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The anabolic response to protein ingestion during postexercise recovery has no upper limit in magnitude and duration in vivo in humans

Absolutely not! Totally makes sense in that context ("nighttime protein" before bed, either when bulking or dieting down), as tolerated.

It's simply the idea that starting and ending the day with an 80g dose of casein (in 100g milk protein), day after day, is something I can imagine causing GI issues for some people.

I take 20 to 40 grams of casein protein before going to sleep, I can't imagine taking 80 grams and having a pleasant digestion and sleep.
 
I take 20 to 40 grams of casein protein before going to sleep, I can't imagine taking 80 grams and having a pleasant digestion and sleep.
Many factors involved here...individual tolerability, being used to it...I take 70 grams before bed (with some proteases) and does not impair my sleep quality at all.
 
Summary:

The study, conducted by Trommelen et al., published in "Cell Reports Medicine" on December 19, 2023, critically examines the anabolic response to protein ingestion following exercise, specifically exploring the magnitude and duration of this response in humans. The research is grounded in the observation that post-exercise recovery is crucial for muscle repair and growth, where protein intake plays a pivotal role. Traditional views have held that there is an upper limit to the anabolic benefits of protein intake in this context, suggesting that consuming protein beyond this limit results in no additional benefit as excess amino acids are simply oxidized. This study challenges and extends these views by examining the effects of consuming significantly large amounts of protein (up to 100g) after exercise.

Study Design and Methods​

The researchers employed a sophisticated experimental approach using a quadruple isotope tracer feeding-infusion technique, which allowed for a detailed tracking of protein digestion, amino acid absorption, and incorporation into muscle protein over a 12-hour period post-exercise. Participants were given either 0g, 25g, or 100g of protein following a session of resistance exercise, and the study meticulously measured various parameters related to protein synthesis, amino acid oxidation, and muscle recovery.

Key Findings​

  1. No Upper Limit to Protein Synthesis: Contrary to previous assumptions, the study found that the anabolic response to protein ingestion does not have an upper limit within the context examined. Specifically, consuming 100g of protein resulted in a greater and more sustained increase in muscle protein synthesis compared to 25g, extending beyond 12 hours post-exercise.
  2. Efficient Use of Protein: The research indicated that the body efficiently utilizes the ingested protein for muscle repair and growth, with minimal impact on amino acid oxidation rates. This suggests that concerns over excessive protein intake leading to wasteful amino acid oxidation may be overstated, at least in the context of post-exercise recovery.
  3. Sustained Amino Acid Availability: One of the novel insights from the study is the sustained increase in plasma amino acid levels following the ingestion of a large protein bolus (100g), which was associated with continued muscle protein synthesis. This prolonged availability of amino acids could be a key factor in supporting extended muscle repair and growth processes.
  4. Muscle and Whole-Body Protein Balance: The findings underscore a dose-response relationship between protein intake and improvements in both muscle and whole-body protein balance post-exercise. This means that higher amounts of protein intake led to better overall protein utilization and balance across the body, contributing to muscle recovery and growth.

Implications​

The study's findings have significant implications for nutritional guidelines and practices related to exercise recovery. It suggests that consuming large amounts of protein after resistance exercise can have prolonged beneficial effects on muscle protein synthesis, challenging the conventional wisdom of a strict upper limit. This could lead to a reevaluation of dietary protein recommendations for athletes and individuals engaged in regular resistance training, emphasizing the potential benefits of higher protein intake for optimal muscle recovery and growth.

Conclusion​

Trommelen et al.'s research contributes valuable insights into the dynamics of protein metabolism during post-exercise recovery. By demonstrating that the body's anabolic response to protein ingestion extends beyond previously believed limits, this study paves the way for new dietary strategies to optimize muscle recovery and growth. It highlights the importance of considering individual protein needs and recovery processes in developing nutritional guidelines for athletes and active individuals.
 
