jimbuick
Legend
I drink tons of milk, cannot say I notice many estrogenic effects...
(Not to say this can't happen, I just haven't had any issues personally)
Insulin spike to add mass
- Thread starter ChrisW002
- Start date
I drink tons of milk, cannot say I notice many estrogenic effects...
(Not to say this can't happen, I just haven't had any issues personally)
MANotaur
Well-known member
wow....Im not really sure what to think about this....maybe I should educate everyone in here as to what insulin IS and what it DOES...then take that same information and apply it to what the OP is asking for.
In addition to its role in regulating glucose metabolism, insulin stimulates lipogenesis, diminishes lipolysis, and increases amino acid transport into cells. Insulin also modulates transcription, altering the cell content of numerous mRNAs. It stimulates growth, DNA synthesis, and cell replication, effects that it holds in common with the insulin-like growth factors (IGFs) and relaxin.
Insulin is synthesized as a preprohormone in the β-cells of the islets of Langerhans. Its signal peptide is removed in the cisternae of the endoplasmic reticulum and it is packaged into secretory vesicles in the Golgi, folded to its native structure, and locked in this conformation by the formation of 2 disulfide bonds. Specific protease activity cleaves the center third of the molecule, which dissociates as C peptide, leaving the amino terminal B peptide disulfide bonded to the carboxy terminal A peptide.
Insulin secretion from β-cells is principally regulated by plasma glucose levels. Increased uptake of glucose by pancreatic β-cells leads to a concomitant increase in metabolism. The increase in metabolism leads to an elevation in the ATP/ADP ratio. This in turn leads to the inhibition of an ATP-sensitive potassium channel (KATP channel). The net result is a depolarization of the cell leading to Ca2+ influx and insulin secretion.
The KATP channel is a complex of 8 polypeptides comprising four copies of the protein encoded by the ABCC8 (ATP-binding cassette, sub-family C, member 8) gene and four copies of the protein encoded by the KCNJ11 (potassium inwardly-rectifying channel, subfamily J, member 11) gene. The ABCC8 encoded protein is also known as the sulfonylurea receptor (SUR). The KCNJ11 encoded protein forms the core of the KATP channel and is called Kir6.2. As might be expected, the role of KATP channels in insulin secretion presents a viable therapeutic target for treating hyperglycemia due to insulin insufficiency as is typical in type 2 diabetes.
Insulin, secreted by the β-cells of the pancreas, is directly infused via the portal vein to the liver, where it exerts profound metabolic effects. These effects are the response of the activation of the insulin receptor which belongs to the class of cell surface receptors that exhibit intrinsic tyrosine kinase activity. The insulin receptor is a heterotetramer of 2 extracellular α-subunits disulfide bonded to 2 transmembrane β-subunits. With respect to hepatic glucose homeostasis, the effects of insulin receptor activation are specific phosphorylation events that lead to an increase in the storage of glucose with a concomitant decrease in hepatic glucose release to the circulation as diagrammed below (only those responses at the level of glycogen synthase and glycogen phosphorylase are represented).
Actions of insulin-insulin receptor interactions at the level of insulin receptor substrate-1 (IRS1) and activation of the kinase cascade leading to altered activities of glycogen phosphorylase and glycogen synthase. PI3K = phosphatidylinositol-3-kinase; PIP2 = phosphatidylinositol-4,5-bisphosphate; PIP3 = phosphatidylinositol-3,4,5-bisphosphate; PDK1 = PIP3-dependent protein kinase; Tsc1 and Tsc2 = Tuberous sclerosis tumor suppressors 1 (hamartin) and 2 (tuberin); Rheb = Ras homolog enriched in brain; mTOR = mammalian target of rapamycin. PKB/Akt = protein kinase B/Akt2; GSK3 = glycogen synthase kinase-3; S6K = 70kDa ribosomal protein S6 kinase, also called p70S6K. The insulin-mediated activation of mTOR also leads to changes in protein synthesis.
Insulin-insulin receptor actions on glycogen homeostasis showing the role of protein targeting glycogen (PTG) in complexing many of the enzymes and substrates together. PTG is a subunit of PP1. Also diagrammed is the response to insulin at the level of glucose transport into cells via GLUT4 translocation to the plasma membrane. GS/GP kinase = glycogen synthase: gycogen phosphorylase kinase. PP1 = protein phosphatase-1. Arrows denote either direction of flow or positive effects, T lines represent inhibitory effects.
