"Purple drank up in my cup, blowin dank up in my truck."
In the rap world, "Purple Drank" means (from UrbanDictionary.com):
"Codeine/promethazine cough syrup mixed in with some sprite. Serve it up in a white styrofoam cup with some ice and your good to go. You can mix it up with all kinds of sodas or just sip the ish . There is NO alcohol in it and its NOT Robitussin. It's thick and purple and comes only by prescription or by your local weedman. Not to be sipped by suckas!!!!!" -0
"Purple Drank, This Is What Causes Slurred Words, Down South We Know It Best, Whether You Got That Fat Ass Blunt Laced With That Purple Lean AKA Liquid Codeine, Or You Just Po'n It Up, You Bound To Feel Better, Prescription Purple Got You Feelin' The Best Of The Best Down South Reppin' 580 Got That C Across My Chest."
Another phrase for consuming Purple Drank is to "Get your lean on." Well, at Scivation, "Dat Purple Drank" and "Getting your LEAN on" have two completely different meanings.
I train at the local Gold's Gyms in Burlington and Graham, NC. The other day, I saw one fellow Getting his LEAN on and sippin' on some Purple Drank. But he wasn't intoxicated at all.
He was training and consuming what could very well be the most complete Workout Nutrition formula ever created.
I am dieting for a show right now and am severely lacking in carbs. But my workouts have not suffered and I am still getting stronger! I credit this with two things:
- Scivation Director of R&D and my diet advisor, Chuck Rudolph www.dietsbychuck.com), is a genius.
- Superior Workout Nutrition.
Let's jump into the science of Xtend and why it helps you get super lean and shredded and supports training on a low carb diet.
- Citrulline Malate
What Are Branched-Chain Amino Acids?
The BCAA's are different from the other 17 amino acids in that they are primarily metabolized in skeletal muscle (Layman, 2003) and metabolized at a much lower rate in the liver (Norton, 2005). The rate limiting enzyme in BCAA catabolism is Branched Chain Keto Acid Dehydrogenase, which is much more active in skeletal muscle than in the liver (Norton, 2005).
Point blank, exercise promotes increased BCAA oxidation (Shirmomura et al., 2004). This increased degradation of BCAA helps maintain energy homeostasis by providing carbon as a direct energy source and glucose homeostasis by providing substrates for the citric-acid cycle and gluconeogenesis.
Amino acids are categorized as glucogenic, ketogenic, or a combination of glucogenic and ketogenic. A glucogenic amino acid when metabolized gives rise to pyruvate or other TCA cycle intermediates that can be used for the production of glucose through gluconeogenesis.
A ketogenic amino acid is metabolized via the fatty acid pathway and gives rise to actyl-CoA, a fatty acid precursor. Leucine is completely ketogenic, valine is completely glucogenic, and isoleucine is both glucogenic and ketogenic. Valine and isoleucine can both be used to produce intermediates for glucose production via gluconeogenesis.
Due to leucine's metabolic properties (discussed below), increasing attention is being given to it and its metabolism. Research has shown plasma leucine levels to decrease during both aerobic and anaerobic exercise (Mero, 1999).
According to Freund and Hanani (2002), "Complete oxidation of leucine in the muscle yields more adenosine triphosphate molecules on a molar basis than complete oxidation of glucose." So leucine can provide skeletal muscle with more ATP than an equal amount of glucose, which is due to leucine being completely ketogenic and metabolized via the fatty acid pathway.
In order to meet the increased demand for BCAA during exercise the body breaks down muscle tissue to supply additional BCAA. By supplying the body exogenous BCAA during exercise, one can meet the increased demand for BCAA oxidation without breaking down muscle tissue to supply the needed BCAA.
Because BCAA serve as a "fuel" for skeletal muscle, supplementing with additional BCAA during your workout improves your performance without the added calories or insulin spike (which can lead to fat storage) caused by carbohydrates.
Leucine Stimulates Leptin Expression Through mTOR Activation In Adipocytes
Intake of leucine stimulates expression of the hormone leptin in adipocytes (the primary site of leptin secretion) through activation of the mTOR pathway (Meijer and Dubbelhuis, 2003). Leptin is a very complicated hormone; the gist of it is involved in the regulation of metabolism, body weight, and appetite.
Leptin secretion is linked with body fat levels; higher body fat is associated with higher leptin secretion and lower body fat is associated with lower leptin levels. When you diet and lose fat, the amount of leptin you secrete decreases, which makes your body "crave" food in an attempt to bring your body fat level back up to where the body is comfortable (known as the body fat "set point").
Leucine has the ability to activate leptin expression and will cause the body to think it is "fed" or receiving "adequate" calories, which will keep things running (specifically your metabolism) smoothly.