This study does not mention anything about PTOR and the body loves being in hemostasis. Also any excess protein will eventually undergo gluconeogenesis. If all this protein contributes to muscle hypertrophy, then there would be a massive number of people all over the place. This study is vague and forgets about many other important factors regarding anabolism and hypertrophy. That's why AAS is so good in building muscle because it prevents catabolism and yields to positive nitrogen balance. I can see more protein with AAS and Insulin would yield to more protein synthesis, but without AAS and Insulin you can consume 200 grams 300 grams post work out and get nowhere.

Studies like these are misleading because they exclude the many other factors and hormones responsible for positive nitrogen balance and muscle hypertrophy. GH will yield to new muscle cells, AAS will grow these new cells, insulin will shuttle Glucose and amino acids into the muscle cell. Without the hormones we use, a person can eat 1000 grams of protein a day and not see much improvement.
 
Many factors involved here...individual tolerability, being used to it...I take 70 grams before bed (with some proteases) and does not impair my sleep quality at all.

Well, it's safe to say that you and Luki are both beasts that grind food without any problems.
 
Well, it's safe to say that you and Luki are both beasts that grind food without any problems.
Three main factors:
We stick to foods that we digest and absorb easily
We give digestion all the help we can
These large amounts of food have been built up over years and years.
 
This is the most elementary shit. I can't believe we're going over this again.
It’ll be gone over another dozen times just in the next year it’s the one topic EVERYONE has an opinion
 
The question is why repair something that works well?

For years bodybuilders have been eating 5-7 meals a day with 40-70g (on average) of protein and achieving great results so why even think about it and try to reinvent the wheel?
This study was more so about resolving some scientific debates about the duration and extent of muscle protein synthesis following a (high) protein meal post-training. (It wasn't really directed at practical long-term applications, although that's what some folks are trying to make out of it, more so than I think is warranted, as noted above.)

-S
 
This study does not mention anything about PTOR and the body loves being in hemostasis. Also any excess protein will eventually undergo gluconeogenesis. If all this protein contributes to muscle hypertrophy, then there would be a massive number of people all over the place. This study is vague and forgets about many other important factors regarding anabolism and hypertrophy. That's why AAS is so good in building muscle because it prevents catabolism and yields to positive nitrogen balance. I can see more protein with AAS and Insulin would yield to more protein synthesis, but without AAS and Insulin you can consume 200 grams 300 grams post work out and get nowhere.

Studies like these are misleading because they exclude the many other factors and hormones responsible for positive nitrogen balance and muscle hypertrophy. GH will yield to new muscle cells, AAS will grow these new cells, insulin will shuttle Glucose and amino acids into the muscle cell. Without the hormones we use, a person can eat 1000 grams of protein a day and not see much improvement.
You mention "PTOR" - do you mean mTOR?


If you read the actual study, you'll see (Figure 5) they measured just about everything possible wrt. signaling, including mTOR1 and gene expression (mRNA) related to muscle growth:

Figure 5. Dissociation between feeding-induced muscle anabolic signaling and protein translation
(A–J) Skeletal muscle phosphorylation status (ratio of phosphorylated to total protein) of mTOR (Ser2448) (A); p70S6K (Thr389) (B); p70S6K (Thr421/Ser424) (C); rpS6
(Ser235/Ser236) (D); 4E-BP1 (Thr37/Thr46) (E); and ACC (Ser79) (H) and protein content of Beclin (F), LC3b (G), Atg 12, (I), and myostatin (J) were all measured by the
western blot technique.
(K–X) Skeletal muscle relative mRNA expression (relative to 18S housekeeping gene) of mTOR (K), p70S6K (L), FOXO1 (M), MurF1 (N), MAFBx (O), PGC1-alpha
(P), myostatin (Q), Beclin1 (R), cATG12 (S), LC3b (T), LAT1SLC (U), SNAT2 (V), CD98 (W), and PAT1 (X) were all measured by real-time qPCR quantification.

