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Big_Boi
11-29-2004, 04:07 PM
Hey, I'm just interested in how long it takes for the protein you drink/eat to turn into muscle. Also, can someone explain the process behind this transformation from PROTEIN to MUSCLE. Thx.

BluSilver
11-29-2004, 04:34 PM
Wow that's gonna be a long post. Look it up- don't make us do all the work! lol Look up protein synthesis.

Big_Boi
11-29-2004, 04:48 PM
Wow that's gonna be a long post. Look it up- don't make us do all the work! lol Look up protein synthesis.

Haha, I guess that makes two lazy people. ;)

pu12en12g
11-30-2004, 09:13 AM
This will get you started:

http://forum.bodybuilding.com/showthread.php?t=337536

http://www.bodybuilding.com/fun/catprot.htm

Big Cat
12-01-2004, 03:42 AM
The short breakdown : A protein consists of a primary structure (sequence of amino acids), secondary structure (a-helix or b-sheet) and a tertiary structure (folding in 3D). Sometimes a quaternary structure if it forms complexes with other structures. All three (or four) make up the specific qualities of a protein by forming specifically formed 3-D structures consisting of amino acid R-groups with different chemical and physiological properties. Allowing for a whole lot of very specific proteins to be made with only a handful of amino acids.

When you ingest that protein, all of that is lost. The acid in the stomach will degrade secondary and tertiary structures and digestive enzymes will begin breaking down the primary structure into amino acids and small peptides that get absorbed in the intestines. This is where a lot of people tend to err. Buying some sort of protein because it gets conserved more with a particular extraction process, when it then just gets completely obliterated in your stomach anyway. The only effect the sort of protein has on your own protein kinetics is the time it takes to break down (casein vs whey for example) and the make-up of amino acids.

In the body the amino acids are now available for use and under the influence of hormones like insulin (also a protein by the way) get taken up by the cells, like muscle cells. When the stimulus for muscle growth is given, chromosomes unfold into chromatids, DNA gets ripped open by DNA helicase and each string gets copied to mRNA by RNA polymerase. mRNA migrates from the nucleus to the Rough endoplasmatic reticulum, where small elements consisting of two subunits, called ribosomes, match each three-base codon (RNA can contain 4 different bases) to a tRNA segment that is opposite to it. When bound that tRNA fragment can also bind a specific amino acid. In this manner all the amino acids that that mRNA fragment encodes for are linked up to form a primary protein, which is then folded into a secondary and tertiary structure and incorporated where needed. In case of muscle that'll be primarily myosin and actin.

Sometimes it can take many, many hours to even see the mRNA show up after a stimulus, and then it still takes quite some time to form and transport the proteins.

That's the short version.

Lok7y
12-01-2004, 07:17 AM
Just to flush out the above, most of the process is regulating via signaling from the Akt/mTOR (mammalian target of rapamycin) pathway, and later downstream p70S6K and PHAS-1/4E-BP1. This is where localized IGF-1 activates protein synthesis, downstream of mTOR, whereas autocrine/p-IGF 'launches' the whole chain.

Calcineurin/NFAT (nuclear factor of activated T cells) is not activated during hypertrophy in vivo, so it is essentially a non-factor in the growth-transcription response.

So when the stimulus to synthesize new contractile tissue presents itself (via a tension stimulus which kicks off the above signaling cascade), mRNA from skeletal muscle start interacting with ribosomes to pull amino acids out of the intracellular pool (where much of ingested protein eventually ends up), form new contractile proteins, and integrate them among the existing myofibrils. It's pretty clear that the actual rate-limiting molecular step for muscle protein synthesis is the rate/speed of actin/myosin heavy chain mRNA translation, since the ribosome concentrations are more than abundant in the RER for transciption needs.

The aforementioned cellular mechanics also provide strong justification for recurring tension stimulii-promoting methods of training, since strength-training upregulates the above mRNA transciptional activity with a ~ 36 hour framework, after which degredation to resting activity levels is virtually 100%.