In most nonhepatic tissues, insulin increases glucose uptake by increasing the number of plasma membrane glucose transporters: GLUTs. Glucose transporters are in a continuous state of turnover. Increases in the plasma membrane content of GLUTs stem from an increase in the rate of recruitment of the transporters into the plasma membrane, deriving from a special pool of preformed transporters localized in the cytoplasm. GLUT1 is present in most tissues, GLUT2 is found primarily in intestine, pancreatic β-cells, kidney and liver, GLUT3 is found primarily in neurons but also found in the intestine, GLUT4 is found in insulin-responsive tissues such as heart, adipose tissue and skeletal muscle and GLUT5 is expressed in intestine, kidney, testes, skeletal muscle, adipose tissue and brain.
In liver glucose uptake is dramatically increased because of increased activity of the enzymes glucokinase, phosphofructokinase-1 (PFK-1), and pyruvate kinase (PK), the key regulatory enzymes of glycolysis. The latter effects are induced by insulin-dependent activation of phosphodiesterase, with decreased PKA activity and diminished phosphorylation of pyruvate kinase and phosphofructokinase-2, PFK-2. Dephosphorylation of pyruvate kinase increases its' activity while dephosphorylation of PFK-2 renders it active as a kinase. The kinase activity of PFK-2 converts fructose-6-phosphate into fructose-2,6-bisphosphate (F2,6BP). F2,6BP is a potent allosteric activator of the rate limiting enzyme of glycolysis, PFK-1, and an inhibitor of the gluconeogenic enzyme, fructose-1,6-bisphosphatase. In addition, phosphatases specific for the phosphorylated forms of the glycolytic enzymes increase in activity under the influence of insulin. All these events lead to conversion of the glycolytic enzymes to their active forms and consequently a significant increase in glycolysis. In addition, glucose-6-phosphatase activity is down-regulated. The net effect is an increase in the content of hepatocyte glucose and its phosphorylated derivatives, with diminished blood glucose.
In addition to the above described events,a diminished cAMP and elevated protein phosphatase activity combine to convert glycogen phosphorylase to its inactive form and glycogen synthase to its active form, with the result that not only is glucose funneled to glycolytic products, but glycogen content is increased as well.
he role of insulin in the stimulation of protein synthesis occurs at the level of translational initiation and elongation and is exerted primarily via a cascade leading to the activation of mammalian target of rapamycin, mTOR, a protein with homology to a family of proteins first identified in yeast that bind to the immunosuppressant drug, rapamycin. Rapamycin gets its name from the fact that the compound was isolated from the bacterium Streptomyces hygroscopicus discovered on Easter Island (Rapa Nui). mTOR is a kinase whose catalytic domain shares significant homology with lipid kinases of the PI3K family.
mTOR is actually a component of two distinct multiprotein complexes termed mTORC1 and mTORC2 (mTOR complex 1 and mTOR complex 2). The activity of mTORC1 is sensitive to inhibition by by rapamycin whereas mTORC2 is not. Within the context of mTOR activity, mTORC1 is the central complex as it is responsible for integrating a diverse series of signal transduction cascades initiated by changes in both intra- and extracellular events. Activation and/or regulation of mTORC1 is involved in the control of cell proliferation, survival, metabolism and stress responses. These events can be triggered by nutrient availability, glucose, oxygen, and numerous different types of cell surface receptor activation, each of which eventually impinge on the activity of mTORC1. The components of mammalian mTORC1 include mTOR, Raptor (regulatory associated protein of TOR), Deptor (DEP domain containing mTOR-interacting protein), mLST8 (mammalian homolog of yeast LST8), and PRAS40 (proline-rich Akt/PKB substrate of 40kDa). Deptor and PRAS40 are inhibitors of mTOR activity within the complex. PRAS40 is a raptor-binding protein that is directly phosphorylated by mTOR, which then prevents PRAS40 inhibition of mTOR.
