adult. Am. J. Clin. Nutr. 28: 29.

Marable, N.L., Hickson, J.F., Korslund, M.K., Herbert, W.G., and Desjardins, R.F. (1979). Urinary nitrogen excretion as influenced by a muscle-building exercise program and protein intake variation. Nutr. Rep. Int. 19: 795.

Dragan, G.I., Vasiliu, A., and Georgescu, E. Effects of increased supply of protein on elite weight lifters. IN: Milk Proteins 1984. Galesloot, T.E. and Timbergen, B.J., Eds. Pudoc. Waningen, Netherlands.

Bucci, L. (1993). Nutritional ergogenic aids--macronutrients. IN: Nutrients as Ergogenic Aids for Sports and Exercise. Bucci, L., Ed. CRC Press. Boca Raton, FL. pp. 16.

Deio · Mar 26, 2009

Hey Dat.

How come our GH-levels are higher when we are fasting?
Is it because of the carbs & fats present in your body when your eating?

We have always told our children to eat to grow tall. But that seems to actually be the opposite of the truth?

I've always though that children who eat much will grow to their full potential.

So I'm kinda confused about that.

-Deio

likkayouth · Mar 26, 2009

Deio said:
Hey Dat.

How come our GH-levels are higher when we are fasting?
Is it because of the carbs & fats present in your body when your eating?

We have always told our children to eat to grow tall. But that seems to actually be the opposite of the truth?

I've always though that children who eat much will grow to their full potential.

So I'm kinda confused about that.

-Deio

If at a construction site the workers work faster when there aren't much construction materials around, it doesn't mean the building will end up taller, because you still need the materials to build it with at that faster pace.

EasyEJL · Mar 26, 2009

Just throwing it out there, but i wonder measured controlled intermittent fasting might help. A lot of bodily processes use negative feedback loops to control levels, but often they take time to kick back in, so its possible that you could manipulate it that way for a higher average level. I'm thinking this from things like leptin + T3, and long term dieting for fat loss. Without the occasional refeed (and/or carbup in the case of a ketogenic setup), those levels drop. But when a refeed/carbup happens, those levels are boosted for the span of days. Not sure whether the same sort of mechanism would work for gh, but i'm going to look around for some info now.

BigTex · Mar 26, 2009

Deio said:
Hey Dat.

How come our GH-levels are higher when we are fasting?
Is it because of the carbs & fats present in your body when your eating?

We have always told our children to eat to grow tall. But that seems to actually be the opposite of the truth?

I've always though that children who eat much will grow to their full potential.

So I'm kinda confused about that.

-Deio

While I am not DAT, I hope I can shed a little light on this one. GH is a decisive component of protein conservation during fasting and been show to be the underlying mechanism involved in a decrease in muscle protein breakdown. As we know fasting increases protein degradation, exactly why this method of weight loss causes you to lose too much muscle mass. GH is the body's protective mechanism to prevent wasting of muscle muscle tissue in times of no food.

No as for telling children to eat to grow tall, nutrients as well as calories are necessary to stimulate growth. With out both, you kids surely will have trouble growing up tall.

EasyEJL said:
Just throwing it out there, but i wonder measured controlled intermittent fasting might help. A lot of bodily processes use negative feedback loops to control levels, but often they take time to kick back in, so its possible that you could manipulate it that way for a higher average level. I'm thinking this from things like leptin + T3, and long term dieting for fat loss. Without the occasional refeed (and/or carbup in the case of a ketogenic setup), those levels drop. But when a refeed/carbup happens, those levels are boosted for the span of days. Not sure whether the same sort of mechanism would work for gh, but i'm going to look around for some info now.

Dr. Fred Hatfield came up with the idea of a calorie cycling diet called the Zig Zag Diet that was based on something similar. By cycling calories you can theoretically cause metabolic shifts thus create a higher set point.

longrob · Mar 26, 2009

dat,
Thanks for the surgery nutrition tips and the encouragment.
-Rob

DatBtrue · Mar 26, 2009

EOD Calorie Restriction = Longevity?

Anti-Aging

Damn all you guys have touched on what has become my latest passion.

EasyEJL your mind is just wasted when it is mixed in with all the "fluff" posts at AM.

You mentioned something that to my mind is an awesome area of research with tremendous potential to make people less susceptible to cancer, better cardiovascular profiles, better memory & less damage to brain, lower oxidative stress, much better insulin sensitivity, prolonged life, ...just on and on...there are a lot of studies going back to the 1940's that demonstrate these positive effect...

I became very interested in every other day calorie restriction when I experimented for years with it on myself and found that if I alternated between:

a day of very low calories (say between 1000 & 1400) w/ food intake primarily at the beginning and end of the day & cardio exercise(s) in the earlier portion of the day followed by no food intake for several hours...

and a day where I ate at about maintenence w/ a higher intake of carbs around a session of weightlifing.

I could readily lose fat & retain muscle. In fact I always made minor but consistent strength gains and felt mentally sharp & had energy during the fasted portion of low cal day.

