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Author Topic: Lex: Fat high v low  (Read 1437 times)
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lex_rooker
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« Reply #10 on: December 18, 2009, 09:30:06 PM »

The post above is rather long and a key point may have been lost in the forrest of words.  What I don't think I made clear is that I believe that there is a distinct difference between dietary protein and protein released through sacrificing internal healthy tissue.

My experience as discussed above is that some percentage of all dietary protein is probably converted to glucose and the conversion rate is probably somewhere around 58% if the source of the protein is meat.

However, my experiments have shown that if the body runs low on glucose and must sacrifice healthy tissue to create it, then it will only do so when necessary, and will only sacrifice the minimum tissue necessary to meet the immediate requirement. 

So, in effect both sides of the argument may have some truth to them.  On the side supporting the theory that protein is only converted to glucose when needed, I think it can be shown that this is probably true if healthy tissue must be sacrificed in the process.  On the side supporting the theory that some percentage of all protein is always being converted to glucose, I think it can be shown that this is probably true for protein consumed as food.

By extension it is also probably true that even when tissue is being sacrificed, the resulting protein is probably converted to glucose at the same percentage (about 58%) as dietary protein.  It's just that healthy tissue won't be sacrificed at all unless there is a critical need.

I also have a theory that the conversion rate is dependent on the amino acid profile of the protein.  Some amino acids can be converted to glucose and others can’t.  For animal protein (meat), it seems that about 58% of the amino acids are available for conversion.  However, protein from plant sources have a completely different amino acid profile and therefore would likely have a totally different rate of conversion.

As dietary protein from meat, and muscle tissue sacrificed to meet a critical glucose requirement are both from animal sources, their amino acid profile would be similar and therefore their conversion rate should be about the same.

I have no idea what the rate of conversion might be for plant based proteins. These always occur in the presence of large amounts of carbohydrate and there is no easy way for a layman to isolate them or determine their amino acid profile.  Without lab facilities capable of doing such an analysis, I have no way to prove or disprove the above theory.

If anyone can confirm (or wishes to shoot holes in) my reasoning, feel free.  I’m very good as sticking my foot in my mouth – to the point that now I just change feet!

Lex
« Last Edit: December 18, 2009, 09:56:49 PM by lex_rooker » Logged
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« Reply #11 on: December 19, 2009, 02:48:10 AM »

This is one of those religious arguments.  There are those that say protein only converts to glucose when needed, and there are others that believe that some portion of all the protein we eat is converted to glucose.  I'm in the second camp as my personal experience supports that some portion of all protein eaten is converted to glucose.

Example:  I eat a mixture of meat and fat that provides 80+% of calories from fat and about 90g protein per day while supplying around 2,000 calories of total energy.  My average blood glucose will hover right around 85 mg/dl.  If my body needed more then it would start sacrificing lean muscle mass or something to create a higher BG level.  But it doesn't do this so it appears that 85 mg/dl is sufficient to meet my body’s need for glucose.  My lean body mass remains stable (based on caliper measurements) as does my weight.  I can eat this high level of fat for months at a time and BG continues to average 85 mg/dl, and lean body mass as well as weight stay stable.  Everything seems to be in balance and happy.

Now, if I reduce the fat level to 65% of calories and raise the amount of protein that I’m consuming to 150g /day, while eating an amount of food that keeps total energy the same at around 2,000 calories, the spikes in BG reach higher peaks after eating, and average BG rises to 100 mg/dl.  If I continue this regimen for several months, everything remains in balance as well, its just that average BG, and the BG spikes after eating are at higher levels.  I don’t seem to gain weight so my assumption is that total energy consumed vs total energy expended is again in balance.

Continuing on with this same line of reasoning, if my body already has a relatively high BG level of 100 mg/dl, then why would BG spike even higher after eating a protein rich meal?  It certainly doesn’t need more glucose.  This could only happen if some portion of all the protein eaten is converted to glucose.

Now I have to ask the question:  If protein is only converted to glucose when the body needs it, and, if my body is happy for months at a time with a BG of 85 mg/dl, then what would cause the rise in BG when more protein is consumed and BG to fall when less protein is consumed?  The only answer that I can come up with is that some portion of all dietary protein is converted to glucose independent of the body’s immediate need.

