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x30001
Kraken
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- Jan 9, 2019
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Okay so we know that it is impossible to build muscle and burn fat at the same time without spinning your wheels and without the use of PEDs. Exceptions to this are:
It's very hard to be so precise with diet so that you gain more muscle than fat while bulking and lose less muscle than fat whilst cutting. I'm not a fan of the ketogenic diet but unfortunately I'm aware of how detrimental carbohydrates can be when it comes to fat gain whilst eating in a caloric surplus. People feel they need to eat carbs to build muscle, or to survive. That's not true, infact, carbohydrates are the only non-essential macronutrient.
Stumbling blocks whilst trying to achieve optimal body composition naturally.
- To be used as glucose to eventually create ATP for the mitochondria to be immediately used as energy.
- To refill depleted glycogen stores via glycogenesis.
- To be transported to adipose tissue (fat tissue) by insulin where the glucose will be broken down into triglycerides.
Insulin spillover occurs when you eat enough carbs so that they can be used for energy, they fully refill glycogen stores in every skeletal muscle tissue and your liver, so any more carbs you eat will result in insulin transporting the glucose to adipose tissue. As you can tell, this is bad. Insulin spillover is usually a stumbling block for those trying to "bulk". Ditch the mass gainers and all the white rolls and be more intricate with what types of food you consume. You are still dieting when bulking. You have to be meticulous if you want the best possible outcome.
Insulin resistance usually happens with high carbohydrate consumption while eating in a caloric deficit. Your body is in an energy deficit and is in a catabolic state more often than it's used to. Your body becomes more sensitive to carbohydrate consumption by it's insulinogenic response to them. ie: you will need far less carbs to refill glycogen stores whilst in an energy deficit, even though your stores will be more depleted than if you weren't in an energy deficit. The body takes on this adaptogenic response and uses carbs for the creation of immediate energy and for glycogen, but is extremely receptive due to the catabolic state of your body. Any excess carbohydrate consumption will insulin resistance. Since you're eating in a caloric deficit, the body has no need to transport glucose to adipose tissue as it is not trying to store fat, it's trying to burn it through other processes I won't get into right now. Insulin spillover and insulin resistance are huge hindrances. Some ways of preventing insulin resistance are.
So. How the fuck do you selectively promote anabolism in skeletal muscle whilst simultaneously promoting catabolic process in other areas (such as fat burning) whilst ensuring you won't cause catabolism in skeletal muscle.
Well: Insulin and 2 amino acids hold the answer.
What you must do is fast. Stop eating and promote catabolism throughout your body. Here's how insulin is released. When you eat food (carbs: direct breakdown into glucose. protein: converted to glucose through gluconeogenis), your body stores glucose in your blood. Insulin and Glucagon are two hormones that act as monitors. When your blood sugar is high, insulin reduces your blood sugar by transporting the glucose out of your blood stream. When your blood sugar is too low, Glucagon increases your blood sugar by transporting glucose into your bloodstream. The real sensor are the beta cells in the 'Islet of Langerhans' in your pancreas. These cells secrete insulin when it detects high blood sugar, or even just when it needs to regulate blood sugar and distribute glucose and transport it to other areas rather than just letting glucose accumulate in the bloodstream. So, now you already know the 3 things glucose can do for you. We know insulin acts as a transporter (I think it uses a transporter called GLUT4 but don't quote me on it), but what does the insulin itself do, does it just disappear? The answer is no. Insulin is the primary activator of anabolic pathways in the body, promoting cellular growth, tumor growth, all sorts of cellular growth. Insulin starts everything off, it can't be selective to any type of anabolism. So insulin itself binds to "Insulin receptors", it attaches to the alpha cells and the beta cells in the receptors "autophosphorylate" the insulin since there's already kinase activity in those cells. The insulin is phosphoralated on tyrosine residues and the result is called IRS. IRS (Insulin Receptor Substrate) has many isoforms, but all isoforms of IRS still lead to the activation of the same growth pathways, the PI3K/AKT/mTOR pathways. So, insulin itself has this unique anabolic role and this is