Pox
12-06-2004, 03:08 PM
Would i get the ****s if i stared takeing nitro-tech right now? And how intence would i have to work out before i could see the pounds stack on?
Thanx

Big Cat
12-06-2004, 03:17 PM
Just to flush out the above, most of the process is regulating via signaling from the Akt/mTOR (mammalian target of rapamycin) pathway, and later downstream p70S6K and PHAS-1/4E-BP1. This is where localized IGF-1 activates protein synthesis, downstream of mTOR, whereas autocrine/p-IGF 'launches' the whole chain.

Calcineurin/NFAT (nuclear factor of activated T cells) is not activated during hypertrophy in vivo, so it is essentially a non-factor in the growth-transcription response.

So when the stimulus to synthesize new contractile tissue presents itself (via a tension stimulus which kicks off the above signaling cascade), mRNA from skeletal muscle start interacting with ribosomes to pull amino acids out of the intracellular pool (where much of ingested protein eventually ends up), form new contractile proteins, and integrate them among the existing myofibrils. It's pretty clear that the actual rate-limiting molecular step for muscle protein synthesis is the rate/speed of actin/myosin heavy chain mRNA translation, since the ribosome concentrations are more than abundant in the RER for transciption needs.

The aforementioned cellular mechanics also provide strong justification for recurring tension stimulii-promoting methods of training, since strength-training upregulates the above mRNA transciptional activity with a ~ 36 hour framework, after which degredation to resting activity levels is virtually 100%.

What's the point of breaking all this down into something people can understand and use, if you are just going to translate it back to textbook theoretics ? This whole paragraph is basically an elaborate explication of what I described as initiation of transcription. Because if the aim was to elaborate and be complete, you are missing a few pages.

Cosmonaut
12-06-2004, 05:32 PM
So when we ingest protein we essentially just keep the bloodstream fool of proteins for the muscles when this synthesis does actually occur? And why does muscle grow at night only what does it do during the day just sit around damaged? Or does it have to do with the HGH being activated at night?

Big_Boi
12-06-2004, 07:11 PM
Would i get the ****s if i stared takeing nitro-tech right now? And how intence would i have to work out before i could see the pounds stack on?
Thanx

Intensity is certainly a key, but it's more about consistency of lifting and eating in the long run that will put on the lbs.

Pr0meTheUS
12-06-2004, 07:39 PM
Sorry for my imbecility, but which part does testosterone fit into?
Or does it even belong here?

Pox
12-07-2004, 09:03 AM
You cats are great... very informative...

I was thinking about doing yoga and such to keep speed up.
But still lift and such...

have you guy saw the ball, and do you think it would be Efficient? Because you do use your core alot in matial arts, boxing, and ground techs...

I just dont want to lose my speed while bulking up

Pox
12-07-2004, 09:13 AM
6'2
175
age:21
?looking to bulk up my center chest?

I have always heard it is hard to mantain speed while bulking up...

I just joined the guard 3 weeks ago. Basic is Feb. 15.
they bumped that **** up to 12 weeks...

str8flexed
12-07-2004, 10:40 AM
Hey, I'm just interested in how long it takes for the protein you drink/eat to turn into muscle. Also, can someone explain the process behind this transformation from PROTEIN to MUSCLE. Thx.

it is slightly more complicated than that and I could write a book on it and still not answer it.

short answer: it depends

str8flexed
12-07-2004, 10:41 AM
So when we ingest protein we essentially just keep the bloodstream fool of proteins for the muscles when this synthesis does actually occur? And why does muscle grow at night only what does it do during the day just sit around damaged? Or does it have to do with the HGH being activated at night?


I don't know who fed you that malarchy but protein turnover most certainly does not happen only at night. In fact, I very much doubt it matters what time of day it is

str8flexed
12-07-2004, 10:45 AM
So when we ingest protein we essentially just keep the bloodstream fool of proteins for the muscles when this synthesis does actually occur? And why does muscle grow at night only what does it do during the day just sit around damaged? Or does it have to do with the HGH being activated at night?