I also have found that if I increase protein consumption even more (above 150g/day), the glucose spike after eating rises even higher, but average BG tends to stabilize right around 100 mg/dl. This makes me believe that enough glucose is being created to cause insulin to kick in and hold it right at the threshold.  When we eat carbs the glucose spike is huge and rapid, often within minutes of eating.  This causes the body to overestimate the insulin requirement and dump more insulin than is needed.  This causes BG to fall rapidly after the high carb meal and it may fall to such an extent that we start craving something sweet to bring the levels back up.  This is the normal see-saw most high carb eaters experience.  When the body creates glucose from protein, the rise is much slower but for a longer duration, often several hours.  The very slow rise allows the pancreas time to react with the proper amount of insulin and BG is much more stable.  It would also keep BG close to the threshold where the body starts to release insulin.  For me this seems to be right at 100 mg/dl.

It is also interesting that when eating a higher level of protein, BG stays in a very tight range right around 100 mg/dl for about 20 hours per day. The other 4 hours is directly after eating where BG slowly rises then gently falls back to the 95-100 range.  When eating less protein and higher fat, BG averages right around 85 mg/dl but swings up and down much more.  It may drop into the mid 70’s a couple of hours before eating, and rise to 110 for an hour or so after eating and then gently falling back to 80-85 where it stays until a few hours before my next meal.  This makes me believe that 85 mg/dl is below the threshold where insulin is released as it is not being held constant, but swings in gentle curves peaking after eating and dipping before the meal. 

BG also swings much more in response to exercise when protein intake is lower.  If I’m eating the low protein protocol and BG is 85 and I then run a couple of miles, BG will fall during the run by maybe 10 points, and it will stay near this lower level until I eat my next meal.  This makes me believe that there is no excess glucose hanging around and if it gets consumed, then it will stay low, with the body only sacrificing tissue to create more if it is necessary.  This would tend to keep BG at the lower threshold.  If I’m eating a large amount of protein and BG is 100 when I start my run, it is usually still between 95 and 100 after the run.  Again, supporting the idea that there may be an overall excess of glucose when eating the higher protein diet and insulin is moderating it at the higher threshold level.

Here is an entry from my journal where I do some mathematical gymnastics that seem to support that about 58% of all the protein eaten is converted glucose.

http://www.rawpaleoforum.com/journals/lex's-journal/msg3720/#msg3720

This was probably more than you wanted to know, but I wanted to give you as complete and answer as possible.

Lex

And what about glycogen stored in the liver ?
Eating meat triggers glucagon which raises BG.
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« Reply #12 on: December 19, 2009, 11:37:13 AM »

And what about glycogen stored in the liver ?

I give up, what about it? 

Eating meat triggers glucagon which raises BG.

I've found nothing that states that eating meat itself triggers the release of glucagon.  Do you have a resource?

Lex   
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« Reply #13 on: December 19, 2009, 11:51:04 AM »

I give up, what about it?  

I've found nothing that states that eating meat itself triggers the release of glucagon.  Do you have a resource?

Lex    

Here for instance : http://www.vivo.colostate.edu/hbooks/pathphys/endocrine/pancreas/glucagon.html

"Elevated blood levels of amino acids, as would be seen after consumption of a protein-rich meal: In this situation, glucagon would foster conversion of excess amino acids to glucose by enhancing gluconeogenesis."

In your explanation, you ignore glycogen stores and how it can impact BG.
After a protein-rich meat, glucagon will stimulate the breakdown of glycogen stored in the liver, thus increasing your BG.
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« Reply #14 on: December 20, 2009, 10:49:20 PM »

"Elevated blood levels of amino acids, as would be seen after consumption of a protein-rich meal: In this situation, glucagon would foster conversion of excess amino acids to glucose by enhancing gluconeogenesis."

In your explanation, you ignore glycogen stores and how it can impact BG.
After a protein-rich meat, glucagon will stimulate the breakdown of glycogen stored in the liver, thus increasing your BG.