why you always hear that it's the most anabolic hormone... because it is! Many of you may have thought that it's main role in "ballooning" muscles was by being an important signalling hub for glycogen synthesis. But muscles can only hold so much water and glycogen. And "storage" is not the same as anabolism or hypertrophy. Insulin is an anabolic hormone and a storage hormone. So, once we have IRS, we immediately activate P85 and PI3K, precursors of many more pathways. PI3K converts PIP2 to PIP3. PIP3 recruits PDK1 which phosphoralates to AKT (AKT and PKB/Protein Kinase B are the same). It's easier to say that insulin activates the AKT pathway, but I deliberately included every single prior pathway because it will be important later. Okay so here's how AKT activation leads to eventual protein synthesis (and many many other anabolic processes which I don't have time to mention in this thread). AKT inhibits TSC2 (Tubleris Sclerosis complex 2). With that inhibited, it's unable to inhibit RHEB (Ras homolog enriched in brain). RHEB is attached to the Ras lysosome in which RAG and Ragulator are also attached to. Activation of the Ras lysosome leads to activation of a whole new pathway called mTORC1 (mammalian Target of Rapamycin Complex 1) mTORC1 phosphoralates into p70s6k which is an extremely important signalling hub for protein synthesis. Pyrimidine synthesis is achieved through phosphorylation to CAD which is a required enzyme in pyrimidine synthesis. Skeletal muscle protein synthesis occurs upon phosphorylation of ribosomal protein S6. S6 being the ultimate substrate of p70s6k. p70s6k also phosphoralates to eEF2K which phosphoralates into eEF2 (eukaryotic Elongation Factor 2) and eIF4B (eukaryotic Initiation Factor 4 B) which phosphorlate to protein S6 which is synthesized in the ribosome of skeletal muscle tissue.
Okay, so is it possible to selectively activate the p70s6k protein without activating AKT or even PI3K in the first place? The answer is maybe. CASTOR1 and Sestrin2 are essentially sensors for the amino acids L-Arginine and L-leucine respectively. CASTOR1 (Cytosolic Arginine Sensor For MTORC1 Subunit 1) is a protein coding gene which is made inactive upon consumption of the amino acid "L-Arginine". The next explanation is convoluted so read carefully. My diagrams should help you understand everything that's going on a bit better. L-Arginine inhibits CASTOR1. CASTOR1 normally inhibits GATOR2, but since CASTOR1 is currently inhibited, it can't inhibit GATOR2. GATOR2 is active. GATOR2 inhibits GATOR1. Since GATOR1 is inhibited, it can't inhibit Rag. Rag is attached to mTORC1 which becomes active through a backdoor without any AKT signalling. Sestrin2 is inhibited by L-Leucine. Sestrin2 inhibits GATOR1 directly. Same result, different backdoor pathways. The problem is that even though the amino acids have no carbohydrates and no calories, they are unique nitrogen containing proteins which are capable of causing the pancreas to release insulin. L-Leucine is known to be more insulinogenic than L-Arginine. But just how insulinogenic are these amino acids? Surely consumption of them (or just L-Arginine) without food shouldn't trigger an insulin response. 2 days ago I found out that IRS has more than 1 inhibitor. Before that, I was only aware that PTEN (Phosphatase and Tensin homolog deleted from Chromasome 10) was the only IRS inhibitor, also inhibiting PIP3, so essentially blocking the anabolic signalling pathways before any pathway becomes active. 2 days ago I found out that p70s6k, the protein responsible for skeletal muscle protein synthesis, is an indirect inhibitor of IRS. It inhibits IRS through a process called negative feedback inhibition.
This leaves us with a problem;
We know that we can selectively activate p70s6k through a backdoor by L-Arginine and L-Leucine consumption and p70s6k inhibits insulin receptor substrate immediately after insulin is autophosphorlated by the insulin receptor. So what happens first? Does consumption of the amino acid(s) cause insulin to be secreted and IRS activates P85 and PI3K before p70s6k is activated so that it can inhibit IRS via negative feedback inhibition? Or does p70s6k get activated faster and can it block IRS before IRS gets the chance to activate the early-stage anabolic pathways? There's no way to know. I was thinking of maybe supplementing with metformin too which will activate AMPK, shutting off AKT, but experimenting with prescription diabeties drugs is just too dangerous.
In a fasted state we can achieve autophagy without skeletal muscle catabolism by having ULK1 active through AMPK activation / AKT shutoff and having p70s6k selectively activated through backdoor process by inhibiting GATOR1 with those 2 amino acids, activating mTORC1 only which will only promote protein synthesis in skeletal muscle and pyrimidine synthesis through the CAD enzyme.