The components of mammalian mTORC2 include mTOR, Deptor, mLST8, Sin1, Poctor (protein observed with Rictor; also known as PRR5L for proline-rich 5-like protein), and Rictor (rapamycin-insensitive companion of mTOR). mTORC2 is involved in the control of the activity of serum- and glucocorticoid-induced kinase (SGK). Full activation of Akt/PKB requires the involvement of mTORC2.
In addition to its role in regulating glucose metabolism, insulin stimulates lipogenesis, diminishes lipolysis, and increases amino acid transport into cells. Insulin also modulates transcription, altering the cell content of numerous mRNAs. It stimulates growth, DNA synthesis, and cell replication, effects that it holds in common with the insulin-like growth factors (IGFs) and relaxin.
Insulin is synthesized as a preprohormone in the β-cells of the islets of Langerhans. Its signal peptide is removed in the cisternae of the endoplasmic reticulum and it is packaged into secretory vesicles in the Golgi, folded to its native structure, and locked in this conformation by the formation of 2 disulfide bonds. Specific protease activity cleaves the center third of the molecule, which dissociates as C peptide, leaving the amino terminal B peptide disulfide bonded to the carboxy terminal A peptide.
Insulin secretion from β-cells is principally regulated by plasma glucose levels. Increased uptake of glucose by pancreatic β-cells leads to a concomitant increase in metabolism. The increase in metabolism leads to an elevation in the ATP/ADP ratio. This in turn leads to the inhibition of an ATP-sensitive potassium channel (KATP channel). The net result is a depolarization of the cell leading to Ca2+ influx and insulin secretion.
The KATP channel is a complex of 8 polypeptides comprising four copies of the protein encoded by the ABCC8 (ATP-binding cassette, sub-family C, member 8) gene and four copies of the protein encoded by the KCNJ11 (potassium inwardly-rectifying channel, subfamily J, member 11) gene. The ABCC8 encoded protein is also known as the sulfonylurea receptor (SUR). The KCNJ11 encoded protein forms the core of the KATP channel and is called Kir6.2. As might be expected, the role of KATP channels in insulin secretion presents a viable therapeutic target for treating hyperglycemia due to insulin insufficiency as is typical in type 2 diabetes.
Insulin, secreted by the β-cells of the pancreas, is directly infused via the portal vein to the liver, where it exerts profound metabolic effects. These effects are the response of the activation of the insulin receptor which belongs to the class of cell surface receptors that exhibit intrinsic tyrosine kinase activity. The insulin receptor is a heterotetramer of 2 extracellular α-subunits disulfide bonded to 2 transmembrane β-subunits. With respect to hepatic glucose homeostasis, the effects of insulin receptor activation are specific phosphorylation events that lead to an increase in the storage of glucose with a concomitant decrease in hepatic glucose release to the circulation as diagrammed below (only those responses at the level of glycogen synthase and glycogen phosphorylase are represented).
Actions of insulin-insulin receptor interactions at the level of insulin receptor substrate-1 (IRS1) and activation of the kinase cascade leading to altered activities of glycogen phosphorylase and glycogen synthase. PI3K = phosphatidylinositol-3-kinase; PIP2 = phosphatidylinositol-4,5-bisphosphate; PIP3 = phosphatidylinositol-3,4,5-bisphosphate; PDK1 = PIP3-dependent protein kinase; Tsc1 and Tsc2 = Tuberous sclerosis tumor suppressors 1 (hamartin) and 2 (tuberin); Rheb = Ras homolog enriched in brain; mTOR = mammalian target of rapamycin. PKB/Akt = protein kinase B/Akt2; GSK3 = glycogen synthase kinase-3; S6K = 70kDa ribosomal protein S6 kinase, also called p70S6K. The insulin-mediated activation of mTOR also leads to changes in protein synthesis.
Insulin-insulin receptor actions on glycogen homeostasis showing the role of protein targeting glycogen (PTG) in complexing many of the enzymes and substrates together. PTG is a subunit of PP1. Also diagrammed is the response to insulin at the level of glucose transport into cells via GLUT4 translocation to the plasma membrane. GS/GP kinase = glycogen synthase: gycogen phosphorylase kinase. PP1 = protein phosphatase-1. Arrows denote either direction of flow or positive effects, T lines represent inhibitory effects.