Frederic,
Most of what I write about is my observations on things I can measure.  I've certainly written about how BG rises after a protein rich meal.  In fact, that was the major thesis of my previous posts on this thread.  I think it is also well known that there are very large glycogen stores in the liver which can be released when necessary.  This is one of the body's major reserves used to regulate glucose levels in the dynamic and chaotic conditions of every day living.

The link you provided seems to validate my direct experience – BG rises after eating a high protein meal.  I never discounted that BG can be affected by liver glycogen stores.  I just have no evidence that it is a significant factor in the conversion of dietary protein to glucose. I have applied simple math to the measurements and observations that I’m able to make, and the results seem to support that about 58% of the protein eaten adds additional glucose or glycogen to the body.  This is demonstrated by the fact that temporary weight gain caused by eating the high protein meal is consistent with the necessary additional water retention required to keep the proper tissue fluid balance if 58% of the protein was converted to glucose or glycogen. This is based on a research document that I read several years ago stating that for every gram of glucose and/or glycogen added (or removed) from blood and tissue, the body must store or release about 6g of water for the body to stay in proper fluid balance.  Glucose or glycogen released from the liver – even if it caused a rise in BG, would not contribute additional glucose to the body and therefore would not require additional water storage for the body to remain in proper fluid balance as newly added glucose derived from a meal would.  Is my reasoning simplistic?  Yup.  Are there a host of variables that could account for the body taking on additional water? Certainly.  However, I’ve done this experiment many times and it always comes out with similar results supporting (not proving) the idea that new glucose is created from dietary protein at some fairly consistant percentage.

 If you are convinced that a significant percentage of the rise in BG after eating a protein rich meal is directly caused by the release of stored liver glycogen, can you demonstrate this either by direct measurement or by inference through a calculation showing how some parameter we can measure tracks closely with the release of liver glycogen stores (or glucagon levels) but would not be affected by the conversion of the dietary protein itself?  In other words, can you disprove the validity of my observations or how I arrived at my conclusions? 

I’ve never claimed to know everything and several of my ideas posted on this form and elsewhere have been proven to be flat out wrong.  I’m not at all bothered by being wrong.  Putting my ideas out in public allows for comment and feedback and provides a learning opportunity.

Lex





« Last Edit: December 20, 2009, 11:17:13 PM by lex_rooker » Logged
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« Reply #15 on: December 21, 2009, 05:30:26 AM »


 If you are convinced that a significant percentage of the rise in BG after eating a protein rich meal is directly caused by the release of stored liver glycogen, can you demonstrate this either by direct measurement or by inference through a calculation showing how some parameter we can measure tracks closely with the release of liver glycogen stores (or glucagon levels) but would not be affected by the conversion of the dietary protein itself?  In other words, can you disprove the validity of my observations or how I arrived at my conclusions?  
Lex

Lex

Your reasoning makes sense to me and I think it might well be essentially correct. By the way your observations are really of high interest from a scientific point of view.

After a look at the biochemistry involved the reason I see for the objection of Frederic to be irrelevant or not hold seems to be the following:

Glucagon is released in case of a protein rich meal that results in a high concentration of amino acids in blood.

 Yet if BG is normal (not too low), there is at any rate a level of glucose in the liver quite high enough to prevent breakdown of glycogen. Glycogenolysis then cannot occur because an enzyme involved in its pathway is merely inactive. This enzyme is the phosphorylase which is inhibited by binding to glucose when its concentration is normal. By the way this is actually a necessary condition since there is no reason to break down glycogen if there is enough glucose in the blood.

In other words this means that if glucagon is released because of elevated levels of amino acids in blood it will trigger the conversion of a fraction of them into glucose but it cannot trigger glycogenolysis if simultaneously BG is normal. For glyconenolysis to take place glucose levels in blood and liver must be low and glucagon released for that specific reason.

  

 
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« Reply #16 on: December 21, 2009, 06:17:15 AM »

If you are convinced that a significant percentage of the rise in BG after eating a protein rich meal is directly caused by the release of stored liver glycogen, can you demonstrate this either by direct measurement or by inference through a calculation showing how some parameter we can measure tracks closely with the release of liver glycogen stores (or glucagon levels) but would not be affected by the conversion of the dietary protein itself?  In other words, can you disprove the validity of my observations or how I arrived at my conclusions?  