I have been researching a pattern of eating involving a day of eating less then 20% of maintenance calories (or a complete fast) followed by eating freely (but not excessively). I have very little doubt that this pattern is as beneficial as calorie restriction diets in promoting longevity. But has the advantage of preserving body mass.

It is interesting that on fasted days there is no depletion of glycogen from muscle, circulating levels do go down but stores are drawn from the liver. I conjecture that during periods of no energy intake the body preserves muscle as best it can (at least in the 24 hour period) so that the homo sapien can use his strength to obtain more energy. *

What is interesting is that the following non-fasted day when energy intake is occurring the body is more insulin sensitive. In fact over time w/ this pattern of eating the body can become up to 7 times more insulin sensitive.

The area that I am attempting to reconcile is whether the use of GHRH/GHRP-6 to restore youthful GH levels (and a little higher IGF-1 levels) undermines the longevity benefits of alternate day calorie restriction?

Resveratrol I suspect is not the answer to longevity in humans even though it mimics many of the transcriptional aspects of calorie restriction. It has been shown not to extend lifespan in normal mice. **

Eating at 60% of maintenance every day is not desirable, but EOD calorie restriction might be the answer to health and longevity while maintaining the body in a fit muscular state.

* - "With the present fasting protocol and maintenance of habitual daily physical activity in the fasting periods, we had expected to detect a decrease in IMTG content in the skeletal muscle. The fact that this was not seen and that muscle glycogen content was unchanged could suggest that skeletal muscle is not immediately involved in recognition of acute energy oscillations." - Effect of intermittent fasting and refeeding on insulin action in healthy men, Nils Halberg, J Appl Physiol 99: 2128-2136, 2005

** - Resveratrol delays age-related deterioration and mimics transcriptional aspects of dietary restriction without extending life span, Pearson KJ , Cell Metab. 2008 Aug;8(2):157-68.

EasyEJL · Mar 26, 2009

DatBtrue said:
Anti-Aging
What is interesting is that the following non-fasted day when energy intake is occurring the body is more insulin sensitive. In fact over time w/ this pattern of eating the body can become up to 7 times more insulin sensitive.

The area that I am attempting to reconcile is whether the use of GHRH/GHRP-6 to restore youthful GH levels (and a little higher IGF-1 levels) undermines the longevity benefits of alternate day calorie restriction?

what sort of diet in general was this on? I was pondering trying something similar, along with a neanderthal/cromagnon/caveman/whatever you choose to call it diet. It seems to fit (as an eating pattern) along with biological anthropology, so I was figuring I may as well go the whole way

My problem with something like that diet is just managing to stick with it for long enough to get a good idea of its effectiveness, with no other changes. I can make a month thru anything, but past that I start to get bored.

WC114 · Mar 26, 2009

So if you lifted 4 days a week, added insulin low dose 7ius.on those days,ghr's all week and did cardio and fasted on the other days or twice a week you could retain or build muscle and just burn the fat and increase lifespan?

DatBtrue · Mar 26, 2009

STUDY: Effect of intermittent fasting and refeeding on insulin action in healthy men

EasyEJL said:
what sort of diet in general was this on?

Eight healthy young Caucasian men, body mass index 25.7 +- 0.4 kg/m2

Throughout the intervention, the subjects were instructed to uphold their normal exercise habits, to maintain their usual macronutrient mixing of their meals, and to eat sufficient quantities of food on the nonfasting days to ensure that their body weight was stable.

The fast period was 20 hours. Each fasting period started at 2200 and ended at 1800 the following day (for protocol see Fig. 1). During the fasting periods the subjects were allowed to drink water and were instructed to maintain habitual activities.

CONCLUSION:

In conclusion, the findings that intermittent fasting increases insulin sensitivity on the whole body level as well as in adipose tissue support the view that cycles of feast and famine are important as an initiator of thrifty genes leading to improvements in metabolic function (6). We suggest that a fastinginduced increase in circulating adiponectin is at least partly responsible for this finding. The change in adiponectin, together with changes in plasma leptin with fasting, underlines the important role of the adipose tissue in recognizing the oscillation in energy stores. Finally, the data indicate that intermittent fasting and physical training may increase insulin action via different mechanisms because muscle energy stores did not change with the present fasting intervention.

EasyEJL said:
I was pondering trying something similar, along with a neanderthal/cromagnon/caveman/whatever you choose to call it diet. It seems to fit (as an eating pattern) along with biological anthropology, so I was figuring I may as well go the whole way

Its interesting you mention this because the preamble of that study contains a similar musing:

OUR GENOME WAS PROBABLY SELECTED during the Late-Paleolithic era (50,000 –10,000 BC), during a time humans existed as hunter-gatherers (6). At that time there were no guarantees in finding food, resulting in intermixed periods of feast and famine. In addition, physical activity had to be a part of our ancestors’ daily living as forage and the hunt for food must have been done through physical activity (15). Cycling between feast and famine, and thus oscillations in energy stores, as well as between exercise and rest, was characteristic in the Late-Paleolithic era and might have driven the selection of genes involved in the regulation of metabolism (30).