In most nonhepatic tissues, insulin increases glucose uptake by increasing the number of plasma membrane glucose transporters: GLUTs. Glucose transporters are in a continuous state of turnover. Increases in the plasma membrane content of GLUTs stem from an increase in the rate of recruitment of the transporters into the plasma membrane, deriving from a special pool of preformed transporters localized in the cytoplasm. GLUT1 is present in most tissues, GLUT2 is found primarily in intestine, pancreatic β-cells, kidney and liver, GLUT3 is found primarily in neurons but also found in the intestine, GLUT4 is found in insulin-responsive tissues such as heart, adipose tissue and skeletal muscle and GLUT5 is expressed in intestine, kidney, testes, skeletal muscle, adipose tissue and brain.
In liver glucose uptake is dramatically increased because of increased activity of the enzymes glucokinase, phosphofructokinase-1 (PFK-1), and pyruvate kinase (PK), the key regulatory enzymes of glycolysis. The latter effects are induced by insulin-dependent activation of phosphodiesterase, with decreased PKA activity and diminished phosphorylation of pyruvate kinase and phosphofructokinase-2, PFK-2. Dephosphorylation of pyruvate kinase increases its' activity while dephosphorylation of PFK-2 renders it active as a kinase. The kinase activity of PFK-2 converts fructose-6-phosphate into fructose-2,6-bisphosphate (F2,6BP). F2,6BP is a potent allosteric activator of the rate limiting enzyme of glycolysis, PFK-1, and an inhibitor of the gluconeogenic enzyme, fructose-1,6-bisphosphatase. In addition, phosphatases specific for the phosphorylated forms of the glycolytic enzymes increase in activity under the influence of insulin. All these events lead to conversion of the glycolytic enzymes to their active forms and consequently a significant increase in glycolysis. In addition, glucose-6-phosphatase activity is down-regulated. The net effect is an increase in the content of hepatocyte glucose and its phosphorylated derivatives, with diminished blood glucose.
In addition to the above described events,a diminished cAMP and elevated protein phosphatase activity combine to convert glycogen phosphorylase to its inactive form and glycogen synthase to its active form, with the result that not only is glucose funneled to glycolytic products, but glycogen content is increased as well.
he role of insulin in the stimulation of protein synthesis occurs at the level of translational initiation and elongation and is exerted primarily via a cascade leading to the activation of mammalian target of rapamycin, mTOR, a protein with homology to a family of proteins first identified in yeast that bind to the immunosuppressant drug, rapamycin. Rapamycin gets its name from the fact that the compound was isolated from the bacterium Streptomyces hygroscopicus discovered on Easter Island (Rapa Nui). mTOR is a kinase whose catalytic domain shares significant homology with lipid kinases of the PI3K family.
mTOR is actually a component of two distinct multiprotein complexes termed mTORC1 and mTORC2 (mTOR complex 1 and mTOR complex 2). The activity of mTORC1 is sensitive to inhibition by by rapamycin whereas mTORC2 is not. Within the context of mTOR activity, mTORC1 is the central complex as it is responsible for integrating a diverse series of signal transduction cascades initiated by changes in both intra- and extracellular events. Activation and/or regulation of mTORC1 is involved in the control of cell proliferation, survival, metabolism and stress responses. These events can be triggered by nutrient availability, glucose, oxygen, and numerous different types of cell surface receptor activation, each of which eventually impinge on the activity of mTORC1. The components of mammalian mTORC1 include mTOR, Raptor (regulatory associated protein of TOR), Deptor (DEP domain containing mTOR-interacting protein), mLST8 (mammalian homolog of yeast LST8), and PRAS40 (proline-rich Akt/PKB substrate of 40kDa). Deptor and PRAS40 are inhibitors of mTOR activity within the complex. PRAS40 is a raptor-binding protein that is directly phosphorylated by mTOR, which then prevents PRAS40 inhibition of mTOR.
The components of mammalian mTORC2 include mTOR, Deptor, mLST8, Sin1, Poctor (protein observed with Rictor; also known as PRR5L for proline-rich 5-like protein), and Rictor (rapamycin-insensitive companion of mTOR). mTORC2 is involved in the control of the activity of serum- and glucocorticoid-induced kinase (SGK). Full activation of Akt/PKB requires the involvement of mTORC2.