when depends on many factors. Much protein synthesis is performed using amino acids from previously degraded endogenous proteins; you must understand that proteins get broken down into their constiutive amino acids during digestion and it is the amino acids that enter the bloodstream... not proteins. (if dietary proteins do get in the bloodstream you would know... because you would have an allergic reaction). These amino acids have literally THOUSANDS of different pathways they can go into, and many of them probably NEVER get incooperated into muscle tissue... while some may get incooperated in a matter of minutes. I really haven't looked at any studies using tracers to examine the kinetics behind this. However, I imagine it depends on fed vs. fasted, total protein intake, meal composition, activity level.... I could go on and on

Cosmonaut
12-07-2004, 01:00 PM
I don't know who fed you that malarchy but protein turnover most certainly does not happen only at night. In fact, I very much doubt it matters what time of day it is
Thats what i figured, it doesn't really make sence that muscle only gets built at night.

CaptainCode
12-08-2004, 04:12 PM
DNA gets ripped open by DNA helicase and each string gets copied to mRNA by RNA polymerase. mRNA migrates from the nucleus to the Rough endoplasmatic reticulum, where small elements consisting of two subunits, called ribosomes, match each three-base codon (RNA can contain 4 different bases) to a tRNA segment that is opposite to it. When bound that tRNA fragment can also bind a specific amino acid. In this manner all the amino acids that that mRNA fragment encodes for are linked up to form a primary protein, which is then folded into a secondary and tertiary structure and incorporated where needed. In case of muscle that'll be primarily myosin and actin.

I'm getting deja-vu of OAC Biology :D

Andrew69
12-09-2004, 08:17 PM
When you ingest that protein, all of that is lost. The acid in the stomach will degrade secondary and tertiary structures and digestive enzymes will begin breaking down the primary structure into amino acids and small peptides that get absorbed in the intestines.

Big Cat,
I have read references to studies that say that di and tripeptides are absorbed in greater concentrations that what was once thought.

Would you agree with that?

str8flexed
12-09-2004, 08:30 PM
Big Cat,
I have read references to studies that say that di and tripeptides are absorbed in greater concentrations that what was once thought.

Would you agree with that?


More than once thought yes, but is it significant is the question. Just becuase it is more than once thought does not mean it is a significant level.

-Layne

gregxy
12-09-2004, 09:42 PM
So, Assuming that the amino acids aren't immediately used
to form new protien, how long would they remain in the blood
stream before being broken down for energy consumption?


Thanks.

str8flexed
12-09-2004, 10:00 PM
So, Assuming that the amino acids aren't immediately used
to form new protien, how long would they remain in the blood
stream before being broken down for energy consumption?


Thanks.

they don't remain in the blood for long, they are utilized rather quickly for whatever purpose.

you guys don't realize it... but I kind of know what direction you are going and believe me... you are splitting hairs

Big Cat
12-10-2004, 10:24 AM
Big Cat,
I have read references to studies that say that di and tripeptides are absorbed in greater concentrations that what was once thought.

Would you agree with that?

No doubt.

That's the reason you should spend your money on whole proteins instead of amino acids, because your body's digestive system is geared to cutting it into the most affectively absorbed fragments. On top of that whole protein is always a ****load cheaper.

Don't let that argument coax you into buying peptides and crap though, those are extremely expensive and the increase in absorption does not warrant the increase in price. In the end you can get more by just consuming more protein, for less money, and get all the other amino's on top.

str8flexed
12-10-2004, 10:56 AM
yup, the only aminos i can ever see supplementing with would be the BCAA's and that would be assuming 1 of 2 things or both

1) your total protein intake is not adequate
2) you are an endurance athlete or you have extremely long and arduous training sessions... i mean like >2 hours

BluSilver
12-10-2004, 04:23 PM
I totally agree about the bcaa supplementation. When I was preparing for a marathon, I'd take bcaa's (mostly Leucine) halfway through my training and it really helped. Now, I consider it a waste of money.

Andrew69
12-10-2004, 10:08 PM
Thanks Big Cat and str8flexed.
I was not headed in that direction, it was just something I had read and wondered what you guys thought about it.

Im always eager to learn from those more experienced :D

Lok7y
12-10-2004, 10:30 PM
I would supplement with free-form leucine if I was dieting heavily. Other than that, I completely agree with Layne.