- Noob lifters/ Beginners
- Obese/Untrained individuals
It's very hard to be so precise with diet so that you gain more muscle than fat while bulking and lose less muscle than fat whilst cutting. I'm not a fan of the ketogenic diet but unfortunately I'm aware of how detrimental carbohydrates can be when it comes to fat gain whilst eating in a caloric surplus. People feel they need to eat carbs to build muscle, or to survive. That's not true, infact, carbohydrates are the only non-essential macronutrient.
Stumbling blocks whilst trying to achieve optimal body composition naturally.
- Insulin resistance while cutting
- Insulin spillover whilst bulking
- To be used as glucose to eventually create ATP for the mitochondria to be immediately used as energy.
- To refill depleted glycogen stores via glycogenesis.
- To be transported to adipose tissue (fat tissue) by insulin where the glucose will be broken down into triglycerides.
Insulin spillover occurs when you eat enough carbs so that they can be used for energy, they fully refill glycogen stores in every skeletal muscle tissue and your liver, so any more carbs you eat will result in insulin transporting the glucose to adipose tissue. As you can tell, this is bad. Insulin spillover is usually a stumbling block for those trying to "bulk". Ditch the mass gainers and all the white rolls and be more intricate with what types of food you consume. You are still dieting when bulking. You have to be meticulous if you want the best possible outcome.
Insulin resistance usually happens with high carbohydrate consumption while eating in a caloric deficit. Your body is in an energy deficit and is in a catabolic state more often than it's used to. Your body becomes more sensitive to carbohydrate consumption by it's insulinogenic response to them. ie: you will need far less carbs to refill glycogen stores whilst in an energy deficit, even though your stores will be more depleted than if you weren't in an energy deficit. The body takes on this adaptogenic response and uses carbs for the creation of immediate energy and for glycogen, but is extremely receptive due to the catabolic state of your body. Any excess carbohydrate consumption will insulin resistance. Since you're eating in a caloric deficit, the body has no need to transport glucose to adipose tissue as it is not trying to store fat, it's trying to burn it through other processes I won't get into right now. Insulin spillover and insulin resistance are huge hindrances. Some ways of preventing insulin resistance are.
- Don't over eat carbs
- Spirulina
- Ashwagandha
- Curcumin
- Intermittent fasting
- Infrequent eating
- Lots of activity throughout the day
- HIIT
So. How the fuck do you selectively promote anabolism in skeletal muscle whilst simultaneously promoting catabolic process in other areas (such as fat burning) whilst ensuring you won't cause catabolism in skeletal muscle.
Well: Insulin and 2 amino acids hold the answer.
What you must do is fast. Stop eating and promote catabolism throughout your body. Here's how insulin is released. When you eat food (carbs: direct breakdown into glucose. protein: converted to glucose through gluconeogenis), your body stores glucose in your blood. Insulin and Glucagon are two hormones that act as monitors. When your blood sugar is high, insulin reduces your blood sugar by transporting the glucose out of your blood stream. When your blood sugar is too low, Glucagon increases your blood sugar by transporting glucose into your bloodstream. The real sensor are the beta cells in the 'Islet of Langerhans' in your pancreas. These cells secrete insulin when it detects high blood sugar, or even just when it needs to regulate blood sugar and distribute glucose and transport it to other areas rather than just letting glucose accumulate in the bloodstream. So, now you already know the 3 things glucose can do for you. We know insulin acts as a transporter (I think it uses a transporter called GLUT4 but don't quote me on it), but what does the insulin itself do, does it just disappear? The answer is no. Insulin is the primary activator of anabolic pathways in the body, promoting cellular growth, tumor growth, all sorts of cellular growth. Insulin starts everything off, it can't be selective to any type of anabolism. So insulin itself binds to "Insulin receptors", it attaches to the alpha cells and the beta cells in the receptors "autophosphorylate" the insulin since there's already kinase activity in those cells. The insulin is phosphoralated on tyrosine residues and the result is called IRS. IRS (Insulin Receptor Substrate) has many isoforms, but all isoforms of IRS still lead to the activation of the same growth pathways, the PI3K/AKT/mTOR pathways. So, insulin itself has this unique anabolic role and this is why you always hear that it's the most anabolic hormone... because