MANotaur
Well-known member
That is insulin in a nutshell....hope that helps cause it just took me nearly a fuggin hour to SCIENTIFICALLY straighten this nonsense out.
now in English for those of you who are semi-scientific literature illiterate.
Insulin is a hormone that serves two primary functions - 1. regulate blood glucose levels. and 2. shuttle nutrients into intended target cells.
This means that yes, a "spike" of insulin is beneficial to muscle hypertrophy and repair. It helps initiate the mTOR pathway and literally force feeds nutrients into the muscle cells. by nutrients I mean sugars, amino acids, and lipids. This all is very important to the repair of muscles because without insulin....our muscles couldnt repair themselves properly. bottom line. You need insulin in order to survive. and you really need insulin in order to build muscle and improve athletic performance, whether its lifting heavy ass weights or running an ultra marathon.
The best way to spike insulin short of injecting your self with 10 units of humalog, is to combine High GI (ultra fast digesting carbohydrates) carbs and a protein blend immediately (within an hour give or take) post work out in a 2:1 ratio.
is it possible to raise insulin without the use of high GI carbs, absolutely! are you going to be able to raise them to an appreciable enough level so that it can effectively do its job? no...your not. If you could, pro body builders wouldnt fool with carbs and insulin injections....
my reccomendation to the op for a post workout shake is a shake containing about 60g of carbs, i prefer waxy maize over dextrose for a number of reasons which i will not detail in this post because i am tired. and a protein mix of 20g WPI and 10g casein. or if you really wanted to get fancy you could do 10 whey hydro, 10 WPI, and 10 Casein to further extend the release of amino acids into the blood stream.
now in English for those of you who are semi-scientific literature illiterate.
Insulin is a hormone that serves two primary functions - 1. regulate blood glucose levels. and 2. shuttle nutrients into intended target cells.
This means that yes, a "spike" of insulin is beneficial to muscle hypertrophy and repair. It helps initiate the mTOR pathway and literally force feeds nutrients into the muscle cells. by nutrients I mean sugars, amino acids, and lipids. This all is very important to the repair of muscles because without insulin....our muscles couldnt repair themselves properly. bottom line. You need insulin in order to survive. and you really need insulin in order to build muscle and improve athletic performance, whether its lifting heavy ass weights or running an ultra marathon.
The best way to spike insulin short of injecting your self with 10 units of humalog, is to combine High GI (ultra fast digesting carbohydrates) carbs and a protein blend immediately (within an hour give or take) post work out in a 2:1 ratio.
is it possible to raise insulin without the use of high GI carbs, absolutely! are you going to be able to raise them to an appreciable enough level so that it can effectively do its job? no...your not. If you could, pro body builders wouldnt fool with carbs and insulin injections....
my reccomendation to the op for a post workout shake is a shake containing about 60g of carbs, i prefer waxy maize over dextrose for a number of reasons which i will not detail in this post because i am tired. and a protein mix of 20g WPI and 10g casein. or if you really wanted to get fancy you could do 10 whey hydro, 10 WPI, and 10 Casein to further extend the release of amino acids into the blood stream.
Tomahawk88
Well-known member
I commend you for your effort but you just brought a nuclear bomb to a fight against a caveman.
But ya that is the protocol I do. Except for right now I am using rilose. Dextrose doesn't sit well with everyone.
But ya that is the protocol I do. Except for right now I am using rilose. Dextrose doesn't sit well with everyone.
MANotaur
Well-known member
i just hate pointless arguments like this where people try to be scientific and fail miserably....if you really dont understand how something works or what it is....dont comment.
im not refering to you hawk, just speaking in generalities.
but lol yeah I did kinda go off on the deep end....hope it all made sense as I have been at work and at school all day and my mind is fried...im skipping chest day today...well im gonna make up for it tommrow and double up.
rilose isnt bad....but waxy maize reigns supreme as for a pwo carb IMO. dextrose is good but your right...some people cant handle it too well.
maltose is a good option too...basically any kind of "simple" sugar will get the trick done...
hell simple sucrose is a viable option...not the best choice but it will give you the desired effect if your in a bind
Tomahawk88
Well-known member
Ya that is why I dont try and be scientific. I know my limitations. Not going to be able to explain something I grasp in my own head to someone who doesnt want to listen. I was trying to be simple and to the point with the OP. Hope he at least got something out of all this.