Thus our genotype selected centuries ago to favor an environment with oscillations in energy stores still exists with few if any changes. The modern sedentary lifestyle common in the westernized countries is characterized by constant high food imbalance between our genotype and the environment in which we live today. This may predispose our potential “thrifty” genes to misexpress metabolic proteins, manifesting in chronic diseases (e.g., Type 2 diabetes) in the industrialized part of the world.

It is well known that physical training increases insulin action (10). The molecular events leading to an exercisemediated increase in insulin action are not fully characterized. In addition, energy usage during each exercise bout in the training regimen with subsequent eating creates oscillations in energy stores. These oscillations are probably not as massive as the oscillations seen between periods of feast and famine for the Late-Paleolithic people, but some similarities might exist, and we speculated whether exercise-induced oscillations in energy stores could be mimicked by intermittent fasting. This study was undertaken to test the hypothesis that 14 days of intermittent fasting and refeeding improves insulin-stimulated glucose disposal.

DatBtrue · Mar 26, 2009

WC114 said:
So if you lifted 4 days a week, added insulin low dose 7ius.on those days,ghr's all week and did cardio and fasted on the other days or twice a week you could retain or build muscle and just burn the fat and increase lifespan?

Retain muscle & burn fat - yes. * But also add MCT oil to down regulate lipogenic genes in adipocytes

Increase lifespan - ??? (I am not sure what effect the exogenously administered insulin would be or the GHRH/GHRPs)

Decrease your risk of cancer (i.e. lower lymphoma incidence, longer survival w/ malignant tumors, and lower rates of proliferation of several cell types) and or increase the ability to handle higher amounts of chemo if you have cancer, reduce oxidation & inflammation in the body, increase the ability for the body to handle stress, lower diabetes incidence, decrease cardiovascular disease risk (lower total cholesterol and triacylglycerol concentrations, a lower heart rate, improved cardiac response to myocardial infarction, increase HDL-cholesterol & lower blood pressure), reduce neurotoxicity, modulate several risk factors, thereby preventing chronic disease - Most likely (all have been demonstrated in either animal or human models)

But you may not even need a complete fast on alternate days. Simply by taking in only 20% to 50% may confer some (if not the longevity) benefit.

The authors of the study, The effect on health of alternate day calorie restriction: Eating less and more than needed on alternate days prolongs life, James B. Johnson, Medical Hypotheses (2006) 67, 209–211 made the following claim and hypothesis before reexamining a study that took place in Spain the 1950's which supports their claim.

"Restricting caloric intake to 60–70% of normal adult weight maintenance requirement prolongs lifespan 30–50% and confers near perfect health across a broad range of species. Every other day feeding produces similar effects in rodents, and profound beneficial physiologic changes have been demonstrated in the absence of weight loss in ob/ob mice. Since May 2003 we have experimented with alternate day calorie restriction, one day consuming 20– 50% of estimated daily caloric requirement and the next day ad lib eating, and have observed health benefits starting in as little as two weeks, in insulin resistance, asthma, seasonal allergies, infectious diseases of viral, bacterial and fungal origin (viral URI, recurrent bacterial tonsillitis, chronic sinusitis, periodontal disease), autoimmune disorder (rheumatoid arthritis), osteoarthritis, symptoms due to CNS inflammatory lesions (Tourette’s, Meniere’s) cardiac arrhythmias (PVCs, atrial fibrillation), menopause related hot flashes. We hypothesize that other many conditions would be delayed, prevented or improved, including Alzheimer’s, Parkinson’s, multiple sclerosis, brain injury due to thrombotic stroke atherosclerosis, NIDDM, congestive heart failure."

I have been on an every other day diet for a couple of months now w/ one of those days below 50% of my maintenance and I feel pretty darn good. The most noticeable effect is a sharper mind/memory although part of that effect comes from my EOD intake of Mucuna pruriens, 40% L-Dopa w/ GHRPs. - **

** - Ghrelin Amplifies Dopamine Signaling by Cross Talk Involving Formation of Growth Hormone Secretagogue Receptor/Dopamine Receptor Subtype 1 Heterodimers, Hong Jiang, Lorena Betancourt, and Roy G. Smith, Molecular Endocrinology 2006 20(8):1772–1785

"In summary, our results demonstrate that GHS-R and D1R are coexpressed in the same neurons and that ghrelin has the capacity to amplify dopamine signaling by a mechanism associated with GHS-R/D1R heterodimer formation. Because ghrelin production is cyclical, this pathway provides temporal control over the magnitude of dopamine signaling in neurons expressing both receptors. A decline in dopamine signaling occurs during aging that is not accompanied by reduced D1R expression in humans, but might be linked to the precipitous decline in expression of the dopamine transporter (44, 45). Therefore, amplifying D1R signaling in a neuronal specific way by administering ghrelin or a ghrelin mimetic could counteract age-related attenuation of dopamine function and benefit cognitive function in the elderly. Finally, our findings provide new information on the potentially broad neuromodulatory roles of ghrelin and GHS-R and invite speculation on their potential for a more profound role in modifying intracellular signaling of other neurotransmitter-activated GPCRs."