amino receptors

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    OK. Why?

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    Quote Originally Posted by David Dunn
    OK. Why?
    I read bcaa's need insulin for absorption,,, not sure how or why...
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    Quote Originally Posted by grngoloco

    I read bcaa's need insulin for absorption,,, not sure how or why...
    Specifically,, low insulin inhibits ansorption into muscle tissue
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    That is different than (digestive) absorption.

    Insulin (glycogen) shuttles aminos into the muscle after absorption. But there is also a thing called glycogenesis where in the body will convert protein/aminos into glycogen in its absence.
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    Quote Originally Posted by David Dunn
    That is different than (digestive) absorption.

    Insulin (glycogen) shuttles aminos into the muscle after absorption. But there is also a thing called glycogenesis where in the body will convert protein/aminos into glycogen in its absence.
    LOL... Like I said, I don't post queries about stuff I already know!
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    Well,, I'll keep taking my aminos individually on an empty stomach,as best I can... wherever it occurs,, there definitely seems to be evidence of competition,, nothing makes me more mad than expensive toilet water
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    Dude, these receptors you are referring to are not broad-spectrum amino acid receptors for dietary protein that you ingest. They are specific receptors for metabolic processes in the body. I'm sorry, but you can't cite activity at the NMDA receptor and thus psotulate that there are "amino acid receptors." There aren't.
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    Quote Originally Posted by grngoloco View Post
    Ok,, it is my understanding that bcaa's do not act the same way upon ingestion as, let's say, arginine, ornithine or glutamine
    That is correct, and has nothing to do with receptors.

    Let me clear up what's happening in the small intestine. After peptide cleavage at a variety of primary levels (pepsin in the stomach, pancreatic release of trypsin/chymotrypsin in the duodenum), we have a bunch of small di and tri peptides. From here, these peptides are further cleaved into individual amino acids at the level of the microvilli by enzymes that we will refer to collectively as "brush-border enzymes" for simplicity. However, di/tri peptides can also enter the enterocyte, at which point enzymes within the cell will reduce them to amino acids. No peptides will enter the bloodstream following intestinal absorption; one way or another, they will be individual amino acids.

    Here's a nice image depicting this:



    And here's a description from one of my textbooks showing how exactly amino acids are absorbed. I had a much better textbook with an image showing means of absorption for each individual EAA, but I'm on break and don't have access to it. You can PM me in a week if you're still interested.


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    Quote Originally Posted by mr.cooper69
    Dude, these receptors you are referring to are not broad-spectrum amino acid receptors for dietary protein that you ingest. They are specific receptors for metabolic processes in the body. I'm sorry, but you can't cite activity at the NMDA receptor and thus psotulate that there are "amino acid receptors." There aren't.
    I think I was talking about transporters and not receptors,, relax a bit,, I'm not as biochemistry educated as a lot of y'all
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    Quote Originally Posted by grngoloco View Post
    I think I was talking about transporters and not receptors,, relax a bit,, I'm not as biochemistry educated as a lot of y'all
    Ok. So what about transporters are you concerned about? Transporters on what level (i.e. intestine, capillary, liver, myocyte, etc..)?
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    Thanks for all the input,,, I came to AM to learn, not put my vast knowledge on display,,, I really do take everything people tell me and put it to further research,,, again, thanks
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    Quote Originally Posted by mr.cooper69 View Post
    That is correct, and has nothing to do with receptors.

    Let me clear up what's happening in the small intestine. After peptide cleavage at a variety of primary levels (pepsin in the stomach, pancreatic release of trypsin/chymotrypsin in the duodenum), we have a bunch of small di and tri peptides. From here, these peptides are further cleaved into individual amino acids at the level of the microvilli by enzymes that we will refer to collectively as "brush-border enzymes" for simplicity. However, di/tri peptides can also enter the enterocyte, at which point enzymes within the cell will reduce them to amino acids. No peptides will enter the bloodstream following intestinal absorption; one way or another, they will be individual amino acids.

    Here's a nice image depicting this:



    And here's a description from one of my textbooks showing how exactly amino acids are absorbed. I had a much better textbook with an image showing means of absorption for each individual EAA, but I'm on break and don't have access to it. You can PM me in a week if you're still interested.


    I basically said this in a post a page back, nice pics though . I believe researchers recently found transport proteins for very short peptides, though.

    edit: didnt read it all, I guess you said that too.
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    Mainly asking about the importance of taking aminos individually and separately .... how important is it?
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    Quote Originally Posted by grngoloco View Post
    Mainly asking about the importance of taking aminos individually and separately .... how important is it?
    Not even remotely important.
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    Been on the go all day,, haven't had time to look into the responses I've gotten,, but I will
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    Quote Originally Posted by mr.cooper69

    Not even remotely important.
    Why do my arginine and glutamine bottles say to take on empty stomach?
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    lol cooper I think we used that same book for one of my nutrition classes
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    Quote Originally Posted by grngoloco View Post
    Why do my arginine and glutamine bottles say to take on empty stomach?
    Because they think free form arginine/glutamine will hit the blood faster without other foods, which is correct. Unfortunately, arginine does not elevate NO nor provide any other worthwhile benefit, and glutamine has failed to improve recovery time and time again. Neither should be your concern. Now you can take BCAAs on an empty stomach to spike blood leucine and maximize MPS.