And they explain:

"In contrast, we did not observe any impact of protein feeding on muscle protein signaling or muscle gene expression (Figure 5). This is in line with previous work that suggests that the molecular response in skeletal muscle to protein ingestion is short lived (<4 h).16,37 Here, we extend these data by demonstrating that the muscle anabolic response to protein ingestion is sustained well beyond (R12 h) the frequently reported transient changes in molecular signaling. Collectively, these data suggest substantial divergence in the time course of the molecular response and the actual metabolic response to feeding (Figure 5Y). Therefore, the magnitude and/or time course of muscle molecular responses should not be used as a proxy to evaluate the magnitude of the postprandial anabolic response to feeding."


But, as I noted in my post above, they didn't muscle MUSCLE Protein breakdown, but measured at the whole body level:

"The postprandial increase in plasma amino acid availability has a negligible impact on whole-body protein breakdown or postprandial amino acid oxidation rates. "

-S
 
You mention "PTOR" - do you mean mTOR?


If you read the actual study, you'll see (Figure 5) they measured just about everything possible wrt. signaling, including mTOR1 and gene expression (mRNA) related to muscle growth:

Figure 5. Dissociation between feeding-induced muscle anabolic signaling and protein translation
(A–J) Skeletal muscle phosphorylation status (ratio of phosphorylated to total protein) of mTOR (Ser2448) (A); p70S6K (Thr389) (B); p70S6K (Thr421/Ser424) (C); rpS6
(Ser235/Ser236) (D); 4E-BP1 (Thr37/Thr46) (E); and ACC (Ser79) (H) and protein content of Beclin (F), LC3b (G), Atg 12, (I), and myostatin (J) were all measured by the
western blot technique.
(K–X) Skeletal muscle relative mRNA expression (relative to 18S housekeeping gene) of mTOR (K), p70S6K (L), FOXO1 (M), MurF1 (N), MAFBx (O), PGC1-alpha
(P), myostatin (Q), Beclin1 (R), cATG12 (S), LC3b (T), LAT1SLC (U), SNAT2 (V), CD98 (W), and PAT1 (X) were all measured by real-time qPCR quantification.

And they explain:

"In contrast, we did not observe any impact of protein feeding on muscle protein signaling or muscle gene expression (Figure 5). This is in line with previous work that suggests that the molecular response in skeletal muscle to protein ingestion is short lived (<4 h).16,37 Here, we extend these data by demonstrating that the muscle anabolic response to protein ingestion is sustained well beyond (R12 h) the frequently reported transient changes in molecular signaling. Collectively, these data suggest substantial divergence in the time course of the molecular response and the actual metabolic response to feeding (Figure 5Y). Therefore, the magnitude and/or time course of muscle molecular responses should not be used as a proxy to evaluate the magnitude of the postprandial anabolic response to feeding."


But, as I noted in my post above, they didn't muscle MUSCLE Protein breakdown, but measured at the whole body level:

"The postprandial increase in plasma amino acid availability has a negligible impact on whole-body protein breakdown or postprandial amino acid oxidation rates. "

-S
The bold part is what I'm trying to say. We all know if we ate a shit lot of protein as bodybuilders, the body could only build so much muscle tissue. That's why it's very hard even for AAS, Inulin and GH users to put massive amounts of muscle even in a year. Granted we need the amino acids to build muscle, but the body eventually can build a certain amount per hour. Building new muscle tissue is a very slow process even if we over supply the amino acid amounts available.

I personally think consuming small amounts of protien through out the day with BCAA during or immediately after the workout and taking insulin with every meal on workout days is a better approach for utilizing the protein we ingest.
 
The bold part is what I'm trying to say. We all know if we ate a shit lot of protein as bodybuilders, the body could only build so much muscle tissue. That's why it's very hard even for AAS, Inulin and GH users to put massive amounts of muscle even in a year. Granted we need the amino acids to build muscle, but the body eventually can build a certain amount per hour. Building new muscle tissue is a very slow process even if we over supply the amino acid amounts available.

I personally think consuming small amounts of protien through out the day with BCAA during or immediately after the workout and taking insulin with every meal on workout days is a better approach for utilizing the protein we ingest.
True, but the more mass you have the higher your protein requirement is. You're fighting protein turnover along with trying to add new tissue.
 

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