What is the over/under % that actually read all of what you wrote? Haha
Ya I got the rilose a while back. It is easy on my stomach so I dont mind it at all and it seems to work for me. Still kind of iffy about which is best IMO. Heard good/bad about waxy maize main thing being the quality/what it is/isnt. Probably going to do a mix of WM and dextrose when rilose is out.
What are you going to double up tomorrow? My viable options for pairings with chest are shoulders, back, and biceps.
MANotaur
Well-known member
Lol dude prolly not enough
But yeah i really like wm for a number of reasons...but that's for another thread lol
And I was planning on chest and back tonight then legs tommorow cause i did bis this and shoulders yesterday
So tommorow...big ass chest day back day and prolly...glute and core???
Tomahawk88
Well-known member
MANotaur said:
Haha so maybe just a little post workout advice.
Let me know when the knowledge bomb explodes for that thread. Will give me a good excuse to use up the WM I have.
Dang I don't know if I could handle that. Been beating my muscles into submission Mountain Dog style. Considering paying the monthly dues after I do a stint on ultra low carb island. Can't imagine doing the workouts I know I would do while on an ultra low carb diet. Once I get my body fat down to something reason time to pack on the muscle and chase 700 again.
MANotaur
Well-known member
I wanna try MD ! I've heard wonderful things about it bit just haven't done it.
Right now Im doing HIT in the style mike mentzer and alternating it with yates B&G style HIT. Just kinda doin my own research to see what kind of results i can get.
Either way..Im gonna be dead tonight
ClaudioAnimal
New member
I would only spike insulin post workout. protein can do it alone but if you add high glycemic carbs into your shake it will spike insulin even more
Tomahawk88
Well-known member
MANotaur said:
I am just going off some tnation articles he wrote. Basically mashing his ideas with others. Love some of the exercises he discusses. Hard and heavy training that is going to leave you drenched in sweat. If it doesn't deplete your glycogen stores you might be a woman.
Now a bad way to train. Are you training with a partner? Could only make HIT work with a regular training partner since it requires such frequent negatives.
My PMS is cleared haha.
MANotaur
Well-known member
Yeah I've got my wife and lil bro lol. Im doing it ot of my garage so its legit. My bro knows what he's doin cause i taught him everything i know lol and my wife touch anything until i tell her. I know its not the best idea to have a woman as a spot bit you gotta make do sometimes. Lol
Im on my phone now but i got some legit input on pwo needs and utilization of wm that Im gonna shoot you as soon as Im back at a comp
MANotaur
Well-known member
TLR
Ehh?
jimbuick
Legend
MANotaur
Well-known member
Lol nice. I don't expect many people to read it. But i love the honesty! Keep it up!
jimbuick
Legend
I'll probably get around to it eventually.
I normally post from the mobile app, so essays are a pain to read.
Tomahawk88
Well-known member
MANotaur said:
Haha sounds legit. Guessing you have a decent set up in the garage. Idk if I could ever be a home gym person. I swear I love seeing some guy have his gf spot him. Most of the time it is some girl who looks like she is afraid of the non color coated dumbbells haha. Plus in the the past lifting never worked well for me. For some reason during that time I loved lying leg curls haha.
Sounds good I am always looking for info to read through. Might send you a link to comb through some stuff to get your opinion.
MANotaur
Well-known member
Sounds like a plan bro! Send away! Im always lookin for a good read!
Jiigzz
Legend
Actually, no its not. Insulin infusion post workout decrease protein degradation following resistance exercise (i.e. favourably altering net protein balance).
insulin p/wo has a net stimulatory effect upon muscle protein synthesis primarily through a reduction in muscle proteolysis. After exercise, insulin has no effect on protein synthesis however it plays a role in reducing protein degradtion (as mentioned above) and increases amino acid transport.
Jiigzz
Legend
I too can use copy and paste.. therefore it is not you who is educating me, rather some random on another website. Just saying.