I’ve never claimed to know everything and several of my ideas posted on this form and elsewhere have been proven to be flat out wrong.  I’m not at all bothered by being wrong.  Putting my ideas out in public allows for comment and feedback and provides a learning opportunity.

Lex

Lex,

I am convinced of...nothing. Just asking questions and trying to understand.

As glucagon and insulin are both in the blood, especially after several hours of fasting and a protein rich meal, how can one be sure that no break down of glycogen from the liver occurs?
After all, amino acids are systematically converted to glucose after a protein rich meal, at approximately always the same rate, even when BG is not too low.
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« Reply #17 on: December 21, 2009, 08:17:39 PM »

Lex,

I am convinced of...nothing. Just asking questions and trying to understand.

As glucagon and insulin are both in the blood, especially after several hours of fasting and a protein rich meal, how can one be sure that no break down of glycogen from the liver occurs?
After all, amino acids are systematically converted to glucose after a protein rich meal, at approximately always the same rate, even when BG is not too low.

I'm in pretty much the same boat.  There is very little I know for sure and I too have far more questions than answers.   

And, of course I'm not sure that there is no breakdown of glycogen from the liver, and I never said there wasn't. Since I don't have a way to measure the contribution of glucose from liver reserves, not sure what, if anything, meaningful I could add to the subject.  My calculations seem to indicate that most of the BG created from a high protein meal is "new" glucose, but again, this is just speculation from simplistic calculations based on rather shaky assumptions derived from experiments with poor (or non existent) controls.  It's a good thing that none of it matters and our bodies will do the right thing regardless of what nonsense our brains invent.

Lex 
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« Reply #18 on: December 21, 2009, 10:30:22 PM »

I'm in pretty much the same boat.  There is very little I know for sure and I too have far more questions than answers.  
....
Then you are no fool, for Tyl Eulenspiegel the trickster of Germanic folklore said: "There is no greater fool than someone who thinks himself clever." I came across that just a couple days ago.

Tricksters are a seemingly universal feature of "primitive" societies. In the most "primitive" of societies--band societies, such as that of the San Bushmen--even the gods make mistakes and are sometimes the butt of jokes. Seems to me that this is the most realistic outlook.

The trickster outlook was echoed by Socrates, who whenever questioned about his judgment on a matter of debate, apparently used to say that he knew nothing for certain, and instead would ask questions of the questioner which eventually resulted in the questioner answering his own question. Plato's writes in his Republic: "Behold...the wisdom of Socrates; he refuses to teach himself, and goes about learning of others...."

My understanding is that Karl Popper added a corollary to this (or perhaps borrowed it form someone else) to the effect of "I only know what I don't know," or "I only know what the existing evidence does NOT support." (These are rough inklings from my memory that could be off).

I am also a great fan of the outlook and work of Nassim Taleb, in part because he is a fellow fan of Socrates and Popper. Taleb further builds on the insights of Socrates and Popper with his "causal opacity" in which "we are limited  in our ability to ferret out causes or in confirming our error rate in causal inference," as evidenced by the terrible track record of "experts" who try to do so.

It seems to me that the trickster spirit of hunter-gatherer mythology, Socrates, Plato, and Taleb all recognize that seeking final, absolute answers is a futile quest. Instead, we use the tools at our disposal to question, investigate and experiment. The end result of our questions is more questions.

[Addendum: And wouldn't you know it, in re-acquainting myself with Popper, I quickly find someone who attempts to shoot Popper's falsification approach to ribbons:

Martin Sewell, "Popper's Falsification," http://science.martinsewell.com/falsification.html

I'd be interested in people's opinions on Sewell's points.]
« Last Edit: December 21, 2009, 11:26:14 PM by PaleoPhil » Logged

> "Medicine improved exponentially when the tinkering barber surgeons took over from the high theorists. They just went with what worked, irrespective of why it worked." -Nassim Taleb
> "no one would touch this type of diet unless they'd tried everything else and this diet alone worked" -T.D.
> Tinkering with dairy & gluten elimination worked for me. I found a theory that explained it (Eaton's Paleolithic nutrition), which pointed me toward more tinkering, with more success. -Me
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