it is! Many of you may have thought that it's main role in "ballooning" muscles was by being an important signalling hub for glycogen synthesis. But muscles can only hold so much water and glycogen. And "storage" is not the same as anabolism or hypertrophy. Insulin is an anabolic hormone and a storage hormone. So, once we have IRS, we immediately activate P85 and PI3K, precursors of many more pathways. PI3K converts PIP2 to PIP3. PIP3 recruits PDK1 which phosphoralates to AKT (AKT and PKB/Protein Kinase B are the same). It's easier to say that insulin activates the AKT pathway, but I deliberately included every single prior pathway because it will be important later. Okay so here's how AKT activation leads to eventual protein synthesis (and many many other anabolic processes which I don't have time to mention in this thread). AKT inhibits TSC2 (Tubleris Sclerosis complex 2). With that inhibited, it's unable to inhibit RHEB (Ras homolog enriched in brain). RHEB is attached to the Ras lysosome in which RAG and Ragulator are also attached to. Activation of the Ras lysosome leads to activation of a whole new pathway called mTORC1 (mammalian Target of Rapamycin Complex 1) mTORC1 phosphoralates into p70s6k which is an extremely important signalling hub for protein synthesis. Pyrimidine synthesis is achieved through phosphorylation to CAD which is a required enzyme in pyrimidine synthesis. Skeletal muscle protein synthesis occurs upon phosphorylation of ribosomal protein S6. S6 being the ultimate substrate of p70s6k. p70s6k also phosphoralates to eEF2K which phosphoralates into eEF2 (eukaryotic Elongation Factor 2) and eIF4B (eukaryotic Initiation Factor 4 B) which phosphorlate to protein S6 which is synthesized in the ribosome of skeletal muscle tissue.
Okay, so is it possible to selectively activate the p70s6k protein without activating AKT or even PI3K in the first place? The answer is maybe. CASTOR1 and Sestrin2 are essentially sensors for the amino acids L-Arginine and L-leucine respectively. CASTOR1 (Cytosolic Arginine Sensor For MTORC1 Subunit 1) is a protein coding gene which is made inactive upon consumption of the amino acid "L-Arginine". The next explanation is convoluted so read carefully. My diagrams should help you understand everything that's going on a bit better. L-Arginine inhibits CASTOR1. CASTOR1 normally inhibits GATOR2, but since CASTOR1 is currently inhibited, it can't inhibit GATOR2. GATOR2 is active. GATOR2 inhibits GATOR1. Since GATOR1 is inhibited, it can't inhibit Rag. Rag is attached to mTORC1 which becomes active through a backdoor without any AKT signalling. Sestrin2 is inhibited by L-Leucine. Sestrin2 inhibits GATOR1 directly. Same result, different backdoor pathways. The problem is that even though the amino acids have no carbohydrates and no calories, they are unique nitrogen containing proteins which are capable of causing the pancreas to release insulin. L-Leucine is known to be more insulinogenic than L-Arginine. But just how insulinogenic are these amino acids? Surely consumption of them (or just L-Arginine) without food shouldn't trigger an insulin response. 2 days ago I found out that IRS has more than 1 inhibitor. Before that, I was only aware that PTEN (Phosphatase and Tensin homolog deleted from Chromasome 10) was the only IRS inhibitor, also inhibiting PIP3, so essentially blocking the anabolic signalling pathways before any pathway becomes active. 2 days ago I found out that p70s6k, the protein responsible for skeletal muscle protein synthesis, is an indirect inhibitor of IRS. It inhibits IRS through a process called negative feedback inhibition.
This leaves us with a problem;
We know that we can selectively activate p70s6k through a backdoor by L-Arginine and L-Leucine consumption and p70s6k inhibits insulin receptor substrate immediately after insulin is autophosphorlated by the insulin receptor. So what happens first? Does consumption of the amino acid(s) cause insulin to be secreted and IRS activates P85 and PI3K before p70s6k is activated so that it can inhibit IRS via negative feedback inhibition? Or does p70s6k get activated faster and can it block IRS before IRS gets the chance to activate the early-stage anabolic pathways? There's no way to know. I was thinking of maybe supplementing with metformin too which will activate AMPK, shutting off AKT, but experimenting with prescription diabeties drugs is just too dangerous.
In a fasted state we can achieve autophagy without skeletal muscle catabolism by having ULK1 active through AMPK activation / AKT shutoff and having p70s6k selectively activated through backdoor process by inhibiting GATOR1 with those 2 amino acids, activating mTORC1 only which will only promote protein synthesis in skeletal muscle and pyrimidine synthesis through the CAD enzyme.
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