BCAA & The Glucose-Alanine Cycle
The BCAA's are involved in maintaining glucose homeostasis through the glucose-alanine cycle (see figure 1). The glucose-alanine cycle involves pyruvate (derived from glucose/glycogen) being transaminated in muscle to form alanine, with the BCAA serving as the main nitrogen source (donors) for the synthesis of alanine (Holecek, 2002).
The newly synthesized alanine is released in the blood stream and sent to the liver where it is converted into glucose through gluconeogenesis. This glucose can then be sent from the liver back to the working muscle to be used as fuel. Supplementing with BCAA allowing your body to create glucose to use for fuel without the added calories or insulin spike (which can lead to fat storage) caused by carbohydrates.
Click Image To Enlarge.
Figure 1: Interorgan Movement Of Branched-Chain Amino Acids (BCAA), ALA, Alanine; GIN, Glutamine; Glu, Glutamate; áKG, Alpha-Keto-Glutarate.
Glutamine is a glucogenic (glucose creating), nonessential amino acid that has multiple roles in the body. Glutamine is synthesized mainly in skeletal muscle and the liver and acts as a "nitrogen shuttle" between organs, a fuel for cells of the immune system and intestines, and a precursor for nucleotide synthesis (Holecek, 2002).
Glutamine is also a powerful cell volumizer (Haussinger et al. 1993). An increase in cell volume, also called cell swelling, stimulates anabolic pathways (synthesis of proteins and glycogen) and inhibits catabolic pathways (protein degradation) (Haussinger, 1993).
According to Houston (2001), "Glutamine content in skeletal muscle and other tissues appears to have a regulatory role in whole body protein synthesis." Glutamine levels inside muscle govern protein synthesis and nitrogen balance and therefore muscle growth (VanAcker et al. 1999).
Adequate glutamine concentrations are needed for optimal health and skeletal muscle hypertrophy. Therefore one would want to keep glutamine levels elevated, especially during/post exercise.
View Top Selling Glutamine Products Here.
Glutamine Metabolism & Exercise
During times of stress, such as exercise, skeletal muscle glutamine levels are depleted. This glutamine released from skeletal muscle is derived from muscle proteins, the intramuscular free amino acid pool, and newly synthesized glutamine (VanAcker, 1999). The newly synthesized glutamine is created by using BCAA's obtained from muscle protein breakdown (Holecek, 2002).
Plasma and muscle glutamine levels are decreased post workout and it can take hours before they are restored (Rowbottom, 1996). A study examining the effect of free-form glutamine and glutamine peptide ingestion on muscle glycogen resynthesis found that plasma glutamine was decreased by 20% post workout with the ingestion of glucose only (control), showed no change with ingestion of whey protein or wheat protein hydrolysate plus glucose drinks, and a 200% increase with ingestion of free-form glutamine plus glucose drink (VanHall, 2000). Free-form glutamine supplementation was needed to elevate plasma glutamine levels post workout.
In addition to restoring and elevating plasma glutamine levels, oral glutamine supplementation increases muscle glycogen storage to the same capacity as glucose (Bowtell, 1999). Glutamine can replenish glycogen levels without the added calories or insulin spike (which can lead to fat storage) caused by carbohydrates.
Mammalian Target Of Rapamycin (mTOR)
The Mammalian Target of Rapamycin (mTOR) is one of the body's protein synthesis regulators. mTOR functions as an energy sensor; it is activated when ATP levels are high and blocked when ATP levels are decreased (AMPK is activated when ATP decreases, which works antagonistically to mTOR).
The main energy-consuming process in the cell is protein synthesis. When mTOR is activated (high ATP levels sensed) protein synthesis is increased and when mTOR is suppressed (low ATP levels are sensed) protein synthesis is blunted.
MTOR activation is vital for skeletal muscle hypertrophy. Interestingly, mTOR is also a nutrient sensor of amino acid availability, specifically of leucine availability. Research has shown that regulation of mTOR by ATP and amino acids act independently through separate mechanisms (Dennis et al., 2001).
It is my belief that combining supplements that increase/elevate ATP levels with BCAA will lead to an increased activation of mTOR, and therefore protein synthesis. Our goal is to keep ATP levels elevated while working out. To do so, we must supply the needed nutrients and substrates before and after the workout to keep ATP levels elevated and our bodies primed for growth. This can be accomplished by supplementing with Citrulline Malate.
Citrulline-Malate has been shown to increase the rate of oxidative ATP production during exercise and the rate of phosphocreatine replenishment post exercise (Bendahan, 2002). Increasing the rate of ATP production during exercise would assist in allowing mTOR to be activated by the BCAA.
Figure 2 - Adapted from: Layman, DK (2003). The role of leucine in weight loss diets and glucose homeostasis. J. Nutr. 133: 261S-267S.