    Quote Originally Posted by bigdavid View Post
    lol cooper I think we used that same book for one of my nutrition classes
    That's one of my mcat prep books so I don't think so .
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    Quote Originally Posted by mr.cooper69 View Post

    That's one of my mcat prep books so I don't think so .
    Well that's why then. I did princeton review also lol..but it looks o so similar to a nutrition book of mine..
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    Quote Originally Posted by mr.cooper69

    Because they think free form arginine/glutamine will hit the blood faster without other foods, which is correct. Unfortunately, arginine does not elevate NO nor provide any other worthwhile benefit, and glutamine has failed to improve recovery time and time again. Neither should be your concern. Now you can take BCAAs on an empty stomach to spike blood leucine and maximize MPS.

    That's one of my mcat prep books so I don't think so .
    I never worried about NO with arginine,,, I was under the impression if taken at very high doses in a 2:1 ratio with ornithine it will stimulate gh release
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    Quote Originally Posted by bigdavid View Post
    Well that's why then. I did princeton review also lol..but it looks o so similar to a nutrition book of mine..

    Ahh nice. I found EK to be far superior...that's the other book I was looking for but I don't have it here.
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    Quote Originally Posted by grngoloco View Post
    I never worried about NO with arginine,,, I was under the impression if taken at very high doses in a 2:1 ratio with ornithine it will stimulate gh release
    It MAY do so but it is not worth it at all. Other things can stimulate GH release without the hassle...not that either will have tangible benefits for body composition. Also keep in mind that arginine attenuates the GH response to exercise.
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    Quote Originally Posted by mr.cooper69

    It MAY do so but it is not worth it at all. Other things can stimulate GH release without the hassle...not that either will have tangible benefits for body composition. Also keep in mind that arginine attenuates the GH response to exercise.
    Thanks again Cooper ... can always count on your expertise,,, out of curiosity,, other than peptides, what else releases gh?
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    Quote Originally Posted by grngoloco View Post
    Thanks again Cooper ... can always count on your expertise,,, out of curiosity,, other than peptides, what else releases gh?
    Alpha GPC, L-DOPA (pre-bed), and generally anything that induces deeper sleep.
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    Quote Originally Posted by mr.cooper69

    Alpha GPC, L-DOPA (pre-bed), and generally anything that induces deeper sleep.
    What about GABA? I sleep great on it
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    Quote Originally Posted by grngoloco View Post
    What about GABA? I sleep great on it
    GABA too. I've never been big on it. I've seen studies showing a very high, very transient increase in GH, but if it helps you sleep deeper, no reason not to use it anyway.
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    I don't think I've ever read that BCAA should be taken on an empty stomach. If anything I've read to dose them 45min post meal to elevate the uptake of nutrients. I think the empty stomach thing might be a misunderstanding do to the fact that many (currently myself included) dose them mid day on a semi empty stomach to keep protein intake elevated while reducing calories consumed. Its also been mentioned to dose them pre cardio if your doing so in a fasted state.

    If I'm not mistaken Lucine on its own can trigger a bit of insulin release. Please correct me if I'm wrong on all fronts.

    Great thread BTW.
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    Quote Originally Posted by lonewolf0420
    I don't think I've ever read that BCAA should be taken on an empty stomach. If anything I've read to dose them 45min post meal to elevate the uptake of nutrients. I think the empty stomach thing might be a misunderstanding do to the fact that many (currently myself included) dose them mid day on a semi empty stomach to keep protein intake elevated while reducing calories consumed. Its also been mentioned to dose them pre cardio if your doing so in a fasted state.

    If I'm not mistaken Lucine on its own can trigger a bit of insulin release. Please correct me if I'm wrong on all fronts.

    Great thread BTW.
    Earlier in the thread I mentioned that bcaa's needed insulin for absorption,,,, I was talking about individual ff aminos,,, not bcaa's
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    Quote Originally Posted by grngoloco

    Earlier in the thread I mentioned that bcaa's needed insulin for absorption,,,, I was talking about individual ff aminos,,, not bcaa's
    Bcaa's behave a bit differently from some of what I've read,,, but I have A LOT more reading to do
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    Quote Originally Posted by lonewolf0420 View Post
    I don't think I've ever read that BCAA should be taken on an empty stomach. If anything I've read to dose them 45min post meal to elevate the uptake of nutrients. I think the empty stomach thing might be a misunderstanding do to the fact that many (currently myself included) dose them mid day on a semi empty stomach to keep protein intake elevated while reducing calories consumed. Its also been mentioned to dose them pre cardio if your doing so in a fasted state.

    If I'm not mistaken Lucine on its own can trigger a bit of insulin release. Please correct me if I'm wrong on all fronts.

    Great thread BTW.
    This is false. Spiking MPS while food is still being digested (and absorbed to a mild degree) is redundant. The best time to take your BCAAs would be 2 or more hours postprandially. Correct on the leucine.
  

  
 

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